Extracellular matrix scaffolding in angiogenesis and capillary homeostasis
Open accessAbstract
The extracellular matrix (ECM) of blood vessels, which is composed of both the vascular basement membrane (BM) and the interstitial ECM is identified as a crucial component of the vasculature. We here focus on the unique molecular composition and scaffolding of the capillary ECM, which provides structural support to blood vessels and regulates properties of endothelial cells and pericytes. The major components of the BM are collagen IV, laminins, heparan sulfate proteoglycans and nidogen and also associated proteins such as collagen XVIII and fibronectin. Their organization and scaffolding in the BM is required for proper capillary morphogenesis and maintenance of vascular homeostasis. The BM also regulates vascular mechanosensing. A better understanding of the mechanical and structural properties of the vascular BM and interstitial ECM therefore opens new perspectives to control physiological and pathological angiogenesis and vascular homeostasis. The overall aim of this review is to explain how ECM scaffolding influences angiogenesis and capillary integrity.
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Loss of laminin, collagen IV, and fibronectin may impair angiogenesis.
“For instance, laminin, collagen IV, and fibronectin loss may impair angiogenesis [60, 61], and glycosaminoglycans (GAGs) removal accompanies growth factors depletion, impairing subsequent cell migration and differentiation [53].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [60]
Cites
Endostatin: an endogenous inhibitor of angiogenesis and tumor growth
O'Reilly, M. S., Boehm, T., Shing, Y., Fukai, N., Vasios, G., Lane, W. S., Flynn, E., Birkhead, J. R., Olsen, B. R., & Folkman, J. (1997) · Cell · doi:10.1016/s0092-8674(00)81848-6 · Cited by 4,486 · see citing works
Pericytes: Developmental, Physiological, and Pathological Perspectives, Problems, and Promises
Armulik, A., Genové, G., & Betsholtz, C. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.07.001 · Cited by 2,653 · see citing works
Pericyte Loss and Microaneurysm Formation in PDGF-B-Deficient Mice
Lindahl, P., Johansson, B. R., Levéen, P., & Betsholtz, C. (1997) · Science · doi:10.1126/science.277.5323.242 · Cited by 2,226 · see citing works
Basement membranes: structure, assembly and role in tumour angiogenesis
Kalluri, R. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1094 · Cited by 1,748 · see citing works
Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions
Hynes, R. O., & Naba, A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004903 · Cited by 1,349 · see citing works
Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
George, E. L., Georges‐Labouesse, E., Patel, R., Rayburn, H., & Hynes, R. O. (1993) · Development · doi:10.1242/dev.119.4.1079 · Cited by 1,305 · see citing works
Endothelial Extracellular Matrix
Davis, G. E., & Senger, D. R. (2005) · Circulation Research · doi:10.1161/01.res.0000191547.64391.e3 · Cited by 1,225 · see citing works
Mice deficient for PDGF B show renal, cardiovascular, and hematological abnormalities.Preprint
Levéen, P., Pekny, M., Gebré‐Medhin, S., Swolin, B., Larsson, E., & Betsholtz, C. (1994) · Genes & Development · doi:10.1101/gad.8.16.1875 · Cited by 1,130 · see citing works
Lack of Pericytes Leads to Endothelial Hyperplasia and Abnormal Vascular Morphogenesis
Hellström, M., Gerhardt, H., Kalén, M., Li, X., Eriksson, U., Wolburg, H., & Betsholtz, C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.3.543 · Cited by 1,103 · see citing works
Abnormal kidney development and hematological disorders in PDGF beta-receptor mutant mice.Preprint
Soriano, P. M. (1994) · Genes & Development · doi:10.1101/gad.8.16.1888 · Cited by 988 · see citing works
A Network Model for the Organization of Type IV Collagen Molecules in Basement Membranes
Timpl, R., Wiedemann, H., van Delden, V., Furthmayr, H., & Kühn, K. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05690.x · Cited by 897 · see citing works
Pöschl, E., Schlötzer-Schrehardt, U. M., Brachvogel, B., Saito, K., Ninomiya, Y., & Mayer, U. (2004) · Development · doi:10.1242/dev.01037 · Cited by 816 · see citing works
Perlecan Maintains the Integrity of Cartilage and Some Basement Membranes
Costell, M., Gustafsson, E., Aszódi, A., Mörgelin, M., Bloch, W., Hunziker, E. B., Addicks, K., Timpl, R., & Fässler, R. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.1109 · Cited by 672 · see citing works
Khoshnoodi, J., Pedchenko, V., & Hudson, B. G. (2008) · Microscopy Research and Technique · doi:10.1002/jemt.20564 · Cited by 668 · see citing works
Elastic fiber homeostasis requires lysyl oxidase–like 1 protein
Liu, X., Zhao, Y., Gao, J., Pawlyk, B., Starcher, B., Spencer, J. A., Yanagisawa, H., Zuo, J., & Li, T. (2004) · Nature Genetics · doi:10.1038/ng1297 · Cited by 663 · see citing works
Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wallPreprint
Lindblom, P., Gerhardt, H., Liebner, S., Abramsson, A., Enge, M., Hellström, M., Bäckström, G., Fredriksson, S., Landegren, U. D., Nyström, H. C., et al. (2003) · Genes & Development · doi:10.1101/gad.266803 · Cited by 659 · see citing works
All in the CCN family: essential matricellular signaling modulators emerge from the bunker
Leask, A., & Abraham, D. (2006) · Journal of Cell Science · doi:10.1242/jcs.03270 · Cited by 653 · see citing works
Bader, B., Rayburn, H., Crowley, D. G., & Hynes, R. O. (1998) · Cell · doi:10.1016/s0092-8674(00)81618-9 · Cited by 649 · see citing works
Role of COL4A1 in Small-Vessel Disease and Hemorrhagic Stroke
