The DOI matches its Crossref record; 150 of the 150 references it cites were found in a registry or an index.
Biological interplay between proteoglycans and their innate immune receptors in inflammation
Open accessAbstract
An emerging body of evidence indicates that secreted proteoglycans act as signaling molecules, in addition to their canonical function in maintaining and regulating the architecture of various extracellular matrices. Proteoglycans interact with a number of receptors that regulate growth, motility and immune response. In part, as a consequence of their complex structure, proteoglycans can induce crosstalk among various families of receptors and can also interact with natural receptor ligands, often blocking and sequestering their bioactivity. In their soluble form, originating from either partial proteolytic processing or through de novo synthesis by activated cells, some proteoglycans can become potent danger signals, denoting tissue stress and injury. Recently, it has been shown that proteoglycans, especially those belonging to the small leucine‐rich and hyaluronan‐binding gene families as well as the glycosaminoglycan hyaluronan, act as endogenous ligands of the toll‐like receptors, a group of central receptors regulating innate immunity. Furthermore, proteoglycans can activate intracellular inflammasomes and trigger sterile inflammation. In this review, we critically assess the signaling events induced by the proteoglycans biglycan, decorin, lumican and versican as well as hyaluronan during inflammation. We discuss the intriguing emerging notion that, in spite of structural diversity of biglycan, decorin, versican and hyaluronan, all of them signal through the same toll‐like receptors, albeit triggering differential responses and biological outcomes. Finally, we review the modes of action of these endogenous ligands of toll‐like receptors and their ability to specifically modify the final signaling events and the inflammatory response.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Pattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895
Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,083
The Extracellular Matrix: Not Just Pretty Fibrils
Hynes, R. O. (2009) · Science · doi:10.1126/science.1176009 · Cited by 3,527
Sterile inflammation: sensing and reacting to damage
Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051
MATRIX PROTEOGLYCANS: From Molecular Design to Cellular Function
Iozzo, R. V. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.609 · Cited by 1,637
Self-citationNegative regulation of transforming growth factor-β by the proteoglycan decorin
Yamaguchi, Y., Mann, D. M., & Ruoslahti, E. (1990) · Nature · doi:10.1038/346281a0 · Cited by 1,516
Signaling in innate immunity and inflammation
Newton, K., & Dixit, V. M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006049 · Cited by 1,513
Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility
Danielson, K. G., Baribault, H., Holmes, D. F., Graham, H., Kadler, K. E., & Iozzo, R. V. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.3.729 · Cited by 1,406
Self-citationRegulation of lung injury and repair by Toll-like receptors and hyaluronan
Jiang, D., Liang, J., Fan, J., Yu, S., Chen, S., Luo, Y., Prestwich, G. D., Mascarenhas, M. M., Garg, H. G., Quinn, D. A., et al. (2005) · Nature Medicine · doi:10.1038/nm1315 · Cited by 1,401
Oligosaccharides of Hyaluronan Activate Dendritic Cells via Toll-like Receptor 4
Termeer, C., Benedix, F., Sleeman, J., Fieber, C., Voith, U., Ahrens, T., Miyake, K., Freudenberg, M., Galanos, C., & Simon, J. C. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20001858 · Cited by 1,378
PAMP s and DAMP s: signal 0s that spur autophagy and immunity
Tang, D., Kang, R., Coyne, C. B., Zeh, H. J., & Lotze, M. T. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01146.x · Cited by 1,221
Carcinoma-produced factors activate myeloid cells through TLR2 to stimulate metastasis
Kim, S., Takahashi, H., Lin, W.-W., Descargues, P., Grivennikov, S., Kim, Y., Luo, J.-L., & Karin, M. (2009) · Nature · doi:10.1038/nature07623 · Cited by 1,100
