Integrins as receptor targets for neurological disorders
Open accessAbstract
This review focuses on the neurobiology of integrins, pathophysiological roles of integrins in neuroplasticity and nervous system disorders, and therapeutic implications of integrins as potential drug targets and possible delivery pathways. Neuroplasticity is a central phenomenon in many neurological conditions such as seizures, trauma, and traumatic brain injury. During the course of many brain diseases, in addition to intracellular compartment changes, alterations in non-cell compartments such as extracellular matrix (ECM) are recognized as an essential process in forming and reorganizing neural connections. Integrins are heterodimeric transmembrane receptors that mediate cell-ECM and cell-cell adhesion events. Although the mechanisms of neuroplasticity remain unclear, it has been suggested that integrins undergo plasticity including clustering through interactions with ECM proteins, modulating ion channels, intracellular Ca(2+) and protein kinase signaling, and reorganization of cytoskeletal filaments. As cell surface receptors, integrins are central to the pathophysiology of many brain diseases, such as epilepsy, and are potential targets for the development of new drugs for neurological disorders.
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The integrin and Alzheimer disease-presenilin signaling pathways are well-known gene routes in the development of abnormal aggressive behaviors.
“Among the top enriched up-regulated pathways in the aggressive Lidia group, the integrin and Alzheimer disease-presenilin signaling pathways are well-known gene routes in the development of abnormal aggressive behaviors [48] (Table 3).”
From Gene expression profiles underlying aggressive behavior in the prefrontal cortex of cattle (2021) · cites this paper as [48]
Increased expression of integrins contributes to imbalanced synaptic function in specific pathological conditions, such as Alzheimer disease and schizophrenia, both often accompanied by episodic aggression and violence.
“Increased expression of integrins contributes to imbalanced synaptic function in specific pathological conditions, such as Alzheimer disease and schizophrenia, both often accompanied by episodic aggression and violence [48].”
From Gene expression profiles underlying aggressive behavior in the prefrontal cortex of cattle (2021) · cites this paper as [48]
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“…are attractive pharmacological targets for designing new therapies for brain diseases (Horwitz, 1997; Clemetson & Clemetson, 1998; Wu & Davis, 1998; Davis et al., 2001; Ross & Borg, 2001; Gall & Lynch, 2004; Jin & Varner, 2004; Lal et al., 2007; Cox et al., 2010; Millard et al., 2011; Reichardt &…”
InfluentialSelf-citationModulation of Calcium Current in Arteriolar Smooth Muscle by αvβ3 and α5β1 Integrin Ligands
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“…the maintenance of use-dependent synaptic reorganization and LTP. Hippocampal synapses are enriched in FN receptors (i.e. α5β1 integrin) that contribute importantly to the stabilization of LTP (Bahr et al., 1997; Staubli et al., 1998; Rohrbough et al., 2000; Chun et al., 2001; Kramar et al., 2002).”
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Integrins direct Src family kinases to regulate distinct phases of oligodendrocyte development
Colognato, H., Ramachandrappa, S., Olsen, I. M. L., & ffrench‐Constant, C. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404076 · Cited by 177 · cited 2× · see citing works
“…oligodendrocyte differentiation and blockage of migration, and αvβ8 promotes astrocyte migration (Fernandez-Valle et al., 1994; Milner et al., 1996; 1997; Stewart et al., 1997; Milner et al., 1999; Blaschuk et al., 2000; Dubovy et al., 2001; Colognato et al., 2004; Colognato & Tzvetanova, 2011).”
Vascular Development of the Brain Requires β8 Integrin Expression in the Neuroepithelium
Proctor, J. M., Zang, K., Wang, D., Wang, R., & Reichardt, L. F. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3467-05.2005 · Cited by 176 · see citing works
Integrins as Unique Receptors for Vascular Control
Martinez‐Lemus, L. A., Wu, X. Y., Wilson, E., Hill, M. A., Davis, G. E., Davis, M. J., & Meininger, G. A. (2003) · Journal of Vascular Research · doi:10.1159/000071886 · Cited by 175 · cited 4× · see citing works
“Studies of integrin-initiated intracellular signaling have shown that integrins modulate Ca and K ion channels, intracellular Ca concentrations, cellular contractile properties, protein kinase activity, and growth factor receptors (Hynes, 1992; Yip & Marsh, 1997; Porter & Hogg, 1998; Wu et al., 1998; Barouch et al., 2…”
InfluentialSelf-citationThelen, K., Kedar, V., Panicker, A. K., Schmid, R. S., Midkiff, B. R., & Maness, P. F. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04918.2002 · Cited by 174 · see citing works
Excitatory Synaptic Input to Granule Cells Increases With Time After Kainate Treatment
Wuarin, J., & Dudek, F. E. (2001) · Journal of Neurophysiology · doi:10.1152/jn.2001.85.3.1067 · Cited by 171 · cited 1× · see citing works
“…could be primary events leading to development of the epilepsy (Tauck & Nadler, 1985; Sutula et al., 1988; de Lanerolle et al., 1989; Chang et al., 1993; Wuarin & Dudek, 2001; Smith & Dudek, 2002; Lin et al., 2003; Bernard-Trifilo et al., 2005; Lin et al., 2005; Gui et al., 2006; Lin et al., 2008).”
Brown, T. (2001) · New England Journal of Medicine · Cited by 169 · see citing works
Antibody to the α4 Integrin Decreases Infarct Size in Transient Focal Cerebral Ischemia in Rats
Becker, K. J., Kindrick, D. L., Relton, J. K., Harlan, J., & Winn, R. K. (2001) · Stroke · doi:10.1161/01.str.32.1.206 · Cited by 168 · see citing works
Wu, X. Y., Davis, G. E., Meininger, G. A., Wilson, E., & Davis, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102436200 · Cited by 168 · see citing works
Self-citationBahr, B. A., Staubli, U., Xiao, P., Chun, D., Ji, Z.-X., Esteban, E. T., & Lynch, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-04-01320.1997 · Cited by 165 · see citing works
Chan, C.-S., Weeber, E. J., Zong, L., Fuchs, E., Sweatt, J. D., & Davis, R. L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4110-05.2006 · Cited by 165 · see citing works
cDNA Cloning and Chromosomal Localization of Human α11 Integrin
Velling, T., Kusche‐Gullberg, M., Sejersen, T., & Gullberg, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25735 · Cited by 161 · see citing works
Huang, Z., Shimazu, K., Woo, N. H., Zang, K., Müller, U., Lu, B., & Reichardt, L. F. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3526-06.2006 · Cited by 159 · cited 1× · see citing works
“In addition, the β1-integrin receptors and their ECM ligands (FN, LN and CN) have been implicated in the process of neurite outgrowth and LTP (Venstrom & Reichardt, 1993; Chan et al., 2003; Huang et al., 2006).”
BackgroundAdult Neuronal Regeneration Induced by Transgenic Integrin Expression
Condic, M. L. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-13-04782.2001 · Cited by 157 · cited 1× · see citing works
“Transfection of adult neuronal cells with α1-integrin results in increased neurite outgrowth on LN, while transfection with α5-integrin enhances neurite outgrowth on FN in vitro (Condic, 2001).”
Natalizumab: Targeting α4-Integrins in Multiple Sclerosis
Engelhardt, B., & Kappos, L. (2007) · Neurodegenerative Diseases · doi:10.1159/000109933 · Cited by 154 · see citing works
Synaptic and glial localization of the integrin αvβ8 in mouse and rat brain
Nishimura, S. L., Boylen, K., Einheber, S., Milner, T. A., Ramos, D. M., & Pytela, R. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00118-8 · Cited by 151 · see citing works
The oligodendrocyte precursor mitogen PDGF stimulates proliferation by activation of αvβ3 integrins
Baron, W., Shattil, S. J., & ffrench‐Constant, C. (2002) · The EMBO Journal · doi:10.1093/emboj/21.8.1957 · Cited by 147 · see citing works
Perlecan domain V is neuroprotective and proangiogenic following ischemic stroke in rodents
Lee, B., Clarke, D. N., Al-Ahmad, A. J., Kahle, M., Parham, C. L., Auckland, L. D., Shaw, C. S., Fidanboylu, M., Orr, A. W., Ogunshola, O. O., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46358 · Cited by 147 · cited 2× · see citing works
“growth factor receptors (Lee et al., 2011).”
Milner, R., Wilby, M. J., Nishimura, S. L., Boylen, K., Edwards, G. M., Fawcett, J. W., Streuli, C. H., Pytela, R., & ffrench‐Constant, C. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8547 · Cited by 139 · cited 1× · see citing works
“…astrocyte adhesion and oligodendrocyte differentiation and blockage of migration, and αvβ8 promotes astrocyte migration (Fernandez-Valle et al., 1994; Milner et al., 1996; 1997; Stewart et al., 1997; Milner et al., 1999; Blaschuk et al., 2000; Dubovy et al., 2001; Colognato et al., 2004;…”
Integrin-Mediated Regulation of Synaptic Morphology, Transmission, and Plasticity
Rohrbough, J., Grotewiel, M., Davis, R. L., & Broadie, K. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06868.2000 · Cited by 135 · cited 1× · see citing works
“…pharmacological targets for designing new therapies for brain diseases (Horwitz, 1997; Clemetson & Clemetson, 1998; Wu & Davis, 1998; Davis et al., 2001; Ross & Borg, 2001; Gall & Lynch, 2004; Jin & Varner, 2004; Lal et al., 2007; Cox et al., 2010; Millard et al., 2011; Reichardt & Prokop, 2011).”
Yamazaki, T., Koo, E. H., & Selkoe, D. J. (1997) · Europe PMC (PubMed Central) · doi:10.1523/jneurosci.17-03-01004.1997 · Cited by 133 · see citing works
Wagner, C. K., & Morrell, J. I. (1996) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19960617)370:1 · Cited by 125 · see citing works
Bernard‐Trifilo, J. A., Kramár, E. A., Torp, R., Lin, C., Pineda, E. A., LYNCH, G. S., & Gall, C. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03062.x · Cited by 120 · cited 7× · see citing works
“…could be primary events leading to development of the epilepsy (Tauck & Nadler, 1985; Sutula et al., 1988; de Lanerolle et al., 1989; Chang et al., 1993; Wuarin & Dudek, 2001; Smith & Dudek, 2002; Lin et al., 2003; Bernard-Trifilo et al., 2005; Lin et al., 2005; Gui et al., 2006; Lin et al., 2008).”
InfluentialAkiyama, H., Kawamata, T., Dedhar, S., & McGeer, P. L. (1991) · Journal of Neuroimmunology · doi:10.1016/0165-5728(91)90067-h · Cited by 120 · cited 1× · see citing works
“In addition, many senile plaques and neurofibrillary tangles in Alzheimer brain tissue are prominently stained for high level VN and VN receptor β3-integrin (Akiyama et al., 1991).”