Gould, D. B., Phalan, F. C., van Mil, S. E., Sundberg, J. P., Vahedi, K., Massin, P., Bousser, M. G., Heutink, P., Miner, J. H., Tournier-Lasserve, E., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa053727 · Cited by 581 · see citing works
Expression and Function of Laminins in the Embryonic and Mature Vasculature
Hallmann, R., Horn, N., Selg, M., Wendler, O., Pausch, F., & Sorokin, L. M. (2005) · Physiological Reviews · doi:10.1152/physrev.00014.2004 · Cited by 575 · see citing works
Tzima, E., del Pozo, M. Á., Shattil, S. J., Chien, S., & Schwartz, M. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4639 · Cited by 571 · see citing works
Mutations in Col4a1 Cause Perinatal Cerebral Hemorrhage and Porencephaly
Gould, D. B., Phalan, F. C., Breedveld, G. J., van Mil, S. E., Smith, R. S., Schimenti, J. C., Aguglia, U., van der Knaap, M. S., Heutink, P., & John, S. W. M. (2005) · Science · doi:10.1126/science.1109418 · Cited by 541 · see citing works
Mäki, J. M., Rasanen, J. P., Tikkanen, H., Sormunen, R. T., Mäkikallio, K., Kivirikko, K. I., & Soininen, R. (2002) · Circulation · doi:10.1161/01.cir.0000038109.84500.1e · Cited by 484 · see citing works
Fox, J. W., Mayer, U., Nischt, R., Aumailley, M., Reinhardt, D. P., Wiedemann, H. P., Mann, K., Timpl, R., Krieg, T., & Engel, J. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04875.x · Cited by 460 · see citing works
Laminins in basement membrane assembly
Hohenester, E., & Yurchenco, P. D. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.21831 · Cited by 459 · see citing works
Saharinen, P., Eklund, L., Miettinen, J., Wirkkala, R., Anisimov, A., Winderlich, M., Nottebaum, A., Vestweber, D., Deutsch, U., Koh, G. Y., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1715 · Cited by 415 · see citing works
COL4A1 Mutations and Hereditary Angiopathy, Nephropathy, Aneurysms, and Muscle Cramps
Plaisier, E. M., Gribouval, O., Alamowitch, S., Mougenot, B., Prost‐Squarcioni, C., Verpont, M. C., Marro, B., Desmettre, T. J., Cohen, S. Y., Roullet, E., et al. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa071906 · Cited by 368 · see citing works
Nagai, N., Hosokawa, M., Itohara, S., Adachi, E., Matsushita, T., Hosokawa, N., & Nagata, K. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1499 · Cited by 368 · see citing works
Jayadev, R., & Sherwood, D. R. (2017) · Current Biology · doi:10.1016/j.cub.2017.02.006 · Cited by 353 · see citing works
Deletion of the Laminin α4 Chain Leads to Impaired Microvessel Maturation
Thyboll, J., Kortesmaa, J., Cao, R., Soininen, R., Wang, L., Iivanainen, A., Sorokin, L. M., Risling, M., Cao, Y., & Tryggvason, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1194-1202.2002 · Cited by 349 · see citing works
Jan, S. L., Amy, C., Cazes, A., Monnot, C., Lamandé, N., Favier, J., Philippe, J., Sibony, M., Gasc, J., Corvol, P. L., et al. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64285-x · Cited by 342 · see citing works
Self-citationNew insights into the roles of agrin
Bezáková, G., & Rüegg, M. A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1074 · Cited by 341 · see citing works
Vascular endothelial growth factor signaling in development and disease
Karaman, S., Leppänen, V., & Alitalo, K. K. (2018) · Development · doi:10.1242/dev.151019 · Cited by 335 · see citing works
Type VI Collagen Anchors Endothelial Basement Membranes by Interacting with Type IV Collagen
Kuo, H., Maslen, C. L., Keene, D. R., & Glanville, R. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26522 · Cited by 334 · see citing works
Kuo, D. S., Labelle-Dumais, C., & Gould, D. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds346 · Cited by 320 · see citing works
Lysyl Oxidase Is Required for Vascular and Diaphragmatic Development in Mice
Hornstra, I. K., Birge, S., STARCHER, B. C., Bailey, A. J., Mecham, R. P., & Shapiro, S. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210144200 · Cited by 309 · see citing works
Flow-Dependent Endothelial YAP Regulation Contributes to Vessel Maintenance
Nakajima, H., Yamamoto, K., Agarwala, S., Terai, K., Fukui, H., Fukuhara, S., Ando, K., Miyazaki, T., Yokota, Y., Schmelzer, E., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.019 · Cited by 308 · see citing works
Löhler, J., Timpl, R., & Jaenisch, R. (1984) · Cell · doi:10.1016/0092-8674(84)90514-2 · Cited by 287 · see citing works
Mäki, J. M., Sormunen, R. T., Lippo, S., Kaarteenaho–Wiik, R., Soininen, R., & Myllyharju, J. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61183-2 · Cited by 279 · see citing works
Heparan Sulfate in trans Potentiates VEGFR-Mediated Angiogenesis
Jakobsson, L., Kreuger, J., Holmborn, K., Lundin, L., Eriksson, I., Kjellén, L., & Claesson, L. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.03.009 · Cited by 275 · see citing works
Miner, J. H., & Li, C. (2000) · Developmental Biology · doi:10.1006/dbio.1999.9546 · Cited by 272 · see citing works
Fibronectins in vascular morphogenesis
Astrof, S., & Hynes, R. O. (2009) · Angiogenesis · doi:10.1007/s10456-009-9136-6 · Cited by 270 · see citing works
Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis
Bhave, G. B., Cummings, C. F., Vanacore, R., Kumagai-Cresse, C., Ero-Tolliver, I. A., Rafi, M., Kang, J.-S., Pedchenko, V. K., Fessler, L. I., Fessler, J. H., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1038 · Cited by 266 · see citing works
Sorokin, L. M., Pausch, F., Frieser, M., Kröger, S., Ohage, E., & Deutzmann, R. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8668 · Cited by 265 · see citing works
A single EGF‐like motif of laminin is responsible for high affinity nidogen binding.