Hyaluronan as an Immune Regulator in Human Diseases
Jiang, D., Liang, J., & Noble, P. W. (2011) · Physiological Reviews · doi:10.1152/physrev.00052.2009 · Cited by 1,060
Hildebrand, A., Romarís, M., Rasmussen, L. M., Heinegård, D., Twardzik, D. R., Border, W. A., & Ruoslahti, E. (1994) · Biochemical Journal · doi:10.1042/bj3020527 · Cited by 994
NOD-LRR PROTEINS: Role in Host-Microbial Interactions and Inflammatory Disease
Inohara, N., Chamaillard, M., McDonald, C., & Nuñez, G. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133347 · Cited by 991
Border, W. A., Noble, N. A., Yamamoto, T., Harper, J. R., Yamaguchi, Y., Pierschbacher, M. D., & Ruoslahti, E. (1992) · Nature · doi:10.1038/360361a0 · Cited by 974
DAMPening Inflammation by Modulating TLR Signalling
Piccinini, A. M., & Midwood, K. S. (2010) · Mediators of Inflammation · doi:10.1155/2010/672395 · Cited by 973
Inflammasomes and Their Roles in Health and Disease
Lamkanfi, M., & Dixit, V. M. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155745 · Cited by 935
The impact of the extracellular matrix on inflammation
Sorokin, L. (2010) · Nature Reviews Immunology · doi:10.1038/nri2852 · Cited by 912
Schaefer, L., Babelova, A., Kiss, E., Hausser, H.-J., Baliova, M., Krzyzankova, M., Marsche, G., Young, M. F., Mihalik, D., Götte, M., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23755 · Cited by 850
Self-citationHyaluronan in Tissue Injury and Repair
Jiang, D., Liang, J., & Noble, P. W. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123337 · Cited by 835
The inflammasome: an integrated view
Gross, O., Thomas, C. J., Guarda, G., & Tschopp, J. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01046.x · Cited by 778
Hyaluronan Fragments Act as an Endogenous Danger Signal by Engaging TLR2
Scheibner, K. A., Lutz, M. A., Boodoo, S., Fenton, M. J., Powell, J. D., & Horton, M. R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.2.1272 · Cited by 708
Midwood, K., Sacre, S., Piccinini, A. M., Inglis, J., Trebaul, A., Chan, E., Drexler, S., Sofat, N., Kashiwagi, M., Orend, G., et al. (2009) · Nature Medicine · doi:10.1038/nm.1987 · Cited by 703
Fisher, L. W., Termine, J. D., & Young, M. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83781-4 · Cited by 702
Bianco, P., Fisher, L. W., Young, M. F., Termine, J. D., & Robey, P. G. (1990) · Journal of Histochemistry & Cytochemistry · doi:10.1177/38.11.2212616 · Cited by 666
Johnson, G. B., Brunn, G. J., Kodaira, Y., & Platt, J. L. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.10.5233 · Cited by 648
Iozzo, R. V., & Murdoch, A. D. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.5.8621059 · Cited by 642
Self-citationShaping Gene Expression in Activated and Resting Primary Macrophages by IL-10
Lang, R., Patel, D., Morris, J. J., Rutschman, R. L., & Murray, P. J. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.5.2253 · Cited by 613
Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
Iozzo, R. V., & Sanderson, R. D. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01236.x · Cited by 569
Self-citationVersican: a versatile extracellular matrix proteoglycan in cell biology
Wight, T. N. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00375-7 · Cited by 562
Structures of the Toll-like Receptor Family and Its Ligand Complexes
Jin, M. S., & Lee, J.-O. (2008) · Immunity · doi:10.1016/j.immuni.2008.07.007 · Cited by 558
Biological Functions of the Small Leucine-rich Proteoglycans: From Genetics to Signal Transduction
Schaefer, L., & Iozzo, R. V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800020200 · Cited by 549
Self-citationProteoglycans: from structural compounds to signaling molecules
Schaefer, L., & Schaefer, R. M. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0821-y · Cited by 548
Self-citationHyaluronan: a multifunctional, megaDalton, stealth molecule
Lee, J. Y., & Spicer, A. P. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00135-6 · Cited by 525
Endogenous ligands of TLR2 and TLR4: agonists or assistants?