The Nonreceptor Tyrosine Kinase Fer Mediates Cross-Talk between N-Cadherin and β1-Integrins
Arregui, C. O., Pathre, P., Lilien, J. E., & Balsamo, J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.6.1263 · Cited by 120 · cited 1× · see citing works
“A peptide that mimics the first coiledcoil domain of Fer prevents Fer accumulation in the integrin cytoplasmic domain and reverses the inhibitory effect of JMP (Arregui et al., 2000).”
BackgroundIntegrins in the development function and dysfunction of the nervous system
Clegg, D. (2003) · Frontiers in bioscience · doi:10.2741/1020 · Cited by 119 · cited 5× · see citing works
“The expression of ECM molecule tenascin-C, which could bind to α8β1, α9β1, αvβ3 and αvβ6 in nervous system (Varnum-Finney et al., 1995; Nakic et al., 1996; Shapiro et al., 1996; Clegg et al., 2003), reaches peak upregulation at 24 h after kainic acid-induced limbic seizures in the CA1 and granule cell layer of adult r…”
InfluentialOliveira‐Ferrer, L., Hauschild, J., Fiedler, W., Bokemeyer, C., Nippgen, J., Çeli̇k, İ., & Schuch, G. (2008) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-27-86 · Cited by 117 · cited 1× · see citing works
“Following cilengitide treatment, endothelial and glioma cells show disassembly of cytoskeleton and disruption of tight junction formation (Oliveira-Ferrer et al., 2008).”
Integrins mediate adhesion to agrin and modulate agrin signaling
Martin, P. T., & Sanes, J. R. (1997) · Development · doi:10.1242/dev.124.19.3909 · Cited by 117 · see citing works
Extracellular matrix in plasticity and epileptogenesis
Dityatev, A. E., & Fellin, T. (2008) · Neuron Glia Biology · doi:10.1017/s1740925x09000118 · Cited by 116 · cited 2× · see citing works
“Emerging evidence shows that integrin and ECM production are altered in physiological and pathological conditions such asmemory, tumor, Alzheimer's disease, stroke, and epilepsy (Clegg et al., 2003; Gall & Lynch, 2004; Dityatev & Fellin, 2008).”
Natalizumab and Progressive Multifocal Leukoencephalopathy
Warnke, C., Menge, T., Hartung, H., Racke, M. K., Cravens, P. D., Bennett, J. L., Frohman, E. M., Greenberg, B. M., Zamvil, S. S., Gold, R., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.161 · Cited by 115 · cited 1× · see citing works
“Wilson et al. (2008) have used polynanoparticles for the targeted delivery of rivastigmine into the rat brain to treat Alzheimer's disease.”
Yang, J., Czech, T., Felizardo, M., Baumgartner, C., & Lübec, G. (2006) · Amino Acids · doi:10.1007/s00726-005-0281-y · Cited by 113 · cited 8× · see citing works
“However, in mesial TLE patients, tubulin α-1 chain, β-tubulin, profilin II, and neuronal tropomodulin are significantly reduced, whereas ezrin and vinculin are significantly increased (Yang et al., 2006).”
InfluentialAnti‐β1 integrin antibody inhibits schwann cell meylination
Fernández‐Valle, C., Gwynn, L. A., Wood, P. M., Carbonetto, S., & Bunge, M. B. (1994) · Journal of Neurobiology · doi:10.1002/neu.480251004 · Cited by 112 · see citing works
Chun, D. E., Gall, C. M., Bi, X., & LYNCH, G. S. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00173-7 · Cited by 111 · cited 5× · see citing works
“Other than RGD, the IIICS region of FN contains a 25-amino acid sequence, including the leucine–aspartate–valine (LDV) motif that binds the α4β1 integrin (Geiger et al., 2001).”
InfluentialWaitkus-Edwards, K. R., Martinez‐Lemus, L. A., Wu, X. Y., Trzeciakowski, J. P., Davis, M. J., Davis, G. E., & Meininger, G. A. (2002) · Circulation Research · doi:10.1161/hh0402.105899 · Cited by 109 · see citing works
Self-citationMatrix Remodeling after Stroke: De Novo Expression of Matrix Proteins and Integrin Receptors
Ellison, J. A., Barone, F. C., & Feuerstein, G. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07996.x · Cited by 108 · cited 1× · see citing works
“After focal ischemic stroke, increased synthesis and release of matrix proteins osteopontin to the normal brain, and the increased expression of integrin αvβ3 indicated that osteopontin plays a novel role in glial activation, organization, and repair functions (Ellison et al., 1999).”
Horwitz, A. F. (1997) · Scientific American · doi:10.1038/scientificamerican0597-68 · Cited by 105 · cited 2× · see citing works
“Therefore, integrins as cell surface receptors are attractive pharmacological targets for designing new therapies for brain diseases (Horwitz, 1997; Clemetson & Clemetson, 1998; Wu & Davis, 1998; Davis et al., 2001; Ross & Borg, 2001; Gall & Lynch, 2004; Jin & Varner, 2004; Lal et al., 2007; Cox et al., 2010; Millard…”
Blaschuk, K., Frost, E. E., & ffrench‐Constant, C. (2000) · Development · doi:10.1242/dev.127.9.1961 · Cited by 102 · see citing works
Blood-brain barrier is impaired in the hippocampus of young adult spontaneously hypertensive rats
Ueno, M., Sakamoto, H., Tomimoto, H., Akiguchi, I., Onodera, M., Huang, C., & Kanenishi, K. (2004) · Acta Neuropathologica · doi:10.1007/s00401-004-0845-z · Cited by 100 · cited 1× · see citing works
“Antibodies against the α4-integrin subunit and a FN specific antibody also stained the taupositive plaques (i.e. neuritic-type plaques) in Alzheimer's disease and Down's syndrome, while ‘preamyloid’ plaques remained negative (Van Gool et al., 1994).”
Gui, P., Wu, X. Y., Ling, S., Stotz, S. C., Winkfein, R. J., Wilson, E., Davis, G. E., Braun, A. P., Zamponi, G. W., & Davis, M. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600433200 · Cited by 97 · see citing works
Self-citationThe α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
Matter, M. L., Zhang, Z., Nordstedt, C., & Ruoslahti, E. I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1019 · Cited by 97 · see citing works
Preciado-Patt, L., Hershkoviz, R., Fridkin, M., & Lider, O. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.3.1189 · Cited by 96 · cited 1× · see citing works
“The α4β1 and αLβ2 integrins in activated microglial cells adjacent to amyloidal plaques indicate inflammatory responses in Alzheimer disease (Preciado-Patt et al., 1996).”
Integrins Regulate NMDA Receptor-Mediated Synaptic Currents
Lin, B., Arai, A., LYNCH, G. S., & Gall, C. M. (2003) · Journal of Neurophysiology · doi:10.1152/jn.00783.2002 · Cited by 96 · see citing works
Varnum‐Finney, B., Venstrom, K., Müller, U., Kypta, R. M., Backus, C., Chiquet, M., & Reichardt, L. F. (1995) · Neuron · doi:10.1016/0896-6273(95)90268-6 · Cited by 95 · see citing works
Increased permeability of blood–brain barrier on the hippocampus of a murine model of senescence
Pelegrı́, C., Canudas, A. M., del Valle, J., Casadesús, G., Smith, M. A., Camins, A., Pallàs, M., & Vilaplana, J. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.07.002 · Cited by 93 · cited 2× · see citing works
“BBB structure could be compromised during stroke, tumor metastasis, and injury (Ueno et al., 2004; Pelegri et al., 2007; Cox et al., 2010).”
Becchetti, A., & Arcangeli, A. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6066-5_10 · Cited by 91 · cited 8× · see citing works
“Growth cone extension requires a permissive range of intracellular Ca2+ concentration, whereas the frequency of Ca2+ waves and spikes controls the rate of axonal elongation/spreading (Becchetti & Arcangeli, 2010).”
Influentialβ7 integrins contribute to demyelinating disease of the central nervous system
Kanwar, J. R., Harrison, J. E. B., Wang, D., Leung, E. Y., Müller, W., Wagner, N., & Krissansen, G. W. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(99)00245-3 · Cited by 91 · cited 1× · see citing works
“These reports concluded that α4β1, α4β7, and αEβ7 integrins may all play a contributory role in the progression of chronic forms of demyelinating disease, and together with their ligands could represent potential targets for improved treatment of some forms of multiple sclerosis (Bartt, 2006; Engelhardt & Kappos, 2008…”
BackgroundAlpha3 integrin receptors contribute to the consolidation of long-term potentiation
Kramár, E. A., Bernard, J. A., Gall, C. M., & LYNCH, G. S. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00540-1 · Cited by 91 · cited 1× · see citing works
“…the maintenance of use-dependent synaptic reorganization and LTP. Hippocampal synapses are enriched in FN receptors (i.e. α5β1 integrin) that contribute importantly to the stabilization of LTP (Bahr et al., 1997; Staubli et al., 1998; Rohrbough et al., 2000; Chun et al., 2001; Kramar et al., 2002).”
Glia unglued: How signals from the extracellular matrix regulate the development of myelinating glia
Colognato, H., & Tzvetanova, I. D. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20966 · Cited by 90 · cited 1× · see citing works
“…oligodendrocyte differentiation and blockage of migration, and αvβ8 promotes astrocyte migration (Fernandez-Valle et al., 1994; Milner et al., 1996; 1997; Stewart et al., 1997; Milner et al., 1999; Blaschuk et al., 2000; Dubovy et al., 2001; Colognato et al., 2004; Colognato & Tzvetanova, 2011).”
Conditional Disruption Of Beta 1 Integrin In Schwann Cells Impedes Interactions With Axons
Feltri, M., Porta, D., Previtali, S. C., Nodari, A., Migliavacca, B., Cassetti, A., Littlewood-Evans, A. J., Reichardt, L. F., Messing, A., Quattrini, A., et al. (2002) · Journal of the Peripheral Nervous System · doi:10.1046/j.1529-8027.2002.02026_1.x · Cited by 90 · see citing works
Laminin and α7β1 integrin regulate agrin-induced clustering of acetylcholine receptors
Burkin, D. J., Kim, J. E., Gu, M., & Kaufman, S. J. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.16.2877 · Cited by 89 · see citing works
Hendriksen, H., Datson, N. A., Ghijsen, W. E. J. M., van Vliet, E. A., Lopes, F. H. D. S., Gorter, J. A., & Vreugdenhil, E. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01778.x · Cited by 88 · cited 1× · see citing works
“Microtubule formation may contribute to synaptic remodeling, such as mossy fiber sprouting and reorganization of neural networks of kindling-induced epileptogenesis (Pollard et al., 1994; Hendriksen et al., 2001; Sato & Abe, 2001).”