Mayer, U., Nischt, R., Pöschl, E., Mann, K., Fukuda, K., Gerl, M., Yamada, Y., & Timpl, R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05836.x · Cited by 264 · see citing works
Bonaldo, P., Russo, V., Bucciotti, F., Doliana, R., & Colombatti, A. (1990) · Biochemistry · doi:10.1021/bi00457a021 · Cited by 263 · see citing works
Laminin isoforms in endothelial and perivascular basement membranes
Yousif, L. F., Russo, J. D., & Sorokin, L. M. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22680 · Cited by 255 · see citing works
Proposal for a unified CCN nomenclature: Table 1
Brigstock, D. R., Goldschmeding, R., Katsube, K.-I., Lam, S. C.-T., Lau, L. F., Lyons, K., Naus, C., Perbal, B., Riser, B., Takigawa, M., et al. (2003) · Molecular Pathology · doi:10.1136/mp.56.2.127 · Cited by 248 · see citing works
Hohenester, E., Tisi, D., Talts, J. F., & Timpl, R. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80388-3 · Cited by 245 · see citing works
Bader, B., Smyth, N. R., Nedbal, S., Miosge, N., Baranowsky, A., Mokkapati, S., Murshed, M., & Nischt, R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6846-6856.2005 · Cited by 244 · see citing works
Schober, J. M., Chen, N., Grzeszkiewicz, T. M., Jovanovic, I., Emeson, E. E., Ugarova, T. P., Ye, R. D., Lau, L. F., & Lam, S. C.-T. (2002) · Blood · doi:10.1182/blood.v99.12.4457 · Cited by 242 · see citing works
An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy
Moll, J., Barzaghi, P., Lin, S., Bezáková, G., Lochmüller, H., Engvall, E., Müller, U., & Rüegg, M. A. (2001) · Nature · doi:10.1038/35095054 · Cited by 238 · see citing works
Stratman, A. N., & Davis, G. E. (2011) · Microscopy and Microanalysis · doi:10.1017/s1431927611012402 · Cited by 232 · see citing works
Menezes, M. J., McClenahan, F. K., Leiton, C. V., Aranmolate, A., Shan, X., & Colognato, H. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3678-13.2014 · Cited by 226 · see citing works
Akimov, S., & Belkin, A. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.16.2989 · Cited by 217 · see citing works
Liu, J. K., Ghattas, I. R., Liu, S., Chen, S., & Rubenstein, J. L. R. (1997) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199712)210:4 · Cited by 217 · see citing works
A current view of perlecan in physiology and pathology: A mosaic of functions
Gubbiotti, M. A., Neill, T., & Iozzo, R. V. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.09.003 · Cited by 216 · see citing works
Fibronectin fibrillogenesis regulates three-dimensional neovessel formationPreprint
Zhou, X., Rowe, R. G., Hiraoka, N., George, J. P., Wirtz, D., Mosher, D. F., Virtanen, I., Chernousov, M. A., & Weiss, S. J. (2008) · Genes & Development · doi:10.1101/gad.1643308 · Cited by 210 · see citing works
Jen, Y., Manova, K., & Benezra, R. (1997) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199701)208:1 · Cited by 210 · see citing works
Bignon, M., Pichol-Thievend, C., Hardouin, J., Malbouyres, M., Bréchot, N., Nasciutti, L. E., Barret, A., Teillon, J., Guillon, E., Etienne, E., et al. (2011) · Blood · doi:10.1182/blood-2010-10-313296 · Cited by 208 · see citing works
Self-citationAttachment of cells to basement membrane collagen type IV.