Erridge, C. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1209775 · Cited by 518
Cancer and Inflammation: An Old Intuition with Rapidly Evolving New Concepts
Trinchieri, G. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075008 · Cited by 511
Biglycan, a Danger Signal That Activates the NLRP3 Inflammasome via Toll-like and P2X Receptors
Babelova, A., Moreth, K., Tsalastra-Greul, W., Zeng-Brouwers, J., Eickelberg, O., Young, M. F., Bruckner, P., Pfeilschifter, J., Schaefer, R. M., Gröne, H.-J., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014266 · Cited by 474
Self-citationHistones from Dying Renal Cells Aggravate Kidney Injury via TLR2 and TLR4
Allam, R., Scherbaum, C. R., Darisipudi, M. N., Mulay, S. R., Hägele, H., Lichtnekert, J., Hagemann, J. H., Rupanagudi, K. V., Ryu, M., Schwarzenberger, C., et al. (2012) · Journal of the American Society of Nephrology · doi:10.1681/asn.2011111077 · Cited by 428
Self-citationZhang, G., Ezura, Y., Chervoneva, I., Robinson, P. S., Beason, D. P., Carine, E. T., Soslowsky, L. J., Iozzo, R. V., & Birk, D. E. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20776 · Cited by 423
Self-citationTheocharis, A. D., Skandalis, S. S., Tzanakakis, G. N., & Karamanos, N. K. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07800.x · Cited by 403
The interaction of versican with its binding partners
WU, Y. J., PIERRE, D. P. L., WU, J., YEE, A. J., & YANG, B. B. (2005) · Cell Research · doi:10.1038/sj.cr.7290318 · Cited by 400
The role of decorin in collagen fibrillogenesis and skin homeostasis
Reed, C. C., & Iozzo, R. V. (2002) · Glycoconjugate Journal · doi:10.1023/a:1025383913444 · Cited by 398
Self-citationInteraction of Biglycan with Type I Collagen
Schönherr, E., Witsch-Prehm, P., Harrach, B., Robenek, H., Rauterberg, J., & Kresse, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2776 · Cited by 386
Decorin Is a Biological Ligand for the Epidermal Growth Factor Receptor
Iozzo, R. V., Moscatello, D. K., McQuillan, D. J., & Eichstetter, I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4489 · Cited by 382
Self-citationTaylor, K. R., Yamasaki, K., Radek, K. A., Nardo, A. D., Goodarzi, H., Golenbock, D., Beutler, B., & Gallo, R. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606352200 · Cited by 382
Hyaluronan cross-linking: a protective mechanism in inflammation?
Day, A. J., & de la Motte, C. A. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.09.009 · Cited by 334
Merline, R., Moreth, K., Beckmann, J., Nastase, M. V., Zeng-Brouwers, J., Tralhão, J. G., Lemarchand, P., Pfeilschifter, J., Schaefer, R. M., Iozzo, R. V., et al. (2011) · Science Signaling · doi:10.1126/scisignal.2001868 · Cited by 333
Self-citationNoble, P. W., McKee, C. M., Cowman, M., & Shin, H. S. (1996) · The Journal of experimental medicine · doi:10.1084/jem.183.5.2373 · Cited by 323
Neill, T., Schaefer, L., & Iozzo, R. V. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.04.029 · Cited by 304
Self-citationThe small leucine‐rich proteoglycan biglycan modulates BMP‐4‐induced osteoblast differentiation
Chen, X.-D., Fisher, L. W., Robey, P. G., & Young, M. F. (2004) · The FASEB Journal · doi:10.1096/fj.03-0899com · Cited by 295
Iozzo, R. V., & Schaefer, L. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07797.x · Cited by 292
Self-citationYamasaki, K., Muto, J., Taylor, K. R., Cogen, A. L., Audish, D., Bertin, J., Grant, E. P., Coyle, A. J., Misaghi, A., Hoffman, H. M., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806084200 · Cited by 287
Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor.
Moscatello, D. K., Santra, M., Mann, D. M., McQuillan, D. J., Wong, A. J., & Iozzo, R. V. (1998) · Journal of Clinical Investigation · doi:10.1172/jci846 · Cited by 272
Self-citationKolb, M., Margetts, P. J., Sime, P. J., & Gauldie, J. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.280.6.l1327 · Cited by 270
Kawashima, H., Hirose, M., Hirose, J., Nagakubo, D., Plaas, A. H. K., & Miyasaka, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003387200 · Cited by 253
Intracellular hyaluronan: a new frontier for inflammation?