Up-regulation of hippocampal metabotropic glutamate receptor 5 in temporal lobe epilepsy patients
Notenboom, R. G. E., Hampson, D. R., Jansen, G. H., van Rijen, P. C., Veelen, C. W. M. V., van Nieuwenhuizen, O., & Graan, P. N. E. D. (2005) · Brain · doi:10.1093/brain/awh673 · Cited by 87 · cited 7× · see citing works
“However, in mesial TLE patients, tubulin α-1 chain, β-tubulin, profilin II, and neuronal tropomodulin are significantly reduced, whereas ezrin and vinculin are significantly increased (Yang et al., 2006).”
InfluentialRole of the hippocampus in epilepsy
Schwartzkroin, P. A. (1994) · Hippocampus · doi:10.1002/hipo.450040302 · Cited by 86 · cited 1× · see citing works
“In temporal lobe epilepsy (TLE), the hippocampus plays a key role in epileptogenesis and epileptic seizures (Schwartzkroin, 1994; Reddy, 2010).”
Integrating bits and pieces: synapse structure and formation in Drosophila embryos
Prokop, A. (1999) · Cell and Tissue Research · doi:10.1007/s004410051345 · Cited by 82 · cited 2× · see citing works
“In this section, we will discuss recent reports on integrin role in the pathophysiology of learning and memory, and selected brain disorders.”
Burkin, D. J., Gu, M., Hodges, B. L., Campanelli, J. T., & Kaufman, S. J. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.1067 · Cited by 81 · see citing works
Hippocampal Metaplasticity Induced by Deficiency in the Extracellular Matrix Glycoprotein Tenascin-R
Bukalo, O., Schachner, M., & Dityatev, A. E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1022-07.2007 · Cited by 80 · cited 1× · see citing works
“ECM protein tenascin-R-deficient mutant mice show impaired LTP, elevated levels of excitatory synaptic transmission, and reduced levels of perisomatic inhibitory currents mediated by GABAA receptors in CA1 of the hippocampus (Bukalo et al., 2007).”
Integrin-mediated reduction in vascular smooth muscle [Ca2+]i induced by RGD-containing peptide
D’Angelo, G. D., Mogford, J. E., Davis, G. E., Davis, M. J., & Meininger, G. A. (1997) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1997.272.4.h2065 · Cited by 80 · see citing works
Fukai, F., Ohtaki, M., Fujii, N., Yajima, H., Ishii, T., Miyazaki, K., & Katayama, T. (1995) · Biochemistry · doi:10.1021/bi00036a018 · Cited by 78 · cited 2× · see citing works
“neuronal activity and vascular reactivity from tissue injury rapidlymodulate integrin signaling with consequent modulation of ion channels and activities, the generation or exposure of new integrin ligands from limited degradation of extracellular matrix through increased extracellular proteases, and/or turnover of ne…”
Seizure‐induced neurogenesis in the adult brain
Kokaia, M. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07612.x · Cited by 76 · cited 1× · see citing works
“In epileptic conditions, increased neuronal proliferation in the DGCs which are principal excitatory glutamatergic phenotype neurons, cause hypersynchronization (Kokaia, 2011).”
Localization and seizure-regulation of integrin β1 mRNA in adult rat brain
Pinkstaff, J. K., LYNCH, G. S., & Gall, C. M. (1998) · Molecular Brain Research · doi:10.1016/s0169-328x(98)00007-2 · Cited by 76 · cited 2× · see citing works
“β1-integrin mRNA levels increased first in neurons and peaked with predominant astroglial expression at 24 h after seizure (Pinkstaff et al., 1998).”
BackgroundIntegrins Modulate Fast Excitatory Transmission at Hippocampal Synapses
Kramár, E. A., Bernard, J. A., Gall, C. M., & LYNCH, G. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210225200 · Cited by 75 · cited 2× · see citing works
“…Momota et al., 1998; Wu et al., 1998; Endo et al., 1999; Davis et al., 2000; Wu et al., 2000; Davis et al., 2002; Waitkus-Edwards et al., 2002; Kramar et al., 2003; Lin et al., 2003; Martinez-Lemus et al., 2003; Bernard-Trifilo et al., 2005; Gui et al., 2006;Wu et al., 2008b; Yang et al.,…”
Correlation between reactive sprouting and microtubule protein expression in epileptic hippocampus
Pollard, H., Khrestchatisky, M., Moreau, J., Ben‐Ari, Y., & Represa, A. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90401-4 · Cited by 74 · cited 1× · see citing works
“Microtubule formation may contribute to synaptic remodeling, such as mossy fiber sprouting and reorganization of neural networks of kindling-induced epileptogenesis (Pollard et al., 1994; Hendriksen et al., 2001; Sato & Abe, 2001).”
Wu, X. Y., Sun, Z., Foskett, A. M., Trzeciakowski, J. P., Meininger, G. A., & Muthuchamy, M. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01156.2009 · Cited by 73 · cited 6× · see citing works
“Other than RGD, the IIICS region of FN contains a 25-amino acid sequence, including the leucine–aspartate–valine (LDV) motif that binds the α4β1 integrin (Geiger et al., 2001).”
InfluentialSelf-citationChen, H., McCarty, D. M., Bruce, A. T., Suzuki, K., & Suzuki, K. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990215)55:4 · Cited by 71 · see citing works
Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy
Momota, Y., Yoshida, S., Ito, J., Shibata, M. S., Kato, K., Sakurai, K., Matsumoto, K., & Shiosaka, S. (1998) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1998.00068.x · Cited by 70 · cited 2× · see citing works
“neuronal activity and vascular reactivity from tissue injury rapidlymodulate integrin signaling with consequent modulation of ion channels and activities, the generation or exposure of new integrin ligands from limited degradation of extracellular matrix through increased extracellular proteases, and/or turnover of ne…”
Testaz, S., Delannet, M., & Duband, J. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.24.4715 · Cited by 70 · see citing works
Polarized distribution of α5 integrin in dendrites of hippocampal and cortical neurons
Bi, X., LYNCH, G. S., Zhou, J., & Gall, C. M. (2001) · The Journal of Comparative Neurology · doi:10.1002/cne.1201 · Cited by 69 · cited 1× · see citing works
“tex (Bi et al., 2001).”
Strekalova, T. V., Sun, M., Sibbe, M., Evers, M. R., Dityatev, A. E., Gass, P., & Schachner, M. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2002.1172 · Cited by 69 · see citing works
Smith, B. N., & Dudek, F. E. (2002) · Journal of Neurophysiology · doi:10.1152/jn.00581.2001 · Cited by 69 · see citing works
Pietri, T., Eder, O., Breau, M. A., Topilko, P., Blanche, M., Brakebusch, C., Fässler, R., Thiery, J. P., & Dufour, S. (2004) · Development · doi:10.1242/dev.01264 · Cited by 68 · cited 1× · see citing works
“radial glial cells and Schwann cell differentiation (Forster et al., 2002; Pietri et al., 2004).”
BackgroundChang, H. P., Lindberg, F. P., Wang, H. L., Huang, A., & Lee, E. H. Y. (1999) · Learning & Memory · doi:10.1101/lm.6.5.448 · Cited by 68 · cited 2× · see citing works
“(1999); Chun et al. (2001); Moiseeva (2001); Ross and Borg (2001); Chan et al.”
Expression of Integrin-Associated Protein Gene Associated with Memory Formation in Rats
Huang, A., Wang, H. L., Tang, Y. P., & Lee, E. H. Y. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-11-04305.1998 · Cited by 66 · see citing works
Regulation of Ion Channels by Integrins
Davis, M. J., Wu, X. Y., Nurkiewicz, T. R., Kawasaki, J., Gui, P., Hill, M. A., & Wilson, E. (2002) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:36:1:41 · Cited by 64 · see citing works
Self-citationMechano-reception in osteoblast-like cells
Jones, D. B., Leivseth, G., & Tenbosch, J. (1995) · Biochemistry and Cell Biology · doi:10.1139/o95-058 · Cited by 61 · cited 2× · see citing works
“neuronal activity and vascular reactivity from tissue injury rapidlymodulate integrin signaling with consequent modulation of ion channels and activities, the generation or exposure of new integrin ligands from limited degradation of extracellular matrix through increased extracellular proteases, and/or turnover of ne…”
Wu, X. Y., Yang, Y., Gui, P., Sohma, Y., Meininger, G. A., Davis, G. E., Braun, A. P., & Davis, M. J. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.149500 · Cited by 60 · see citing works
Self-citationIntegrins, Synaptic Plasticity and Epileptogenesis
Gall, C. M., & LYNCH, G. S. (2004) · Advances in experimental medicine and biology · doi:10.1007/978-1-4757-6376-8_2 · Cited by 59 · cited 7× · see citing works
“The β1-integrin expression is reported broadly increased and have been implicated in the process of neurite outgrowth during the seizure episode (Venstrom & Reichardt, 1993; Gall & Lynch, 2004).”
InfluentialPerosa, S. R., Porcionatto, M. A., Cukiert, A., Martins, J. R. M., Passeroti, C. C., Amado, D., Matas, S. L. A., Nader, H. B., Cavalheiro, É. A., Leite, J. P., et al. (2002) · Brain Research Bulletin · doi:10.1016/s0361-9230(02)00822-5 · Cited by 58 · see citing works
Endo, A., Nagai, N., Urano, T., Takada, Y., Hashimoto, K., & Takada, A. (1999) · Neuroscience Research · doi:10.1016/s0168-0102(98)00105-9 · Cited by 57 · cited 2× · see citing works
“neuronal activity and vascular reactivity from tissue injury rapidlymodulate integrin signaling with consequent modulation of ion channels and activities, the generation or exposure of new integrin ligands from limited degradation of extracellular matrix through increased extracellular proteases, and/or turnover of ne…”
Strachan, L. R., & Condic, M. L. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405024 · Cited by 56 · see citing works
Biomarcadores en la medicina cardiovascular
Martı́n-Ventura, J. L., Blanco‐Colio, L. M., Tuñón, J., Muñoz‐García, B., Madrigal‐Matute, J., Moreno, J. A., de Céniga, M. V., & Egido, J. (2009) · Revista Española de Cardiología · doi:10.1016/s0300-8932(09)71335-1 · Cited by 55 · see citing works
Glukhova, M. A., & Koteliansky, V. (1995) · Elsevier eBooks · doi:10.1016/b978-012632310-8/50004-8 · Cited by 53 · see citing works
Meiners, S. A., & Mercado, M. L. T. (2003) · Molecular Neurobiology · doi:10.1385/mn:27:2:177 · Cited by 53 · cited 3× · see citing works
“PDGF stimulated a protein kinase C-dependent activation of αvβ3 integrin, which in turn induced oligodendrocyte proliferation via a phosphatidylinositol 3-kinase-dependent signaling pathway (Baron et al., 2002).”