Aumailley, M., & Timpl, R. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.4.1569 · Cited by 204 · see citing works
Dean, R. A., Butler, G. S., Hamma‐Kourbali, Y., Delbé, J., Brigstock, D. R., Courty, J., & Overall, C. M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00821-07 · Cited by 196 · see citing works
Blood flow drives lumen formation by inverse membrane blebbing during angiogenesis in vivo
Gebala, V., Collins, R., Geudens, I., Phng, L., & Gerhardt, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3320 · Cited by 195 · see citing works
Three Novel Collagen VI Chains with High Homology to the α3 Chain
Gara, S. K., Grumati, P., Urciuolo, A., Bonaldo, P., Kobbe, B., Koch, M., Paulsson, M., & Wagener, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709540200 · Cited by 186 · see citing works
Nanoscale protein architecture of the kidney glomerular basement membrane
Suleiman, H. Y., Zhang, L., Roth, R. A., Heuser, J. E., Miner, J. H., Shaw, A. S., & Dani, A. (2013) · eLife · doi:10.7554/elife.01149 · Cited by 185 · see citing works
Fontana, L., Chen, Y., Prijatelj, P., Sakai, T., Fässler, R., Sakai, L. Y., & Rifkin, D. B. (2005) · The FASEB Journal · doi:10.1096/fj.05-4134com · Cited by 181 · see citing works
Behrens, D. T., Villone, D., Koch, M., Brunner, G., Sorokin, L. M., Robenek, H., Bruckner‐Tuderman, L., Brückner, P., & Hansen, U. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336073 · Cited by 176 · see citing works
Integrin-dependent and -independent functions of astrocytic fibronectin in retinal angiogenesis
Stenzel, D., Lundkvist, A., Sauvaget, D., Busse, M., Graupera, M., van der Flier, A., Wijelath, E. S., Murray, J., Sobel, M., Costell, M., et al. (2011) · Development · doi:10.1242/dev.071381 · Cited by 154 · see citing works
Galaup, A., Perdiguero, E. G., Souktani, R., Durand, M., Cazes, A., Monnot, C., Teillon, J., Jan, S. L., Bouleti, C., Briois, G., et al. (2011) · Circulation · doi:10.1161/circulationaha.111.049072 · Cited by 152 · see citing works
Self-citationEndothelial basement membrane limits tip cell formation by inducing Dll4/Notch signalling in vivo
Stenzel, D., Franco, C. A., Estrach, S., Mettouchi, A., Sauvaget, D., Rosewell, I. R., Schertel, A., Armer, H. E. J., Domogatskaya, A., Rodin, S., et al. (2011) · EMBO Reports · doi:10.1038/embor.2011.194 · Cited by 152 · see citing works
Utriainen, A. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh213 · Cited by 152 · see citing works
The multiple functions of collagen XVIII in development and disease
Seppinen, L., & Pihlajaniemi, T. A. (2010) · Matrix Biology · doi:10.1016/j.matbio.2010.11.001 · Cited by 150 · see citing works
Mutations in FN1 cause glomerulopathy with fibronectin deposits
Castelletti, F., Donadelli, R., Banterla, F., Hildebrandt, F., Zipfel, P. F., Bresin, E., Otto, E. A., Skerka, C., Renieri, A., Todeschini, M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707730105 · Cited by 148 · see citing works
Agtmael, T. V., Schlötzer-Schrehardt, U. M., McKie, L., Brownstein, D. G., Lee, A., Cross, S. H., Sado, Y., Mullins, J. J., Pöschl, E., & Jackson, I. J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi348 · Cited by 146 · see citing works
Clinical spectrum of type IV collagen (COL4A1) mutations: a novel genetic multisystem disease
Vahedi, K., & Alamowitch, S. (2010) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32834232c6 · Cited by 142 · see citing works
The role of pericytic laminin in blood brain barrier integrity maintenance
Gautam, J., Zhang, X., & Yao, Y. (2016) · Scientific Reports · doi:10.1038/srep36450 · Cited by 139 · see citing works
Genotype-phenotype correlations in pathology caused by collagen type IV alpha 1 and 2 mutations
Jeanne, M., & Gould, D. B. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.10.003 · Cited by 135 · see citing works
Collagen XVIII/endostatin is essential for vision and retinal pigment epithelial function
Marneros, A. G., Keene, D. R., Hansen, U. J., Fukai, N., Moulton, K. S., Goletz, P. W., Moiseyev, G. P., Pawlyk, B. S., Halfter, W. M., Dong, S., et al. (2003) · The EMBO Journal · doi:10.1038/sj.emboj.7600014 · Cited by 134 · see citing works
Cloning of the Mouse Laminin α4 cDNA. Expression in a Subset of Endothelium
Frieser, M., Nöckel, H., Pausch, F., Röder, C., Hahn, A., Deutzmann, R., & Sorokin, L. M. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00727.x · Cited by 134 · see citing works
Endostatin and endorepellin: A common route of action for similar angiostatic cancer avengers
Poluzzi, C., Iozzo, R. V., & Schaefer, L. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.10.012 · Cited by 133 · see citing works
Lord, M. S., Chuang, C. Y., Melrose, J., Davies, M. J., Iozzo, R. V., & Whitelock, J. M. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.016 · Cited by 130 · see citing works
Favor, J., Gloeckner, C. J., Janik, D., Klempt, M., Neuhäuser-Klaus, A., Pretsch, W., Schmahl, W., & Quintanilla-Fend, L. (2006) · Genetics · doi:10.1534/genetics.106.064733 · Cited by 129 · see citing works
Collagen VI is a basement membrane component that regulates epithelial cell–fibronectin interactions
Groulx, J., Gagné, D., Benoit, Y. D., Martel, D., Basora, N., & Beaulieu, J. (2011) · Matrix Biology · doi:10.1016/j.matbio.2011.03.002 · Cited by 127 · see citing works
Obberghen‐Schilling, E. V., Tucker, R. P., Saupe, F., Gasser, I., Cseh, B., & Orend, G. (2011) · The International Journal of Developmental Biology · doi:10.1387/ijdb.103243eo · Cited by 126 · see citing works