HASCALL, V (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.02.013 · Cited by 246
Biglycan: A Multivalent Proteoglycan Providing Structure and Signals
Nastase, M. V., Young, M. F., & Schaefer, L. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412456380 · Cited by 238
Self-citationChoi, H. U., Johnson, T. L., Pal, S., Tang, L. H., Rosenberg, L., & Neame, P. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81694-0 · Cited by 235
Decorin is a novel antagonistic ligand of the Met receptor
Goldoni, S., Humphries, A., Nyström, A., Sattar, S., Owens, R. T., McQuillan, D. J., Ireton, K., & Iozzo, R. V. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200901129 · Cited by 227
Self-citationSantra, M., Reed, C. C., & Iozzo, R. V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205317200 · Cited by 226
Self-citationSustained Down-regulation of the Epidermal Growth Factor Receptor by Decorin
Csordás, G., Santra, M., Reed, C. C., Eichstetter, I., McQuillan, D. J., Gross, D., Nugent, M. A., Hajnóczky, G., & Iozzo, R. V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005609200 · Cited by 220
Self-citationAkashi-Takamura, S., & Miyake, K. (2008) · Current Opinion in Immunology · doi:10.1016/j.coi.2008.07.001 · Cited by 213
Decorin, a Novel Player in the Insulin-like Growth Factor System
Schönherr, E., Sunderkötter, C., Iozzo, R. V., & Schaefer, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500451200 · Cited by 210
Self-citationMoreth, K., Brodbeck, R., Babelova, A., Gretz, N., Spieker, T., Zeng-Brouwers, J., Pfeilschifter, J., Young, M. F., Schaefer, R. M., & Schaefer, L. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42213 · Cited by 207
Self-citationThe matricellular functions of small leucine-rich proteoglycans (SLRPs)
Merline, R., Schaefer, R. M., & Schaefer, L. (2009) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-009-0066-2 · Cited by 200
Self-citationOspelt, C., & Gay, S. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.10.010 · Cited by 197
Correlation of Peripheral-Blood Gene Expression With the Extent of Coronary Artery Stenosis
Wingrove, J. A., Daniels, S. E., Sehnert, A. J., Tingley, W., Elashoff, M. R., Rosenberg, S., Buellesfeld, L., Grube, E., Newby, L. K., Ginsburg, G. S., et al. (2008) · Circulation: Cardiovascular Genetics · doi:10.1161/circgenetics.108.782730 · Cited by 196
Intrinsic danger: activation of Toll-like receptors in rheumatoid arthritis
Goh, F. G., & Midwood, K. S. (2012) · Rheumatology · doi:10.1093/rheumatology/ker257 · Cited by 192
de la Motte, C. A., Hascall, V. C., Calabro, A., Yen-Lieberman, B., & Strong, S. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30747 · Cited by 189
Transient Transgene Expression of Decorin in the Lung Reduces the Fibrotic Response to Bleomycin
KOLB, M., MARGETTS, P. J., GALT, T., SIME, P. J., XING, Z., SCHMIDT, M., & GAULDIE, J. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.163.3.2006084 · Cited by 189
Douglas, T., Heinemann, S., Bierbaum, S., Scharnweber, D., & Worch, H. (2006) · Biomacromolecules · doi:10.1021/bm0603746 · Cited by 184
Seidler, D. G., Goldoni, S., Agnew, C., Cardi, C., Thakur, M. L., Owens, R. T., McQuillan, D. J., & Iozzo, R. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602853200 · Cited by 180
Self-citationDecorin–TGFβ Axis in Hepatic Fibrosis and Cirrhosis
Baghy, K., Iozzo, R. V., & Kovalszky, I. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412438104 · Cited by 178
Self-citationCentral Resistin Overexposure Induces Insulin Resistance Through Toll-Like Receptor 4
Benomar, Y., Gertler, A., De Lacy, P., Crépin, D., Ould Hamouda, H., Riffault, L., & Taouis, M. (2013) · Diabetes · doi:10.2337/db12-0237 · Cited by 177
Bollyky, P. L., Lord, J. D., Masewicz, S. A., Evanko, S. P., Buckner, J. H., Wight, T. N., & Nepom, G. T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.2.744 · Cited by 173
Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components
Reinboth, B., Hanssen, E., Cleary, E. G., & Gibson, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109540200 · Cited by 168