Haack, H., & Hynes, R. O. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0213 · Cited by 53 · cited 3× · see citing works
“…peripheral nervous system, including failure of normal nerve arborization, delay in Schwann cell migration, survival, proliferation, and differentiation, and defective neuromuscular junction differentiation (GrausPorta et al., 2001; Haack & Hynes, 2001; Feltri et al., 2002; Pietri et al., 2004).”
Proteolysis of cell adhesion molecules by serine proteases: a role in long term potentiation?
Hoffman, K. B., Martinez, J., & LYNCH, G. S. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00906-8 · Cited by 51 · cited 5× · see citing works
“…extracellular proteases, and/or turnover of new integrins (Banes et al., 1995; Fukai et al., 1995; Jones et al., 1995; Gualandris et al., 1996; Hoffman et al., 1998a, 1998b; Momota et al., 1998; Wu et al., 1998; Endo et al., 1999; Davis et al., 2000; Wu et al., 2000; Davis et al., 2002;…”
InfluentialKawaguchi, S., & Hirano, T. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.10.012 · Cited by 51 · see citing works
Biomarkers in Cardiovascular Medicine
Martı́n-Ventura, J. L., Blanco‐Colio, L. M., Tuñón, J., Muñoz‐García, B., Madrigal‐Matute, J., Moreno, J. A., de Céniga, M. V., & Egido, J. (2009) · Revista Española de Cardiología (English Edition) · doi:10.1016/s1885-5857(09)72232-7 · Cited by 50 · cited 2× · see citing works
“…support the utility of integrin ligands as potential biomarkers for diagnosis and treatment of tumor and cardiovascular diseases (Cai et al., 2008; Martin-Ventura et al., 2009). α6β4 integrin to laminin of Schwann cells and myelin is detected in the serum of Guillain–Barre syndrome patients while…”
Marchetti, G., Escuin, S., van der Flier, A., Arcangelis, A. D., Hynes, R. O., & Georges‐Labouesse, E. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07072.x · Cited by 50 · see citing works
Treatment of refractory epilepsy with natalizumab in a patient with multiple sclerosis. Case report
Sotgiu, S., Murrighile, M. R., & Constantin, G. (2010) · BMC Neurology · doi:10.1186/1471-2377-10-84 · Cited by 49 · cited 1× · see citing works
“Some inhibitors such as HYD1 for α6β1 and ATN-161 for FN sequence to block signaling have been studied in clinical or pre-clinical trials (Cianfrocca et al., 2006; Sroka et al., 2006).”
Kassner, P. D., & Berg, D. K. (1997) · Journal of Neurobiology · doi:10.1002/(sici)1097-4695(199712)33:7 · Cited by 48 · see citing works
An Arg-Gly-Asp peptide stimulates constriction in rat afferent arteriole
Yip, K., & Marsh, D. J. (1997) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1997.273.5.f768 · Cited by 48 · cited 1× · see citing works
“…ion channels, intracellular Ca2+ concentrations, cellular contractile properties, protein kinase activity, and growth factor receptors (Hynes, 1992; Yip & Marsh, 1997; Porter & Hogg, 1998; Wu et al., 1998; Barouch et al., 2000; Chan et al., 2001; Danen & Yamada, 2001; Davis et al., 2001; Wu et…”
Yang, Y., Wu, X. Y., Gui, P., Wu, J., Sheng, J., Ling, S., Braun, A. P., Davis, G. E., & Davis, M. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.033506 · Cited by 47 · cited 1× · see citing works
“A series of observations from our previous studies show that at least 3 different integrins regulate CaL, Ca activated K channels and myogenic responses in vascular systems, and in heterologously expressed smooth muscle CaL in HEK cells through inside–out and outside–in signaling between integrin and FAC (Wu et al., 1…”
BackgroundSelf-citationHoffman, K. B., Pinkstaff, J. K., Gall, C. M., & LYNCH, G. S. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00727-6 · Cited by 47 · cited 6× · see citing works
“Data compiled from: Horwitz (1997); Clemetson and Clemetson (1998); Wu and Davis (1998); Ross and Borg (2001); Staunton et al.”
InfluentialMultiple sclerosis, natalizumab therapy, and progressive multifocal leukoencephalopathy
Bartt, R. E. (2006) · Current Opinion in Neurology · doi:10.1097/01.wco.0000236612.66839.a2 · Cited by 47 · cited 2× · see citing works
“These reports concluded that α4β1, α4β7, and αEβ7 integrins may all play a contributory role in the progression of chronic forms of demyelinating disease, and together with their ligands could represent potential targets for improved treatment of some forms of multiple sclerosis (Bartt, 2006; Engelhardt & Kappos, 2008…”
Darius, J., Meyer, F. P., Sabel, B. A., & Schröeder, U. (2000) · Journal of Pharmacy and Pharmacology · doi:10.1211/0022357001774958 · Cited by 45 · cited 2× · see citing works
“This study suggested that nanoparticles loaded with valproic acid may help to reduce the toxic side effects of valproate therapy, not by reducing the therapeutically necessary dosage but by inhibition of formation of toxic metabolites (Darius et al., 2000).”
Neuroendocrinological aspects of epilepsy: Important issues and trends in future research
Pack, A. M., Reddy, D. S., Duncan, S., & Herzog, A. G. (2011) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2011.02.009 · Cited by 44 · cited 1× · see citing works
“Integrin neurobiology may provide a novel target to develop new drug candidates as ‘anti-epileptogenic’ (Reddy, 2010; Pack et al., 2011).”
Self-citationHoffman, K. B., Larson, J., Bahr, B. A., & LYNCH, G. S. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00907-x · Cited by 44 · cited 6× · see citing works
“…extracellular proteases, and/or turnover of new integrins (Banes et al., 1995; Fukai et al., 1995; Jones et al., 1995; Gualandris et al., 1996; Hoffman et al., 1998a, 1998b; Momota et al., 1998; Wu et al., 1998; Endo et al., 1999; Davis et al., 2000; Wu et al., 2000; Davis et al., 2002;…”
InfluentialKinin B1 and B2 receptors are overexpressed in the hippocampus of humans with temporal lobe epilepsy
Perosa, S. R., Argañaraz, G. A., Goto, E. M., Costa, L. G. P., Konno, A. C., Varella, P. P. V., Santiago, J. F. C., Pesquero, J. B., Canzian, M., Amado, D., et al. (2006) · Hippocampus · doi:10.1002/hipo.20239 · Cited by 44 · see citing works
Naffah‐Mazzacoratti, M. D. G., Porcionatto, M. A., Scorza, F. A., Amado, D., Silva, R. H., Bellissimo, M. I., Nader, H. B., & Cavalheiro, É. A. (1999) · Brain Research Bulletin · doi:10.1016/s0361-9230(99)00195-1 · Cited by 41 · cited 2× · see citing works
“…and synthesis of ECM molecules (e.g. FN, reelin, and glycosaminoglycans), and activation of integrin– intracellular signaling pathways following seizure activity in the hippocampus (Hoffman et al., 1998b, 1998c; Naffah-Mazzacoratti et al., 1999; Perosa et al., 2002a, 2002b; Gong et al., 2007).”
Selective disruption by protein kinases of G-protein-mediated Ca2+ channel modulation
Shapiro, M. S., Zhou, J., & Hille, B. (1996) · Journal of Neurophysiology · doi:10.1152/jn.1996.76.1.311 · Cited by 40 · see citing works
Gall, C. M., Pinkstaff, J. K., Lauterborn, J. C., Xie, Y., & LYNCH, G. S. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00990-9 · Cited by 39 · see citing works
Targeting Integrin Structure and Function in Disease
Staunton, D. E., Lupher, M., Liddington, R., & Gallatin, W. M. (2006) · Advances in immunology · doi:10.1016/s0065-2776(06)91003-7 · Cited by 38 · cited 1× · see citing works
“…and oligodendrocyte differentiation and blockage of migration, and αvβ8 promotes astrocyte migration (Fernandez-Valle et al., 1994; Milner et al., 1996; 1997; Stewart et al., 1997; Milner et al., 1999; Blaschuk et al., 2000; Dubovy et al., 2001; Colognato et al., 2004; Colognato & Tzvetanova,…”
Fürtinger, S., Pirker, S., Czech, T., Baumgartner, C., & Sperk, G. (2003) · Neuroscience Letters · doi:10.1016/j.neulet.2003.08.046 · Cited by 38 · cited 1× · see citing works
“Aberrant expressions of neurotransmitter receptors, cytoskeletal proteins, synaptic proteins, antioxidant proteins, and MEK have been found in the hippocampus of patients with TLE (Furtinger et al., 2003; Notenboom et al., 2006; Yang et al., 2006; Perosa et al., 2007).”
BackgroundBirnbaum, G., Kotilinek, L., Schlievert, P. M., Clark, H. B., Trotter, J. L., Horváth, E., Gao, E. N., Cox, M. E., & Braun, P. E. (1996) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19960515)44:4 · Cited by 38 · see citing works
Lin, C., LYNCH, G. S., & Gall, C. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03203.x · Cited by 37 · cited 1× · see citing works
“There are several reports regarding β1-integrin family activated excitatory NMDA currents and Ca currents in neurons as discussed above (Lin et al., 2003; Bernard-Trifilo et al., 2005; Lin et al., 2005; Gui et al., 2006; Lin et al., 2008).”
BackgroundIntegrin mobilizes intracellular Ca2+ in renal vascular smooth muscle cells
Chan, W.-L., Holstein‐Rathlou, N., & Yip, K. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.280.3.c593 · Cited by 37 · see citing works
Lively, S. S., & Brown, I. R. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05696.x · Cited by 35 · see citing works
Chang, H., Ma, Y., Wan, F. J., Tsai, L. Y., Lindberg, F. P., & Lee, E. H. Y. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00478-4 · Cited by 34 · cited 1× · see citing works
“Furthermore, disruption of the integrin-associated protein produces memory deficits in mice (Huang et al., 1998; Chang et al., 1999, 2001).”
Integrins and cardiovascular disease
Clemetson, K. J., & Clemetson, J. M. (1998) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050179 · Cited by 34 · cited 2× · see citing works
“Data compiled from: Horwitz (1997); Clemetson and Clemetson (1998); Wu and Davis (1998); Ross and Borg (2001); Staunton et al.”