Joutel, A., Haddad, I., Ratelade, J., & Nelson, M. T. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.62 · Cited by 126 · see citing works
Primary structure and expression of a novel human laminin α4 chain
Iivanainen, A., Sainio, K., Sariola, H. V., & Tryggvason, K. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00462-i · Cited by 123 · see citing works
Tillet, E., Wiedemann, H., Golbik, R. P., Pan, T., ZHANG, R., Mann, K., Chu, M., & Timpl, R. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18727.x · Cited by 116 · see citing works
Hou, G., Mulholland, D., Gronska, M. A., & Bendeck, M. P. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64751-7 · Cited by 116 · see citing works
Laminin Variants and Integrin Laminin Receptors in Developing and Adult Human Smooth Muscle
Glukhova, M. A., Koteliansky, V., Fondacci, C., Marotte, F., & Rappaport, L. (1993) · Developmental Biology · doi:10.1006/dbio.1993.1147 · Cited by 115 · see citing works
Xu, Y., & Yu, Q. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103661200 · Cited by 114 · see citing works
A central function for perlecan in skeletal muscle and cardiovascular development
Zoeller, J. J., McQuillan, A., Whitelock, J. M., Ho, S., & Iozzo, R. V. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708022 · Cited by 113 · see citing works
The Supramolecular Organization of Collagen VI Microfibrils
Baldock, C., Sherratt, M. J., Shuttleworth, C. A., & Kielty, C. M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00585-0 · Cited by 111 · see citing works
Laminin: loss-of-function studies
Yao, Y. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2381-0 · Cited by 111 · see citing works
Chung, C. Y., & Erickson, H. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.12.1413 · Cited by 109 · see citing works
Biosynthetic and structural properties of endothelial cell type VIII collagen.
Sage, H., Trüeb, B., & BORNSTEIN, P. K. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44129-9 · Cited by 109 · see citing works
Rasi, K., Piuhola, J., Czabanka, M., Sormunen, R. T., Ilves, M., Leskinen, H. K., Rysä, J., Kerkelä, R., Janmey, P. A., Heljäsvaara, R., et al. (2010) · Circulation Research · doi:10.1161/circresaha.110.222133 · Cited by 103 · see citing works
Chomel, C., Cazes, A., Faye, C., Bignon, M., Perdiguero, E. G., Ardidie‐Robouant, C., Barret, A., Ricard‐Blum, S., Muller, L., Germain, S., et al. (2008) · The FASEB Journal · doi:10.1096/fj.08-115170 · Cited by 100 · see citing works
Self-citationKoide, T., Takahara, Y., Asada, S., & Nagata, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106497200 · Cited by 100 · see citing works
Lysyl Oxidase-like-2 Cross-links Collagen IV of Glomerular Basement Membrane
Añazco, C. C., Jiménez, A. J. L., Rafi, M., Vega‐Montoto, L., Zhang, M., Hudson, B. G., & Vanacore, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.738856 · Cited by 97 · see citing works
Martín, A. L., Salvador, F., Moreno‐Bueno, G., Floristán, A., Ruiz‐Herguido, C., Cuevas, E. P., Morales, S., Santos, V., Csiszár, K., Dubus, P. R., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201489975 · Cited by 93 · see citing works
The sulfilimine cross-link of collagen IV contributes to kidney tubular basement membrane stiffness
Bhave, G. B., Colon, S., & Ferrell, N. J. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00096.2017 · Cited by 91 · see citing works
Endothelial basement membrane laminin 511 is essential for shear stress response
Russo, J. D., Luik, A., Yousif, L. F., Budny, S., Oberleithner, H., Hofschröer, V., Klingauf, J., VanBavel, E., Bakker, E. N. T. P., Hellstrand, P., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694756 · Cited by 91 · see citing works
Effects of high glucose on integrin activity and fibronectin matrix assembly by mesangial cells
Miller, C. G., Pozzi, A., Zent, R., & Schwarzbauer, J. E. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-03-0800 · Cited by 89 · see citing works
Enzymatic and non-enzymatic functions of the lysyl oxidase family in bone
Trackman, P. C. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.01.001 · Cited by 86 · see citing works
Expression of novel 400‐kDa laminin chains by mouse and bovine endothelial cells
Sorokin, L. M., Winfred, G. I. R. G., Göpfert, T., Hallmann, R., & Deutzmann, R. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19031.x · Cited by 83 · see citing works
Hereditary cerebral small vessel diseases: a review
Federico, A., Di Donato, I., Bianchi, S., Di Palma, C., Taglia, I., & Dotti, M. T. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.07.041 · Cited by 82 · see citing works
Integrating Activities of Laminins that Drive Basement Membrane Assembly and Function
Yurchenco, P. D. (2015) · Current topics in membranes · doi:10.1016/bs.ctm.2015.05.001 · Cited by 82 · see citing works
Alteration of Developmental and Pathological Retinal Angiogenesis in angptl4-deficient Mice
Perdiguero, E. G., Galaup, A., Durand, M., Teillon, J., Philippe, J., Valenzuela, D. M., Murphy, A. J., Yancopoulos, G. D., Thurston, G., & Germain, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220061 · Cited by 80 · see citing works
Self-citationExpression of Collagen XVIII and Localization of Its Glycosaminoglycan Attachment Sites
Dong, S., Cole, G. J., & Halfter, W. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209276200 · Cited by 76 · see citing works
Cseh, B., Fernandez-Sauze, S., Grall, D., Schaub, S., Doma, E., & Obberghen‐Schilling, E. V. (2010) · Journal of Cell Science · doi:10.1242/jcs.073346 · Cited by 73 · see citing works
Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.