Goldoni, S., & Iozzo, R. V. (2008) · International Journal of Cancer · doi:10.1002/ijc.23930 · Cited by 168
Self-citationDecorin Antagonizes the Angiogenic Network
Neill, T., Painter, H., Buraschi, S., Owens, R. T., Lisanti, M. P., Schaefer, L., & Iozzo, R. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.283499 · Cited by 165
Self-citationSchaefer, L., Macakova, K., Raslik, I., Micegova, M., Gröne, H.-J., Schönherr, E., Robenek, H., Echtermeyer, F. G., Grässel, S., Bruckner, P., et al. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64937-1 · Cited by 160
Self-citationSmall leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation
Moreth, K., Iozzo, R. V., & Schaefer, L. (2012) · Cell Cycle · doi:10.4161/cc.20316 · Cited by 158
Self-citationHyaluronan and versican in the control of human T-lymphocyte adhesion and migration
Evanko, S. P., Potter‐Perigo, S., Bollyky, P. L., Nepom, G. T., & Wight, T. N. (2011) · Matrix Biology · doi:10.1016/j.matbio.2011.10.004 · Cited by 157
del Fresno, C., Otero, K., Gómez-García, L., González-León, M. C., Rangel, L. S., Fuentes‐Prior, P., Escoll, P., Baos, R., Caveda, L., García, F., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.5.3032 · Cited by 154
Iozzo, R. V., Buraschi, S., Genua, M., Xu, S., Solomides, C., Peiper, S. C., Gomella, L. G., Owens, R. T., & Morrione, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.262766 · Cited by 152
Self-citationSjöberg, A. P., Manderson, G. A., Mörgelin, M., Day, A. J., Heinegård, D. K., & Blom, A. M. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.09.018 · Cited by 144
Non-proteoglycan forms of biglycan increase with age in human articular cartilage
Roughley, P. J., White, R. J., Magny, M., Liu, J., Pearce, R. H., & Mort, J. S. (1993) · Biochemical Journal · doi:10.1042/bj2950421 · Cited by 139
miRNAs regulate expression and function of extracellular matrix molecules
Rutnam, Z. J., Wight, T. N., & Yang, B. B. (2012) · Matrix Biology · doi:10.1016/j.matbio.2012.11.003 · Cited by 138
Bollyky, P. L., Wu, R. P., Falk, B. A., Lord, J. D., Long, S. A., Preisinger, A., Teng, B. J., Holt, G. E., Standifer, N. E., Braun, K. R., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017360108 · Cited by 137
Said, N. A., Sänchez‐Carbayo, M., Smith, S. C., & Theodorescu, D. (2012) · Journal of Clinical Investigation · doi:10.1172/jci61392 · Cited by 135
Simple Primary Structure, Complex Turnover Regulation and Multiple Roles of Hyaluronan
Itano, N. (2008) · The Journal of Biochemistry · doi:10.1093/jb/mvn046 · Cited by 134
Cooperative action of germ-line mutations in decorin and p53 accelerates lymphoma tumorigenesis
Iozzo, R. V., Chakrani, F., Perrotti, D., McQuillan, D. J., Skórski, T., Calabretta, B., & Eichstetter, I. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3092 · Cited by 133
Self-citationRole of Versican, Hyaluronan and CD44 in Ovarian Cancer Metastasis
Ween, M. P., Oehler, M. K., & Ricciardelli, C. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12021009 · Cited by 133
Wu, F., Vij, N., Roberts, L., López-Briones, S., Joyce, S., & Chakravarti, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702402200 · Cited by 133
Decorin Antagonizes Met Receptor Activity and Down-regulates β-Catenin and Myc Levels
Buraschi, S., Pal, N., Tyler-Rubinstein, N., Owens, R. T., Neill, T., & Iozzo, R. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172841 · Cited by 133
Self-citationDecorin Is a Novel VEGFR-2-Binding Antagonist for the Human Extravillous Trophoblast
Khan, G. A., Girish, G. V., Lala, N., Guglielmo, G. M. D., & Lala, P. K. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0426 · Cited by 129
Hyaluronan matrices in pathobiological processes
Wang, A., de la Motte, C., Lauer, M. E., & Hascall, V. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08069.x · Cited by 127
Johnstone, B., Markopoulos, M., Neame, P. J., & Caterson, B. (1993) · Biochemical Journal · doi:10.1042/bj2920661 · Cited by 126
Tumour necrosis factor‐α interacts with biglycan and decorin