Integrins: Novel Therapeutic Targets for Cardiovascular Diseases
Lal, H., Guleria, R. S., Foster, D. M., Lu, G., Watson, L. E., Sanghi, S., Smith, M., & Dostal, D. E. (2007) · Cardiovascular & Hematological Agents in Medicinal Chemistry · doi:10.2174/187152507780363223 · Cited by 34 · cited 2× · see citing works
“Therefore, integrins as cell surface receptors are attractive pharmacological targets for designing new therapies for brain diseases (Horwitz, 1997; Clemetson & Clemetson, 1998; Wu & Davis, 1998; Davis et al., 2001; Ross & Borg, 2001; Gall & Lynch, 2004; Jin & Varner, 2004; Lal et al., 2007; Cox et al., 2010; Millard…”
Synthetic D-amino acid peptide inhibits tumor cell motility on laminin-5
Sroka, T. C. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl005 · Cited by 34 · see citing works
Fasen, K., Elger, C. E., & Lie, A. A. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0733-y · Cited by 33 · cited 2× · see citing works
“After pilocarpine-induced status epilepticus, strong immunoreactivity for α1-, α2-, α4-, α5-, β1-, β3-, and β4-integrins is observed in reactive astrocytes (Fasen et al., 2003).”
BackgroundPerosa, S. R., Porcionatto, M. A., Cukiert, A., Martins, J. R. M., Amado, D., Nader, H. B., Cavalheiro, É. A., Leite, J. P., & Naffah‐Mazzacoratti, M. D. G. (2002) · Epilepsia · doi:10.1046/j.1528-1157.43.s.5.30.x · Cited by 31 · cited 2× · see citing works
“The increased concentration of hyaluronic acid and chondroitin sulfate in the hippocampus of TLE patients demonstrates the importance of the matrix compounds during neosynaptogenesis, neurite outgrowth, and the mossy fiber sprouting found in temporal lobe epilepsy phenomena (Perosa et al., 2002a).”
Immunocytochemical localization of a cell adhesion molecule, integrin α5β1, in nerve growth cones
Yanagida, H., Tanaka, J., & Maruo, S. (1999) · Journal of Orthopaedic Science · doi:10.1007/s007760050116 · Cited by 30 · cited 1× · see citing works
“2) (Pinkstaff et al., 1999; Renaudin et al., 1999; Yanagida et al., 1999; Chun et al., 2001; Chan et al., 2003; Morini & Becchetti, 2010).”
Lin, C. Y., Hilgenberg, L. G. W., Smith, M. A., LYNCH, G. S., & Gall, C. M. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.01.001 · Cited by 30 · cited 3× · see citing works
“…could be primary events leading to development of the epilepsy (Tauck & Nadler, 1985; Sutula et al., 1988; de Lanerolle et al., 1989; Chang et al., 1993; Wuarin & Dudek, 2001; Smith & Dudek, 2002; Lin et al., 2003; Bernard-Trifilo et al., 2005; Lin et al., 2005; Gui et al., 2006; Lin et al., 2008).”
Association of Integrin α2 Gene Variants with Ischemic Stroke
Matarín, M., Brown, W. M., Hardy, J., Rich, S. S., Singleton, A., Brown, R. D., Brott, T. G., Worrall, B. B., Meschia, J. F., ISGS, S., et al. (2007) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600508 · Cited by 29 · cited 1× · see citing works
“Genetic variants with integrin α2-subunit have been reported to be associated with an increased risk for ischemic stroke (Matarin et al., 2008).”
BackgroundChang, F.-L. F., Hawrylak, N., & Greenough, W. T. (1993) · Brain Research · doi:10.1016/0006-8993(93)91252-n · Cited by 28 · cited 5× · see citing works
“…neurons, and could be primary events leading to development of the epilepsy (Tauck & Nadler, 1985; Sutula et al., 1988; de Lanerolle et al., 1989; Chang et al., 1993; Wuarin & Dudek, 2001; Smith & Dudek, 2002; Lin et al., 2003; Bernard-Trifilo et al., 2005; Lin et al., 2005; Gui et al., 2006;…”
InfluentialGrooms, S. Y., & Jones, L. S. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00524-7 · Cited by 28 · cited 4× · see citing works
“There is increasing evidence for a functional correlation between the localization of integrins in the hippocampus and the role that integrins may play in neuronal epileptiform activities (Chang et al., 1993; Grooms & Jones, 1997).”
InfluentialPivotal role for beta-1 integrin in neurovascular remodelling after ischemic stroke
Lathia, J. D., Chigurupati, S., Thundyil, J., Selvaraj, P., Mughal, M. R., Woodruff, T. M., Chan, S. L., Karamyan, V. T., Mattson, M. P., & Arumugam, T. V. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.10.007 · Cited by 28 · cited 1× · see citing works
“Following stroke, β1-integrin is increased in cerebral blood vessel in ipsilateral ischemic cortex, and is involved in modulating angiogenesis in ischemic stroke (Lathia et al., 2010).”
Salehi-Had, H., Roh, M., Giani, A., Hisatomi, T., Nakao, S., Kim, I. K., Gragoudas, E. S., Vavvas, D. G., Guccione, S., & Miller, J. W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018864 · Cited by 27 · see citing works
The vascular smooth muscle cell: Molecular and biological responses to the extracellular matrix
Jackson, C. L. (1995) · Academic Press eBooks · Cited by 27 · see citing works
Introduction: The role of extracellular matrix in nervous system development and maintenance
Reichardt, L. F., & Prokop, A. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20975 · Cited by 24 · cited 6× · see citing works
“…pharmacological targets for designing new therapies for brain diseases (Horwitz, 1997; Clemetson & Clemetson, 1998; Wu & Davis, 1998; Davis et al., 2001; Ross & Borg, 2001; Gall & Lynch, 2004; Jin & Varner, 2004; Lal et al., 2007; Cox et al., 2010; Millard et al., 2011; Reichardt & Prokop, 2011).”
InfluentialInvolvement of β1 integrin in βAP-induced apoptosis in human neuroblastoma cells
Bozzo, C., Lombardi, G., Santoro, C., & Canonico, P. L. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2003.09.008 · Cited by 21 · see citing works
Wu, Y., Wang, X., Mo, X., Li, J., Yuan, J., Zheng, J., Feng, Y., & Tang, M. S. (2011) · International Journal of Neuroscience · doi:10.3109/00207454.2011.558224 · Cited by 19 · see citing works
Treatment of acute coronary syndrome: Part 1: Non-ST-segment acute coronary syndrome
Trost, J. C., & Lange, R. A. (2011) · Critical Care Medicine · doi:10.1097/ccm.0b013e31821e855f · Cited by 19 · see citing works
Fibronectin increases the force production of mouse papillary muscles via α5β1 integrin
Wu, X. Y., Chakraborty, S., Heaps, C. L., Davis, M. J., Meininger, G. A., & Muthuchamy, M. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.10.003 · Cited by 17 · see citing works
Self-citationGool, D. V., Carmeliet, G., Triau, E., Cassiman, J., & Dom, R. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90241-0 · Cited by 16 · see citing works
Contraction augments L‐type Ca2+ currents in adherent guinea‐pig cardiomyocytes
Rueckschloss, U., & Isenberg, G. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2004.062604 · Cited by 14 · see citing works
Increases in mRNA levels for Tα1-tubulin in the rat kindling model of epilepsy
Sato, K., & Abe, K. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02459-3 · Cited by 11 · see citing works
Circulating fragments of myelin-associated α6β4 integrin in Guillain–Barré syndrome
Sessa, G., Nemni, R., Canal, N., & Marchisio, P. C. (1997) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00143-4 · Cited by 8 · see citing works
Integrin Receptors and Ligand-Gated Channels
Morini, R., & Becchetti, A. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6066-5_9 · Cited by 7 · cited 3× · see citing works
“2) (Pinkstaff et al., 1999; Renaudin et al., 1999; Yanagida et al., 1999; Chun et al., 2001; Chan et al., 2003; Morini & Becchetti, 2010).”
Treatment of Acute Coronary Syndromes
Tahiliani, N., Trivedi, A., & Deshmukh, H. G. (2002) · New England Journal of Medicine · doi:10.1056/nejm200201173460313 · Cited by 7 · cited 1× · see citing works
“…receptors are attractive pharmacological targets for designing new therapies for brain diseases (Horwitz, 1997; Clemetson & Clemetson, 1998; Wu & Davis, 1998; Davis et al., 2001; Ross & Borg, 2001; Gall & Lynch, 2004; Jin & Varner, 2004; Lal et al., 2007; Cox et al., 2010; Millard et al., 2011;…”
Adkisson, W. O., & Benditt, D. G. (2012) · EP Europace · doi:10.1093/europace/eus224 · Cited by 5 · see citing works
Distinct roles for astrocyte αvβ5 and αvβ8 integrins in adhesion and migration
Milner, R., Huang, X., Wu, J., Nishimura, S. L., Pytela, R., Sheppard, D., & ffrench‐Constant, C. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.23.4271 · Cited by 1 · see citing works
Nolte (2001) · doi:10.1002/1098-1136(20010101)33:1
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- Wu X Gui PC Li J Balasubramanian B Braun AP Zamponi GW 2010a Regulation of cardiac (Cav1.2a), smooth muscle (Cav1.2b) and neuronal (Cav1.2c) L-type calcium channels by alpha (5) beta (1) integrin activation Texas A&M Health Science Center Research Symposium College Station, Texas
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Ludwig, B. S., Kessler, H., Kossatz, S., & Reuning, U. (2021) · Cancers · doi:10.3390/cancers13071711 · Cited by 239 · see citing works
“Most of the eight RGD binding integrins are expressed at elevated levels in various cancer types where they contribute to crucial pathophysiological functions in cancer as well as in other diseases, such as neurological disorders [36], sepsis [37], fibrosis [38], cardiovascular diseases [39], and viral infections [40].”
BackgroundThe Concise Guide to PHARMACOLOGY 2013/14: Catalytic Receptors
Alexander, S. P. H., Benson, H. E., Faccenda, E., Pawson, A. J., Sharman, J. L., Spedding, M., Peters, J. A., Harmar, A. J., & Collaborators, C. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12449 · Cited by 220 · see citing works
Recent progress of drug nanoformulations targeting to brain
Khan, A. R., Yang, X., Fu, M., & Zhai, G. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.10.004 · Cited by 212 · see citing works
Sulfonylurea Receptor 1 in Central Nervous System Injury: A Focused Review
Simard, J. M., Woo, S. K., Schwartzbauer, G., & Gerzanich, V. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.91 · Cited by 201 · see citing works
“Mechanosensitive activation of these transcription factors likely occurs via integrins, the family of extracellular matrix receptors that has been widely implicated in a range of functions including gene expression, cell proliferation, migration and differentiation, and cell survival (Wu and Reddy, 2012).”
BackgroundYou, Y., Borgmann, K., Edara, V. V., Stacy, S., Ghorpade, A., & Ikezu, T. (2020) · Journal of Extracellular Vesicles · doi:10.1080/20013078.2019.1706801 · Cited by 176 · see citing works
“Integrins are known to control cell development, mediate cell interaction and modulate immune signalling in glial cells [29].”