Hopf, M., Göhring, W., Ries, A., Timpl, R., & Hohenester, E. (2001) · Nature Structural Biology · doi:10.1038/89683 · Cited by 71 · see citing works
Abnormalities in neural crest cell migration in laminin α5 mutant mice
Coles, E. G., Gammill, L. S., Miner, J. H., & Bronner-Fraser, M. E. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.10.031 · Cited by 69 · see citing works
Douglass, S. M., Goyal, A. K., & Iozzo, R. V. (2015) · Connective Tissue Research · doi:10.3109/03008207.2015.1045297 · Cited by 68 · see citing works
Steiner, E., Enzmann, G. U., Lyck, R., Lin, S., Rüegg, M. A., Kröger, S., & Engelhardt, B. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1969-7 · Cited by 67 · see citing works
Filla, M. S., Dimeo, K. D., Tong, T., & Peters, D. M. P. (2017) · Experimental Eye Research · doi:10.1016/j.exer.2017.08.017 · Cited by 67 · see citing works
Secretion and Matrix Assembly of Recombinant Type VI Collagen
Colombatti, A., Mucignat, M. T., & Bonaldo, P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13105 · Cited by 66 · see citing works
Collagen IV trafficking: The inside-out and beyond story
Chioran, A., Duncan, S., Catalano, A., Brown, T. J., & Ringuette, M. J. (2017) · Developmental Biology · doi:10.1016/j.ydbio.2017.09.037 · Cited by 66 · see citing works
McKee, K. K., Capizzi, S., & Yurchenco, P. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809719200 · Cited by 65 · see citing works
Hurskainen, M., Eklund, L., Hägg, P. O., Fruttiger, M., Sormunen, R. T., Ilves, M., & Pihlajaniemi, T. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-3101fje · Cited by 65 · see citing works
Binding and calcium-induced aggregation of laminin onto lipid bilayers.
Kalb, E., & Engel, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55170-x · Cited by 63 · see citing works
Perdiguero, E. G., Liabotis, A., Durand, M., Faye, C., Ricard‐Blum, S., Simonutti, M., Augustin, S., Robb, B. M., Pâques, M., Valenzuela, D. M., et al. (2016) · The Journal of Pathology · doi:10.1002/path.4805 · Cited by 63 · see citing works
Self-citationThe Bi-Functional Organization of Human Basement Membranes
Halfter, W. M., Monnier, C., Müller, D., Oertle, P., Uechi, G. T., Balasubramani, M., Safi, F., Lim, R. Y. H., Loparić, M., & Henrich, P. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067660 · Cited by 61 · see citing works
Uechi, G. T., Sun, Z., Schreiber, E. M., Halfter, W. M., & Balasubramani, M. (2014) · Journal of Proteome Research · doi:10.1021/pr5002065 · Cited by 59 · see citing works
Tsoutsman, T., Wang, X., Garchow, K., Riser, B. L., Twigg, S. M., & Semsarian, C. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.05.019 · Cited by 57 · see citing works
Cecchi, F., Pajalunga, D., Fowler, C. A., Üren, A., Rabe, D. C., Peruzzi, B., MacDonald, N. J., Blackman, D. K., Stahl, S. J., Byrd, R. A., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.06.029 · Cited by 50 · see citing works
Type VIII Collagen in Murine Development
Sage, H., & Iruela‐Arispe, M. L. (1990) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1990.tb17914.x · Cited by 50 · see citing works
Laminin Modulates Morphogenic Properties of the Collagen XVIII Endostatin Domain
Javaherian, K., Park, S. Y., Pickl, W. F., LaMontagne, K. R., Sjin, R. T. T., Gillies, S. D., & Lo, K.-M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206358200 · Cited by 47 · see citing works
Beckouche, N., Bignon, M., Lelarge, V., Mathivet, T., Pichol-Thievend, C., Berndt, S., Hardouin, J., Garand, M., Ardidie‐Robouant, C., Barret, A., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa0963 · Cited by 46 · see citing works
Self-citationRoles of fibronectin isoforms in neonatal vascular development and matrix integrity
Kumra, H., Sabatier, L., Hassan, A., Sakai, T., Mosher, D. F., Brinckmann, J., & Reinhardt, D. P. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2004812 · Cited by 43 · see citing works
Blood Vessel Basement Membrane Alterations in Human Retinal Microaneurysms During Aging
López‐Luppo, M., Nacher, V., Ramos, D., Catita, J., Navarro, M., Carretero, A., Rodríguez‐Baeza, A., Mendes-Jorge, L., & Ruberte, J. (2017) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.16-19998 · Cited by 42 · see citing works
Angiopoietin-3 Is Tethered on the Cell Surface via Heparan Sulfate Proteoglycans
Xu, Y., Liu, Y.-J., & Yu, Q. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400292200 · Cited by 38 · see citing works
Akagawa, H., Narita, A., Yamada, H., Tajima, A., Krischek, B., Kasuya, H., Hori, T., Kubota, M., Saeki, N., Hata, A., et al. (2007) · Human Genetics · doi:10.1007/s00439-007-0333-3 · Cited by 34 · see citing works
Exome Sequencing Identifies LOXL2 Mutation as a Cause of Familial Intracranial Aneurysm
Wu, Y., Li, Z., Shi, Y., Chen, L., Haibin, T., Wang, Z., Yin, C., Liu, L., & Hu, J. (2017) · World Neurosurgery · doi:10.1016/j.wneu.2017.10.094 · Cited by 32 · see citing works
Microfluidic traction force microscopy to study mechanotransduction in angiogenesis
Boldock, L., Wittkowske, C., & Perrault, C. M. (2017) · Microcirculation · doi:10.1111/micc.12361 · Cited by 31 · see citing works
Laminin isoforms in atherosclerotic arteries from mice and man.