Tufvesson, E., & Westergren‐Thorsson, G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03439-7 · Cited by 119
WISP-1 Binds to Decorin and Biglycan
Desnoyers, L., Arnott, D. P., & Pennica, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108339200 · Cited by 116
More than matrix: The multifaceted role of decorin in cancer
Sofeu-Feugaing, D. D., Götte, M., & Viola, M. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.08.004 · Cited by 115
Vial, C., Gutiérrez, J., Santander, C., Cabrera, D., & Brandan, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.189365 · Cited by 113
A role for decorin in the remodeling of myocardial infarction
Weis, S. M., ZIMMERMAN, S., SHAH, M., Covell, J., Omens, J. H., ROSSJR, J., Dalton, N., Jones, Y., REED, C., & Iozzo, R. V. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.05.003 · Cited by 111
Self-citationLumican Regulates Corneal Inflammatory Responses by Modulating Fas-Fas Ligand Signaling
Vij, N., Roberts, L., Joyce, S., & Chakravarti, S. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-0833 · Cited by 103
Liu, Y.-Y., Lee, C., Dedaj, R., Zhao, H., Mrabat, H., Sheidlin, A., Syrkina, O. L., Huang, P., Garg, H. G., Hales, C. A., et al. (2008) · Critical Care · doi:10.1186/cc6982 · Cited by 100
Baghy, K., Dezső, K., László, V., Fullár, A., Péterfia, B. F., Paku, S., Nagy, P., Schaff, Z., Iozzo, R. V., & Kovalszky, I. (2010) · Laboratory Investigation · doi:10.1038/labinvest.2010.172 · Cited by 98
Self-citationBrandan, E., Cabello‐Verrugio, C., & Vial, C. (2008) · Matrix Biology · doi:10.1016/j.matbio.2008.07.004 · Cited by 95
Importance of Hyaluronan-CD44 Interactions in Inflammation and Tumorigenesis
Heldin, P., Karousou, E., Olofsson, B., Porsch, H., Nishitsuka, K., & Skandalis, S. S. (2008) · Connective Tissue Research · doi:10.1080/03008200802143323 · Cited by 94
Hyperelongated biglycan: the surreptitious initiator of atherosclerosis
Little, P. J., Osman, N., & O’Brien, K. D. (2008) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32830dd7c4 · Cited by 92
Hill, D. R., Kessler, S. P., Rho, H. K., Cowman, M. K., & de la Motte, C. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.356238 · Cited by 92
Monocyte-to-Macrophage Differentiation
Chang, M. Y., Chan, C. K., Braun, K. R., Green, P. S., O’Brien, K. D., Chait, A., Day, A. J., & Wight, T. N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.324988 · Cited by 91
Schaefer, L., Tsalastra, W., Bábelová, A., Baliova, M., Minnerup, J., Sorokin, L. M., Gröne, H., Reinhardt, D. P., Pfeilschifter, J. M., Iozzo, R. V., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060497 · Cited by 88
Self-citationBuraschi, S., Neill, T., Owens, R. T., Iniguez, L. A., Purkins, G., Vadigepalli, R., Evans, B. J., Schaefer, L., Peiper, S. C., Wang, Z., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045559 · Cited by 87
Self-citationSong, R., Zeng, Q., Ao, L., Yu, J. A., Cleveland, J. C., Zhao, K.-S., Fullerton, D. A., & Meng, X. (2012) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.112.300116 · Cited by 86
Arterial remodeling in vascular disease: a key role for hyaluronan and versican
Thomas, N. (2008) · Frontiers in bioscience · doi:10.2741/3052 · Cited by 86
The interaction of versican with its binding partners
YAO, Y., Jiong, Wu, et al. (2005) · Acta Scientiarum Naturalium Universitatis Sunyatseni · Cited by 86
Extracellular matrix molecules: endogenous danger signals as new drug targets in kidney diseases
Schaefer, L. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.11.007 · Cited by 84
Self-citationMerline, R., Lazaroski, S., Bábelová, A., Tsalastra, W., Pfeilschifter, J. M., Schlüter, K., Günther, A., Iozzo, R. V., Schaefer, R. M., & Schaefer, L. (2009) · PubMed · Cited by 84
Self-citationSmall leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation
Schaefer, L., & Iozzo, R. V. (2012) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.12.002 · Cited by 83
Self-citationLigation of TLR2 by Versican: A Link Between Inflammation and Metastasis