BackgroundExosome-Based Delivery of miR-124 in a Huntington’s Disease Model
Lee, S.-T., Im, W., Ban, J.-J., Lee, M., Jung, K.-H., Lee, S. K., Chu, K., & Kim, M. (2017) · Journal of Movement Disorders · doi:10.14802/jmd.16054 · Cited by 164 · see citing works
You, Y., Muraoka, S., Jedrychowski, M. P., Hu, J., McQuade, A., Young‐Pearse, T. L., Aslebagh, R., Shaffer, S. A., Gygi, S. P., Blurton-Jones, M. M., et al. (2022) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12183 · Cited by 161 · see citing works
“Integrins, including ITGB1, are implicated in regulating synaptic plasticity and immune responses in neurodegenerative conditions (Wu & Reddy, 2012).”
Mechanisms of Action and Persistent Neuroplasticity by Drugs of Abuse
Korpi, E. R., den Hollander, B., Farooq, U., Vashchinkina, E., Rajkumar, R., Nutt, D. J., Hyytiä, P., & Dawe, G. S. (2015) · Pharmacological Reviews · doi:10.1124/pr.115.010967 · Cited by 148 · see citing works
“ECM plays an important role in regulating actin polymerization, spine morphology, and GluA2 subunit trafficking in culture (Wu and Reddy, 2012).”
BackgroundThe bile acid TUDCA and neurodegenerative disorders: An overview
Zangerolamo, L., Vettorazzi, J. F., Rosa, L. R. D. O., Carneiro, E. M., & Barbosa, H. C. L. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119252 · Cited by 127 · see citing works
Wiera, G., & Mozrzymas, J. W. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00427 · Cited by 117 · see citing works
“Interestingly, mossy fibers show immunoreactivity for α2-, β4- and β5-integrins (Wu and Reddy, 2012) while perisynaptic astrocyte processes in stratum lucidum contain β1integrin (Schuster et al.”
Backgroundβ1 integrin signaling promotes neuronal migration along vascular scaffolds in the post-stroke brain
Fujioka, T., Kaneko, N., Ajioka, I., Nakaguchi, K., Omata, T., Ohba, H., Fässler, R., García‐Verdugo, J. M., Sekiguchi, K., Matsukawa, N., et al. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.01.005 · Cited by 110 · see citing works
Integrin activity in neuronal connectivity
Lilja, J., & Ivaska, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.212803 · Cited by 103 · see citing works
“1) (Park and Goda, 2016; Wu and Reddy, 2012).”
The Blood–Brain Barrier and Its Intercellular Junctions in Age-Related Brain Disorders
Costea, L., Mészáros, Á., Bauer, H., Bauer, H., Traweger, A., Wilhelm, I., Farkas, A. E., & Krizbai, I. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215472 · Cited by 98 · see citing works
“Researchers have found connections between integrins and aging [65,66] and neurological disorders [67].”
BackgroundObesity-induced blood-brain barrier dysfunction: phenotypes and mechanisms
Feng, Z., Fang, C., Ma, Y., & Chang, J. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03104-9 · Cited by 104 · see citing works
“ECM receptors, such as integrins and dystroglycan, are also expressed at the brain microvasculature and mediate the connections between cellular and matrix components in physiology and disease [59–61].”
BackgroundECM receptors in neuronal structure, synaptic plasticity, and behavior
Kerrisk, M. E., Cingolani, L. A., & Koleske, A. J. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00005-0 · Cited by 90 · see citing works
“…subunits α3, α5, α8, α(V), β1, and β3 function in a variety of roles in the brain, including neuronal migration, synapse and dendrite development, morphogenesis and stability, and synaptic plasticity (Gupton and Gertler, 2010; McCarty et al., 2005; Rehberg et al., 2014; Wu and Reddy, 2012).”
Khanna, A. R., Kahle, K. T., Walcott, B. P., Gerzanich, V., & Simard, J. M. (2013) · Translational Stroke Research · doi:10.1007/s12975-013-0307-9 · Cited by 93 · see citing works
“The upregulation of SUR1 is first observed only in microvascular endothelial cells, but is eventually evident in neurons [52]; by 24 h, SUR1 is upregulated in all members of the neurogliovascular unit in the affected tissue [44].”
The fundamental unit of pain is the cell
Reichling, D. B., Green, P. G., & Levine, J. D. (2013) · Pain · doi:10.1016/j.pain.2013.05.037 · Cited by 92 · see citing works
“as from the extracellular environment into the cell [58,228,243].”
BackgroundRoles of blood-brain barrier integrins and extracellular matrix in stroke
Edwards, D. N., & Bix, G. J. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00151.2018 · Cited by 90 · see citing works
Cescon, M., Chen, P., Castagnaro, S., Gregorio, I. D., & Bonaldo, P. (2016) · Aging · doi:10.18632/aging.100924 · Cited by 85 · see citing works
“Studies on the localization of integrin subunits within brain regions reported the expression of α1, α2, α3, αv, β1 and β3 integrin chains in the cortex and hippocampus [58], where integrins were shown to be involved in dendritic spine remodeling [59], interneuron migrating trajectories [60] and in glial-mediated CNS…”
BackgroundLaminins and their receptors in the CNS
Nirwane, A. M., & Yao, Y. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12454 · Cited by 85 · see citing works
Wu, Y., Liu, W., Zhou, Y., Hilton, T., Zhao, Z., Liu, W., Wang, M., Yeon, J., Houck, K., Thiagarajan, P., et al. (2018) · Blood · doi:10.1182/blood-2018-03-841932 · Cited by 87 · see citing works
Self-citationExtracellular Vesicles Regulate Sympatho-Excitation by Nrf2 in Heart Failure
Tian, C., Gao, L., Rudebush, T., Yu, L., & Zucker, I. H. (2022) · Circulation Research · doi:10.1161/circresaha.122.320916 · Cited by 81 · see citing works
A Photoresponsive Hyaluronan Hydrogel Nanocomposite for Dynamic Macrophage Immunomodulation
Wang, H., Morales, R. T., Cui, X., Huang, J., Qian, W., Tong, J., & Chen, W. (2018) · Advanced Healthcare Materials · doi:10.1002/adhm.201801234 · Cited by 77 · see citing works
Hove, I. V., Hu, T., Beets, K., Bergen, T. V., Etienne, I., Stitt, A. W., Vermassen, E., & Feyen, J. H. M. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2021.100966 · Cited by 79 · see citing works
Gabrych, D. R., Lau, V. Z., Niwa, S., & Silverman, M. A. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00419 · Cited by 71 · see citing works
“Multiple thorough reviews exist that summarize the functions of α5β1 integrins in neurons (Clegg et al., 2003; Wu and Reddy, 2012; Frontiers in Cellular Neuroscience | www.frontiersin.org 13 September 2019 | Volume 13 | Article 419 Lilja and Ivaska, 2018), therefore, we will only focus on a select…”
InfluentialMultiscale Mechanobiology in Brain Physiology and Diseases
Procès, A., Luciano, M., Kalukula, Y., Ris, L., & Gabriele, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.823857 · Cited by 68 · see citing works
Focal adhesion kinase (FAK) perspectives in mechanobiology: implications for cell behaviour
Tomakidi, P., Schulz, S., Proksch, S., Weber, W., & Steinberg, T. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1945-2 · Cited by 67 · see citing works
“fibronectin (Wu and Reddy 2012) interaction-routed focal adhesion sites, or optionally dislocated from them.”
BackgroundBerezin, V., Walmod, P. S., Filippov, M. A., & Dityatev, A. E. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00015-3 · Cited by 62 · see citing works
Cell adhesion molecules in Alzheimer's disease
Nielsen, H. M., & Wennström, M. (2012) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s19829 · Cited by 64 · see citing works
“54 Numerous studies have shown that integrins are also involved in synaptic transmission, synaptic plasticity, and LTP. 9 Therefore, it is interesting that a preclinical study demonstrated the preventative role of integrin α v on A β -induced LTP inhibition, 61 which when extrapolated, may…”
InfluentialXu, Y., Au, N. P. B., & Ma, C. H. E. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.896852 · Cited by 63 · see citing works
Milk osteopontin promotes brain development by up‐regulating osteopontin in the brain in early life
Jiang, R., Prell, C., & Lönnerdal, B. L. (2018) · The FASEB Journal · doi:10.1096/fj.201701290rr · Cited by 60 · see citing works
“It is known that OPN interacts with integrin receptors, and these receptors are found onmost CNS cell membranes (74).”
BackgroundIntegrin adhesion in brain assembly: From molecular structure to neuropsychiatric disorders
Jaudon, F., Thalhammer, A., & Cingolani, L. A. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14859 · Cited by 57 · see citing works
“Early studies indicated that the expression of various integrins and ECM proteins is up-regulated following epileptic seizures (Table 1; (Wu & Reddy, 2012).”
BackgroundInfluentialLv, X., Li, Z., Guan, J., Hu, S., Zhang, J., Lan, Y., Zhao, K., Lu, H., Song, D., He, H., et al. (2018) · Journal of Virology · doi:10.1128/jvi.01736-18 · Cited by 58 · see citing works
“The function of integrins depends on the rapid transformation of their own conformation (25, 26).”
BackgroundThe Role of Tenascin-C in Tissue Injury and Repair After Stroke
Okada, T., & Suzuki, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.607587 · Cited by 57 · see citing works
Anwar, M. M., Özkan, E., & Özdemir, Y. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15372 · Cited by 55 · see citing works
“Several treatment approaches include integrin as a direct clinical therapeutic target, modulation of integrin activity, and controlling integrin expression (Wojcik-Stanaszek et al., 2011; Wu & Reddy, 2012).”
BackgroundEberwein, P., Laird, D. F., Schulz, S., Reinhard, T., Steinberg, T., & Tomakidi, P. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.06.004 · Cited by 47 · see citing works
Layer-By-Layer: The Case for 3D Bioprinting Neurons to Create Patient-Specific Epilepsy Models
Antill‐O'Brien, N., Bourke, J., & O’Connell, C. D. (2019) · Materials · doi:10.3390/ma12193218 · Cited by 47 · see citing works
“Certainly, different integrin binding sites play an important role in multiple signalling pathways [68,69].”
BackgroundLoss of mural cell-derived laminin aggravates hemorrhagic brain injury
Gautam, J., Xu, L., Nirwane, A. M., Nguyen, B., & Yao, Y. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01788-3 · Cited by 47 · see citing works
Emerging Molecular Targets for Anti-Epileptogenic and Epilepsy Modifying Drugs
Łukasiuk, K., & Lasoń, W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032928 · Cited by 45 · see citing works
Singh, V., Erady, C., & Balasubramanian, N. (2018) · Journal of Cell Science · doi:10.1242/jcs.215855 · Cited by 45 · see citing works
“Cell-matrix adhesion is a vital regulator of many cellular processes (Berrier and Yamada, 2007; Caswell et al., 2009; Danen and Yamada, 2001) and disease conditions (Desgrosellier and Cheresh, 2010; Wu and Reddy, 2012).”