Rauch, U., Saxena, A., Stefan Lorkowski, A., Rauterberg, J., Björkbacka, H., Durbeej, M., & Hultgårdh‐Nilsson, A. (2011) · PubMed · doi:10.14670/hh-26.711 · Cited by 26 · see citing works
Connective Tissue Growth Factor (CTGF) Expression Modulates Response to High Glucose
James, L. R., Le, C., Doherty, H. E., Kim, H., & Maeda, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070441 · Cited by 19 · see citing works
Chaqour, B. (2013) · PubMed · Cited by 18 · see citing works
Leu, S.-J. J., Sung, J.-S., Huang, M.-L., Chen, M., & Tsai, T.-W. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.04.045 · Cited by 14 · see citing works
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Mathew‐Steiner, S. S., Roy, S., & Sen, C. K. (2021) · Bioengineering · doi:10.3390/bioengineering8050063 · Cited by 1,041 · see citing works
3D and 4D Printing of Polymers for Tissue Engineering Applications
Tamay, D. G., Usal, T. D., Alagoz, A. S., Yücel, D., Hasırcı, N., & Hasırcı, V. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00164 · Cited by 419 · see citing works
Kasravi, M., Ahmadi, A., Babajani, A., Mazloomnejad, R., Hatamnejad, M. R., Shariatzadeh, S., Bahrami, S., & Niknejad, H. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00348-z · Cited by 316 · see citing works
Hydrogel Network Dynamics Regulate Vascular Morphogenesis
Zhao, W., Schnellmann, R., Pruitt, H. C., & Gerecht, S. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.08.005 · Cited by 163 · see citing works
Reed, M. J., Damodarasamy, M., & Banks, W. A. (2019) · Tissue Barriers · doi:10.1080/21688370.2019.1651157 · Cited by 158 · see citing works
Mechanical Aspects of Angiogenesis
Kretschmer, M., Rüdiger, D., & Zahler, S. (2021) · Cancers · doi:10.3390/cancers13194987 · Cited by 151 · see citing works
Functionally heterogeneous human satellite cells identified by single cell RNA sequencing
Barruet, E., Garcia, S. M., Striedinger, K., Wu, J., Lee, S., Byrnes, L. E., Wong, A., Sun, X., Tamaki, S. J., Brack, A. S., et al. (2020) · eLife · doi:10.7554/elife.51576 · Cited by 137 · see citing works
Extracellular matrix dynamics in vascular remodeling
Ma, Z., Mao, C., Jia, Y., Fu, Y., & Kong, W. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00147.2020 · Cited by 129 · see citing works
Retinal capillary basement membrane thickening: Role in the pathogenesis of diabetic retinopathy
Roy, S., & Kim, D. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100903 · Cited by 127 · see citing works
Hulett, N. A., Scalzo, R. L., & Reusch, J. E. B. (2022) · Nutrients · doi:10.3390/nu14030647 · Cited by 125 · see citing works
Progress in biomaterials inspired by the extracellular matrix
Chen, Z., Du, C., Liu, S., Liu, J., Yang, Y., Dong, L., Zhao, W., Huang, W., & Lei, Y. (2024) · Giant · doi:10.1016/j.giant.2024.100323 · Cited by 132 · see citing works
Intelligent Vascularized 3D/4D/5D/6D-Printed Tissue Scaffolds
Han, X., Saiding, Q., Cai, X., Xiao, Y., Wang, P., Cai, Z., Gong, X., Gong, W., Zhang, X., & Cui, W. (2023) · Nano-Micro Letters · doi:10.1007/s40820-023-01187-2 · Cited by 116 · see citing works
Wareham, L. K., Baratta, R. O., Buono, B. J. D., Schlumpf, E., & Calkins, D. J. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00704-0 · Cited by 111 · see citing works
Hydrogel scaffolds in bone regeneration: Their promising roles in angiogenesis
Liu, J., Yang, L., Liu, K., & Gao, F. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1050954 · Cited by 90 · see citing works
Heparan sulfate proteoglycans: The sweet side of development turns sour in mucopolysaccharidoses
Pasquale, V. D., & Pavone, L. M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165539 · Cited by 86 · see citing works
Bauer, Y., de Bernard, S., Hickey, P. M., Ballard, K., Cruz, J. P., Cornelisse, P., Chadha‐Boreham, H., Distler, O., Rosenberg, D., Doelberg, M., et al. (2020) · European Respiratory Journal · doi:10.1183/13993003.02591-2020 · Cited by 84 · see citing works
Heparan Sulfate Proteoglycan Signaling in Tumor Microenvironment