Wang, W., Xu, G., Jia, W., Ma, J., Li, J., Ge, Y., Ren, W., Yu, J.-H., & Liu, W. (2009) · Archives of Medical Research · doi:10.1016/j.arcmed.2009.04.005 · Cited by 82
Decorin Deficiency Enhances Progressive Nephropathy in Diabetic Mice
Williams, K. J., Qiu, G., Usui, H. K., Dunn, S., McCue, P. A., Böttinger, E. P., Iozzo, R. V., & Sharma, K. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070079 · Cited by 80
Self-citationSmall Leucine-Rich Proteoglycans in Kidney Disease
Schaefer, L. (2011) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010050570 · Cited by 80
Self-citationHyaluronan in intestinal homeostasis and inflammation: implications for fibrosis
de la Motte, C. A. (2011) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00063.2011 · Cited by 78
Carlson, E. C., Lin, M., Liu, C., Kao, W. W. ‐., Perez, V. L., & Pearlman, E. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705823200 · Cited by 76
Potter‐Perigo, S., Johnson, P. Y., Evanko, S. P., Chan, C. K., Braun, K. R., Wilkinson, T. S., Altman, L. C., & Wight, T. N. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2009-0081oc · Cited by 75
Lumican is required for neutrophil extravasation following corneal injury and wound healing
Hayashi, Y., Call, M. K., Chikama, T., Liu, H., Carlson, E. C., Sun, Y., Pearlman, E. M., Funderburgh, J. L., Babcock, G. F., Liu, C., et al. (2010) · Journal of Cell Science · doi:10.1242/jcs.068221 · Cited by 65
Extracellular matrix protein lumican regulates inflammation in a mouse model of colitis
Lohr, K., Sardana, H., Lee, S., Wu, F., Huso, D. L., Hamad, A. R. A., & Chakravarti, S. (2011) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21713 · Cited by 65
Hyaluronan Fragments Promote Inflammation by Down-Regulating the Anti-inflammatory A2a Receptor
Collins, S. L., Black, K. E., Chan‐Li, Y., Ahn, Y., Cole, P. A., Powell, J. D., & Horton, M. R. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0387oc · Cited by 64
Versican is induced in infiltrating monocytes in myocardial infarction
Toeda, K., Nakamura, K., Hirohata, S., Hatipoğlu, Ö. F., Demircan, K., Yamawaki, H., Ogawa, H., Kusachi, S., Shiratori, Y., & Ninomiya, Y. (2005) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-005-8051-4 · Cited by 64
The Low Density Lipoprotein Receptor-related Protein Functions as an Endocytic Receptor for Decorin
Brandan, E., Retamal, C., Cabello‐Verrugio, C., & Marzolo, M. (2006) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84070-x · Cited by 62
Biglycan Is a Positive Modulator of BMP-2 Induced Osteoblast Differentiation
Mochida, Y., Parisuthiman, D., & Yamauchi, M. (2007) · Springer eBooks · doi:10.1007/978-0-387-34133-0_7 · Cited by 56
CD14 but not MD2 transmit signals from DAMP
Chun, K., & Seong, S. (2009) · International Immunopharmacology · doi:10.1016/j.intimp.2009.10.002 · Cited by 54
McDonald, J. A., & Hascall, V. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100064200 · Cited by 54
The proinflammatory role of hyaluronan–CD44 interactions in renal injury
Wuthrich, R. P. (1999) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/14.11.2554 · Cited by 51
The Role for Decorin in Delayed-Type Hypersensitivity
Seidler, D. G., Mohamed, N. A. E., Bocian, C., Stadtmann, A., Hermann, S., Schäfers, K. P., Schäfers, M. A., Iozzo, R. V., Zarbock, A., & Götte, M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100373 · Cited by 51
Self-citationShao, H., Lee, S., Gae-Scott, S., Nakata, C., Chen, S., Hamad, A. R. A., & Chakravarti, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380550 · Cited by 50
Inflammation Amplification by Versican: The First Mediator
Zhang, Z., Miao, L., & Wang, L. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13066873 · Cited by 49
Popović, Z. V., Wang, S., Papatriantafyllou, M., Kaya, Z., Porubský, Š., Meisner, M., Bonrouhi, M., Burgdorf, S., Young, M. F., Schaefer, L., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003478 · Cited by 45
Self-citationCo-ordinate induction of collagen type I and biglycan expression in keloids.