BackgroundWillis, C. L., Camire, R. B., Brule, S. A., & Ray, D. E. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.06.061 · Cited by 43 · see citing works
“Integrins are transmembrane receptors expressed on astrocytes and endothelial cells (Wu and Reddy 2012).”
BackgroundTshilenge, K., Aguirre, C. G., Bons, J., Gerencser, A. A., Basisty, N., Song, S., Rose, J., Lopez‐Ramirez, A., Naphade, S. B., Loureiro, A., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100534 · Cited by 41 · see citing works
“Dysregulation of ECM components impairs the formation and maintenance of neural circuitry and increases risk for several neurological pathologies, such as HD, AD, and autism spectrum disorder (81).”
BackgroundMolecular Profiling of the Lateral Habenula in a Rat Model of Depression
Christensen, T. T., Jensen, L., Bouzinova, E. V., & Wiborg, O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080666 · Cited by 37 · see citing works
“All three pathways mentioned in the present study: growth factor receptor signaling, Wnt signaling and integrin-mediated signaling, converge on activating the transcription factor cAMP response elementbinding protein (CREB), which is known to regulate the transcription of several genes implicated in depression patholo…”
Qu, F., Lorenzo, D. N., King, S. J., Brooks, R., Bear, J. E., & Bennett, V. (2016) · eLife · doi:10.7554/elife.20417 · Cited by 35 · see citing works
Fibrinogen Chains Intrinsic to the Brain
Golanov, E. V., Sharpe, M. A., Regnier‐Golanov, A., del Zoppo, G. J., Baskin, D. S., & Britz, G. W. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00541 · Cited by 35 · see citing works
“The important role of integrins in the regulation of extracellular matrix and synaptic activity is well-established (Wu and Reddy, 2012; Park and Goda, 2016; Lilja and Ivaska, 2018).”
BackgroundLana, D., Ugolini, F., Wenk, G. L., Giovannini, M. G., Zecchi‐Orlandini, S., & Nosi, D. (2018) · The FASEB Journal · doi:10.1096/fj.201801539r · Cited by 32 · see citing works
Mural cell-derived laminin-α5 plays a detrimental role in ischemic stroke
Nirwane, A. M., Johnson, J., Nguyen, B., Miner, J. H., & Yao, Y. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0676-8 · Cited by 34 · see citing works
Immunomodulatory role of the extracellular matrix protein tenascin-C in neuroinflammation
Wiemann, S., Reinhard, J., & Faissner, A. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190081 · Cited by 33 · see citing works
Ladiwala, U., Basu, H., & Mathur, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038613 · Cited by 33 · see citing works
Rosenfeld, C. S., Hekman, J. P., Johnson, J. L., Lyu, Z., Ortega, M. T., Joshi, T., Mao, J., Vladimirova, A. V., Gulevich, R. G., Kharlamova, A. V., et al. (2019) · Genes Brain & Behavior · doi:10.1111/gbb.12614 · Cited by 33 · see citing works
Shida, M., Mikami, T., Tamura, J.-I., & Kitagawa, H. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.06.004 · Cited by 31 · see citing works
Kim, T., Valera, E., & Desplats, P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1577-3 · Cited by 30 · see citing works
“Integrins, which mediate ECM signaling events, have been largely involved in brain plasticity and pathophysiology, including oligodendrocyte differentiation and migration [35].”
Wang, T., Peng, Q., Liu, B., Liu, Y., & Wang, Y. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00418 · Cited by 27 · see citing works
Loohuis, N. F. M. O., Kasri, N. N., Glennon, J. C., van Bokhoven, H., Hébert, S. S., Kaplan, B. B., Martens, G. J. M., & Aschrafi, A. (2016) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2016.02.009 · Cited by 29 · see citing works
“Previous research already suggested that defects in the ECMreceptor interaction and actin cytoskeleton pathways may underlie disturbances in proper memory formation (Wu and Reddy, 2012), and may be causative for ID and SZ (Dityatev et al., 2010; Evans et al., 2007).”
BackgroundInfluentialAdhering towards tumorigenicity: altered adhesion mechanisms in glioblastoma cancer stem cells
Turaga, S. M., & Lathia, J. D. (2016) · CNS Oncology · doi:10.2217/cns-2016-0015 · Cited by 29 · see citing works
LFA-1 Controls Th1 and Th17 Motility Behavior in the Inflamed Central Nervous System
Dusi, S., Angiari, S., Pietronigro, E. C., Lopez, N., Angelini, G., Zenaro, E., Bianca, V. D., Tosadori, G., Paris, F., Amoruso, A., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02436 · Cited by 30 · see citing works
“between the ECM, the intracellular cytoskeleton, and signaling pathways (63).”
BackgroundHan, C., Zhao, X., Liu, Y., Wang, K., Chen, N., Hu, W., Zhang, J., Ge, M., & Meng, F. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.10.021 · Cited by 28 · see citing works
Nanotechnology in Stroke: New Trails with Smaller Scales
Toljan, K., Ashok, A., Labhasetwar, V. D., & Hussain, M. S. (2023) · Biomedicines · doi:10.3390/biomedicines11030780 · Cited by 29 · see citing works
A guide for blood–brain barrier models
Soliman, Y., Al‐khodor, J., Koken, G. Y., & Mustafaoğlu, N. (2024) · FEBS Letters · doi:10.1002/1873-3468.15053 · Cited by 27 · see citing works
“Dystroglycan signaling can also regulate cell migration through its interaction with focal adhesion kinase (FAK) and paxillin [93].”
Endogenous Mechanisms of Neuroprotection: To Boost or Not to Be
Marmolejo-Martínez-Artesero, S., Casas, C., & Romeo-Guitart, D. (2021) · Cells · doi:10.3390/cells10020370 · Cited by 27 · see citing works
Wiernasz, E., Kaliszewska, A., Brutkowski, W., Bednarczyk, J., Gorniak, M., Kaza, B., & Łukasiuk, K. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1455-3 · Cited by 26 · see citing works
“Seizures activate integrin signaling and induce a turnover in adhesive contacts [26, 27], which hypothetically may be linked to increased Ttyh1 expression observed during epileptogenesis and epilepsy [10, 28].”
BackgroundWhat Non-neuronal Mechanisms Should Be Studied to Understand Epileptic Seizures?
Janigro, D., & Walker, M. C. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-94-017-8914-1_20 · Cited by 25 · see citing works
“Integrin expression is also increased during epileptogenesis and in pathologies associated with the development of epilepsy [87].”
BackgroundMaking tracks: microglia and the extracellular matrix
Wareham, L. K., & Calkins, D. J. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00898-x · Cited by 31 · see citing works
“The type of contact microglia make with ECM components is influenced by extracellular cytokines such as TNFα and the immune-derived interferons IFN-α and IFN-γ, which in turn upregulate the expression of ECM receptor binding proteins including integrins [183–185].”
Hlavac, N., & VandeVord, P. J. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00099 · Cited by 25 · see citing works
Mohandas, N., Loke, Y. J., Hopkins, S., Mackenzie, L., Bennett, C., Berkovic, S. F., Vadlamudi, L., & Craig, J. M. (2019) · Epigenomics · doi:10.2217/epi-2018-0136 · Cited by 24 · see citing works
Gene expression profiles underlying aggressive behavior in the prefrontal cortex of cattle
Eusebi, P. G., Sevane, N., O’Rourke, T., Pizarro, M., Boeckx, C., & Dunner, S. (2021) · BMC Genomics · doi:10.1186/s12864-021-07505-5 · Cited by 24 · see citing works
López‐Rodríguez, V., Galindo-Sarco, C. M., García-Pérez, F. O., Ferro‐Flores, G., Arrieta, O. G., & Ávila‐Rodríguez, M. A. (2015) · Journal of Nuclear Medicine · doi:10.2967/jnumed.115.161653 · Cited by 23 · see citing works
“However, other authors have reported the expression of a vast variety of integrin receptors in different structures of adult brain, including the heterodimeric αVβ3 and its subunits αV and β3, which may explain this uptake (37-39).”
BackgroundOsteopontin-metallothionein I/II interactions in experimental autoimmune encephalomyelitis.
Jakovac, H., Kezele, T. G., Šućurović, S., Mulac‐Jeričević, B., & Radošević-Stašić, B. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.03.020 · Cited by 24 · see citing works
“5A f) and that OPN activities were more related to its RGD-binding domain of OPN than to OPN-C fragment, but in spite of the fact that these findings are in line with current knowledge showing that binding of RGD fragment of many ECM proteins leads to activation and conformational change of integrin receptor and activ…”
Irisin-Associated Neuroprotective and Rehabilitative Strategies for Stroke
Huberman, M. A., d’Adesky, N., Niazi, Q. B., Pérez‐Pinzón, M. A., Bramlett, H. M., & Raval, A. P. (2021) · NeuroMolecular Medicine · doi:10.1007/s12017-021-08666-y · Cited by 23 · see citing works
“The αV/ β5 Integrin is expressed in many cells, including neuronal cells and has been a receptor target for neurological disorders for its role in neuroplasticity, cell survival, migration, and differentiation (Wu & Reddy, 2012).”
BackgroundCeruloplasmin Deamidation in Neurodegeneration: From Loss to Gain of Function
Zanardi, A., & Alessio, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020663 · Cited by 22 · see citing works
“In particular, considering that integrins recognized by isoDGR motif (such as αVβ3, αVβ5, αVβ6,αVβ8 and α5β1) [9,22,25] are widely expressed in the nervous system by both neuronal and glial cells [81], other cells out of CPEpiCs could also be targeted by the NGR-containing deamidated proteins.”
Backgroundαvβ3 Integrin Antagonists Enhance Chemotherapy Response in an Orthotopic Pancreatic Cancer Model
Coskun, M. D., Sudha, T., Bharali, D. J., Çelikler, S., Davis, P. J., & Mousa, S. A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00095 · Cited by 21 · see citing works
“, 2010), rheumatoid arthritis related diseases (Wilder, 2002), and several neurological disorders (Wu and Reddy, 2012).”
BackgroundGohel, D., Zhang, P., Gupta, A. K., Li, Y., Chiang, C., Li, L., Hou, Y., Pieper, A. A., Cummings, J. L., & Cheng, F. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231391 · Cited by 23 · see citing works
“This signaling pathway is known to have pathophysiological role in neurodevelopment, plasticity, and central nervous system (CNS) diseases [51–53].”
BackgroundIncreased expression of copine VI in patients with refractory epilepsy and a rat model
Zhu, B., Zha, J., Long, Y., Hu, X., Chen, G., & Wang, X. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2015.11.041 · Cited by 21 · see citing works
“The A domain of copines mediates protein-protein interaction [8] and is similar to the von Willebrand A (VWA) domain found in integrins that are central to the pathophysiology of many brain diseases, such as epilepsy [28].”