Hunzelmann, N., Anders, S., Sollberg, S., Schönherr, E., & Krieg, T. M. (1996) · PubMed · Cited by 44
The galactosaminoglycan-containing decorin and its impact on diseases
Seidler, D. G. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.07.012 · Cited by 41
Hwang, J., Johnson, P. Y., Braun, K. R., et al. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070875 · Cited by 36
Kitaya, K., & Yasuo, T. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0908535 · Cited by 35
Macrophages exposed to hypoxia secrete proteoglycans for which LDL has higher affinity
Asplund, A., Fridén, V., Stillemark-Billton, P., Camejo, G., & Bondjers, G. (2010) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2010.12.017 · Cited by 32
Haemopoietic biglycan produced by brain cells stimulates growth of microglial cells
Kikuchi, A., Tomoyasu, H., Kido, I., Takahashi, K., Tanaka, A., Nonaka, I., Iwakami, N., & Kamo, I. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(99)00258-1 · Cited by 27
Innate immune recognition receptors and damage-associated molecular patterns in plaque inflammation
Lundberg, A. M., & Yan, Z.-Q. (2011) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32834ada80 · Cited by 27
Wu, B., Huan, T., Gong, J., Zhou, P., & Bai, Z. (2011) · Journal of Genetics · doi:10.1007/s12041-011-0097-3 · Cited by 26
Co-ordinate induction of collagen type I and biglycan expression in keloids
Hunzelmann, N., Anders, S., Sollberg, S., Schönherr, E., & Krieg, T. M. (1996) · British Journal of Dermatology · doi:10.1046/j.1365-2133.1996.d01-1011.x · Cited by 23
Biglycan: a promising new therapeutic for neuromuscular and musculoskeletal diseases
Young, M. F., & Fallon, J. R. (2012) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.07.008 · Cited by 21
Adapala, V. J. K., Ward, M., & Ajuwon, K. M. (2012) · Journal of Inflammation · doi:10.1186/1476-9255-9-15 · Cited by 21
Regulatory roles of hyaluronan in health and disease
Hascall, V., & Karamanos, N. K. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08068.x · Cited by 15
3.3 The pathobiology of versican
Wight, T. N. (2012) · De Gruyter eBooks · doi:10.1515/9783110258776.154 · Cited by 3
Cited by
Complexity of Danger: The Diverse Nature of Damage-associated Molecular Patterns
Schaefer, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.619304 · Cited by 622
Self-citationHyaluronan: molecular size‐dependent signaling and biological functions in inflammation and cancer
Tavianatou, A. G., Caon, I., Franchi, M., Piperigkou, Z., Galesso, D., & Karamanos, N. K. (2019) · The FEBS Journal · doi:10.1111/febs.14777 · Cited by 462
Proteoglycan Chemical Diversity Drives Multifunctional Cell Regulation and Therapeutics
Karamanos, N. K., Piperigkou, Z., Theocharis, A. D., Watanabe, H., Franchi, M., Baud, S., Brézillon, S., Götte, M., Passi, A., Vigetti, D., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00354 · Cited by 367
Self-citationMyocardial Extracellular Matrix: An Ever-Changing and Diverse Entity
Rienks, M., Papageorgiou, A.-P., Frangogiannis, N. G., & Heymans, S. (2014) · Circulation Research · doi:10.1161/circresaha.114.302533 · Cited by 366
DAMPs as mediators of sterile inflammation in aging-related pathologies
Feldman, N., Rotter-Maskowitz, A., & Okun, E. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.01.003 · Cited by 283
Metadata
- Authors
- Frey, H., Schroeder, N., Manon‐Jensen, T., Iozzo, R. V., & Schaefer, L.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2013-02-21
- Volume
- 280
- Issue
- 10
- Pages
- 2165-2179
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2026550755
- Cited by
- 274
- References
- 150
- FWCI
- 14.77
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.