MethodWu, X. Y., Muthuchamy, M., & Reddy, D. S. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00088 · Cited by 20 · see citing works
“…a connection between ECM and the intracellular focal adhesion complex (FAC) molecules including non-receptor tyrosine kinases (NRTKs) focal adhesion kinase (FAK) and Src, as well as cytoskeleton proteins, including talin and actin (Wu et al., 1998, 2001; Pinkstaff et al., 1999; Wu and Reddy, 2012).”
BackgroundSelf-citationTee, J. Y., Sutharsan, R., Fan, Y., & Mackay‐Sim, A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.005 · Cited by 19 · see citing works
“All the integrin receptors detected in patient and control cells are commonly expressed by neurons and glia in the brain (Wu and Reddy, 2012), although the ECM composition of the developing and mature brain involves integrin-binding proteins (Jones et al., 2011; Katic et al., 2014), as well as…”
Kerrisk, M. E., & Koleske, A. J. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.07.018 · Cited by 19 · see citing works
Kiss, D., Ioja, E., Toth, I., Barany, Z., Jocsak, G., Bartha, T., Horvath, T., & Zsarnovszky, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051440 · Cited by 18 · see citing works
“Additionally, the observed changes in transcription and translation rates in response to ZEN treatment might be induced by certain cellular adaptations to the applied experimental conditions and by the loss of tissue integrity, such as the absence of extracellular matrix proteins, integrins, and certain glycoproteins…”
BackgroundBrzdąk, P., Lebida, K., Wyroślak, M., & Mozrzymas, J. W. (2023) · Scientific Reports · doi:10.1038/s41598-023-31882-4 · Cited by 14 · see citing works
Yu, I., Chang, H., Chen, K., Lu, Y., Shy, H.-T., Chen, C.-Y., Lee, K., & Lee, L. (2019) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2019.00016 · Cited by 15 · see citing works
“Among these CTGF-binding proteins, integrins, lowdensity lipoprotein receptor-related protein 1 (LRP1), and vascular endothelial growth factor (VEGF) are known to modulate the development of oligodendrocyte in various aspects (Wu and Reddy, 2012; Auderset et al., 2016; Safina et al., 2016).”
BackgroundWu, X. Y., Muthuchamy, M., & Reddy, D. S. (2017) · Epilepsy Research · doi:10.1016/j.eplepsyres.2017.10.013 · Cited by 16 · see citing works
Self-citationde Araújo, M. A., Marques, T. E. B. S., Octacílio-Silva, S., Silva, C. L. D. A., Pereira, M. G. A. G., Peixoto-Santos, J. E., Kandratavicius, L., Leite, J. P., Garcia‐Cairasco, N., de Castro, O. W., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163855 · Cited by 15 · see citing works
Neuroplasticidad: aspectos bioquímicos y neurofisiológicos
Garcés-Vieira, M. V., & Suárez-Escudero, J. C. (2014) · CES Medicina · Cited by 14 · see citing works
Bhuiyan, P., Sun, Z., Khan, M. A., Hossain, M. A., Rahman, M. H., & Qian, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e25191 · Cited by 14 · see citing works
“Previously, it has been reported that SZ patient-derived cells are sensitive to ECM proteins that bind integrin receptors, thus resulting in increases in focal adhesion number and size in response to ECM proteins and alterations in cell shape and cytoskeleton [55].”
BackgroundCassone, C. G., Taylor, J. J., O’Brien, J. M., Williams, A., Yauk, C. L., Crump, D., & Kennedy, S. W. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs219 · Cited by 13 · see citing works
“Integrin receptors and signaling 396 Integrins are transmembrane receptors essential to embryonic development and necessary 397 for neuronal cells to attach, spread, migrate and extend processes on extracellular matrix 398 molecules and mediate cell-cell and cell-matrix adhesion events (Wu and Reddy 2012).”
BackgroundEvolving Evidence of Calreticulin as a Pharmacological Target in Neurological Disorders
Kotian, V., Sarmah, D., Kaur, H., Kesharwani, R., Verma, G., Mounica, L., Veeresh, P., Kalia, K., Borah, A., Wang, X., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00158 · Cited by 13 · see citing works
Jackson, T. C., Gorse, K., Herrmann, J. R., & Kochanek, P. M. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02250-4 · Cited by 13 · see citing works
“There are at least 21 different integrin receptors in the brain, based on permutations in their subunit dimerization [37].”
BackgroundProteomic Response of the Brain to Hypoxic Stress in Marine Medaka Fish (Oryzias melastigma)
Lai, K. P., Tam, N. Y.-K., Wang, S. Y., Tse, W. K. F., Lin, X., Chan, T., Tong, Y., Zhang, J., Au, D. W. T., Wu, R. S. S., et al. (2021) · Frontiers in Marine Science · doi:10.3389/fmars.2021.618489 · Cited by 12 · see citing works
“Notably, aberrations in integrin signaling within the brain may impair the synaptic activity in brain disorders such as schizophrenia and epilepsy (Wu and Reddy, 2012).”
BackgroundThe Intricate Interplay: Microbial Metabolites and the Gut‐Liver‐Brain Axis in Parkinson's Disease
Kishanchand, D. K., A., A. K. K., Chandrababu, K., Philips, C. A., Sivan, U., & Chakrapani, P. S. B. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70016 · Cited by 11 · see citing works
Gong, L., Zheng, Y., Liu, S., & Peng, Z. (2018) · Europe PMC (PubMed Central) · doi:10.22034/apjcp.2018.19.9.2493 · Cited by 11 · see citing works
“…in the formed MCA may promote the formation of focal adhesion complex, through its cytoplasmic region, to activate intracellular focal adhesion kinase (FAK) activation, leading to tumor cell invasion and metastasis (Sun et al., 2014; Li et al., 2017; Kukkurainen et al., 2014; Wu and Reddy, 2012).”
BackgroundBitiktas, S., Tan, B., Kavraal, Ş., Yousef, M., Bayar, Y., Dursun, N., & Süer, C. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23985 · Cited by 11 · see citing works
Poormoghadam, D., Almasi, A., Ashrafizadeh, M., Vishkaei, A. S., Rezayat, S. M., & Tavakol, S. (2020) · Nanotechnology · doi:10.1088/1361-6528/ab8d6b · Cited by 11 · see citing works
Role of dynamin 2 in the disassembly of focal adhesions
Briñas, L., Vassilopoulos, S., Bonne, G., Guicheney, P., & Bitoun, M. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1040-2 · Cited by 11 · see citing works
“On the other hand, integrin-based adhesion sites play important roles in the regulation of cell surface receptor, neurotransmitter receptors and calcium signalling in neurons [59], several processes potentially impaired by DNM2 mutation.”
BackgroundSelective Integrin α5β1 Targeting through Spatially Constrained Multivalent DNA-Based Nanoparticles
Kurisinkal, E. E., Caroprese, V., Koga, M. M., Morzy, D., & Bastings, M. M. C. (2022) · Molecules · doi:10.3390/molecules27154968 · Cited by 10 · see citing works
“The integrin α5β1 has been implicated in several diseases, ranging from cancer, inflammation [11], respiratory diseases [12], neurological disorders [13] and viruses, including SARS-CoV-2 [14], besides being engaged in cell adhesion [15].”
BackgroundLicheri, V., & Brigman, J. L. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.753537 · Cited by 10 · see citing works
“Several integrin α and β subunits are highly expressed in growth cones and synapses (Wu and Reddy, 2012; Park and Goda, 2016), and it is well established their role in building and maintain synaptic structure during the phases of the development (Benson et al.”
BackgroundCo-Expression Analysis of microRNAs and Proteins in Brain of Alzheimer’s Disease Patients
Watson, C. N., Begum, G., Ashman, E., Thorn, D., Yakoub, K. M., Hariri, M. A., Nehme, A., Mondello, S., Kobeissy, F. H., Belli, A., et al. (2022) · Cells · doi:10.3390/cells11010163 · Cited by 12 · see citing works
“hsamiR-30e-5p and Integrin beta-1 (ITGB1), a receptor for collagen, is another interaction, and it was suggested to undergo plasticity through interactions with ECM proteins, modulating ion channels, intracellular Ca2+ and protein kinases signalling, and reorganization of cytoskeletal filaments [47].”
BackgroundEnhanced glaucomatous damage accompanied by glial response in a new multifactorial mouse model
Reinehr, S., Girbig, R. M., Schulte, K. K., Theile, J., Asaad, M. A., Fuchshofer, R., Dick, H. B., & Joachim, S. C. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1017076 · Cited by 10 · see citing works
Yasodharababu, M., & Nair, A. K. (2020) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-020-00615-2 · Cited by 10 · see citing works
Advances in Polymer Micelles for Cancer Therapy: From Conventional to Smart Delivery Systems
Bryaskova, R. G., Staykov, K., & Ganchev, D. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18020177 · Cited by 9 · see citing works
Suresh, N. T., Vimina, E. R., & Krishnakumar, U. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107323 · Cited by 9 · see citing works
Sim, H., Seo, J., Kim, J., Oh, M., Lee, J., Baek, A., Lee, S.-Y., Chung, S., Son, M., Chae, J., et al. (2020) · Life · doi:10.3390/life10120331 · Cited by 9 · see citing works
“As integrin dysfunction is involved in the pathogenesis of several disease states, many studies have targeted them for studying neurodegenerative diseases [34,35].”
Background
- Authors
- Wu, X., & Reddy, D. S.
- Affiliations
- Texas A&M Health Science Center (US)
- Corresponding author
- Reddy, Doodipala Samba
- Venue
- Pharmacology & Therapeutics
- Publisher
- Elsevier BV
- Published
- 2012-04
- Volume
- 134
- Issue
- 1
- Pages
- 68-81
- ISSN
- 0163-7258 (ISSN-L)
- PMC
- PMC3288359
- OpenAlex
- W2015445832
- Cited by
- 175
- References
- 202
- Citations by year
- 2026: 12 · 2025: 19 · 2024: 12 · 2023: 16 · 2022: 12 · 2021: 17 · 2020: 12 · 2019: 21 · 2018: 14 · 2017: 5 · 2016: 10 · 2015: 5 · 2014: 8 · 2013: 8 · 2012: 4
- FWCI
- 0.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Pharmacology & Therapeutics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS051398, NS051398)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- integrins, neuroplasticity, neurological disorders, extracellular matrix, cell-cell adhesion, cell-matrix adhesion, integrin clustering, epilepsy, traumatic brain injury, seizures, therapeutic target, drug delivery, cytoskeletal remodeling, calcium signaling, protein kinase signaling
- MeSH terms
- Animals, Brain Diseases, Humans, Integrins
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