Pasquale, V. D., & Pavone, L. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186588 · Cited by 77 · see citing works
Clinical Potential of Mesenchymal Stem Cell-Derived Exosomes in Bone Regeneration
Torrecillas-Baena, B., Pulido-Escribano, V., Dorado, G., Gálvez-Moreno, M. Á., Camacho-Cardeñosa, M., & Casado‐Díaz, A. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12134385 · Cited by 74 · see citing works
Liu, Y., Zhang, Y., Mei, T., Cao, H., Hu, Y., Jia, W., Wang, J., Zhang, Z., Wang, Z., Le, W., et al. (2022) · Advanced Science · doi:10.1002/advs.202104299 · Cited by 70 · see citing works
Effect of Angiogenesis in Bone Tissue Engineering
Huang, J., Han, Q., Cai, M., Zhu, J., Li, L., Yu, L., Wang, Z., Fan, G., Zhu, Y., Lü, J., et al. (2022) · Annals of Biomedical Engineering · doi:10.1007/s10439-022-02970-9 · Cited by 64 · see citing works
The role of extracellular matrix in angiogenesis: Beyond adhesion and structure
Libby, J. R., Royce, H. A., Walker, S. R., & Li, L. (2024) · Biomaterials and Biosystems · doi:10.1016/j.bbiosy.2024.100097 · Cited by 63 · see citing works
Pourmasoumi, P., Moghaddam, A., Mahand, S. N., Heidari, F., Moghaddam, Z. S., Arjmand, M., Kuehnert, I., Kruppke, B., Wiesmann, H., & Khonakdar, H. A. (2022) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2022.2110480 · Cited by 62 · see citing works
Vascular Extracellular Matrix in Atherosclerosis
Nubila, A. D., Dilella, G., Simone, R., & Barbieri, S. S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212017 · Cited by 69 · see citing works
In vitro 3D Systems to Model Tumor Angiogenesis and Interactions With Stromal Cells
Brassard-Jollive, N., Monnot, C., Muller, L., & Germain, S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.594903 · Cited by 58 · see citing works
Self-citationLopes, S. V., Collins, M. N., Reis, R. L., Oliveira, J. M., & Silva‐Correia, J. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.1c00051 · Cited by 60 · see citing works
Metal ions and the extracellular matrix in tumor migration
Stelling, M. P., Motta, J. M., Mashid, M., Johnson, W. E., Pavão, M. S. G., & Farrell, N. P. (2019) · FEBS Journal · doi:10.1111/febs.14986 · Cited by 57 · see citing works
The extracellular matrix mechanics in the vasculature
Wang, D., Brady, T., Santhanam, L., & Gerecht, S. (2023) · Nature Cardiovascular Research · doi:10.1038/s44161-023-00311-0 · Cited by 55 · see citing works
Proteoglycans and Immunobiology of Cancer—Therapeutic Implications
Tzanakakis, G. N., Neagu, M. T., Tsatsakis, A. M., & Nikitovic, D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00875 · Cited by 54 · see citing works
Tenascin-C: A Key Regulator in Angiogenesis during Wound Healing
Wang, Y., Wang, G., & Liu, H. (2022) · Biomolecules · doi:10.3390/biom12111689 · Cited by 51 · see citing works
Unraveling the molecular mechanisms between inflammation and tumor angiogenesis.
Zhou, W., Yang, L., Nie, L., & Lin, H. (2021) · PubMed Central · Cited by 51 · see citing works
Nidogen: A matrix protein with potential roles in musculoskeletal tissue regeneration
Zhou, S., Chen, S., Pei, Y. A., & Pei, M. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.03.004 · Cited by 48 · see citing works
Cheng, P., Cao, T., Zhao, X., Lu, W., Miao, S., Ning, F., Wang, D., Gao, Y., Wang, L., Pei, G., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.10.021 · Cited by 47 · see citing works
Jiang, Y., Wang, S., Wang, C., Xu, R.-H., Wang, W., Jiang, Y., Wang, M., Jiang, L., Dai, L.-H., Wang, J., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106119 · Cited by 42 · see citing works
Pericytes in Cerebrovascular Diseases: An Emerging Therapeutic Target
Su, X., Huang, L., Qu, Y., Xiao, D., & Mu, D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00519 · Cited by 44 · see citing works
Senk, A., & Djonov, V. (2021) · Scientific Reports · doi:10.1038/s41598-021-98852-6 · Cited by 45 · see citing works
Ovarian tissue damage after grafting: systematic review of strategies to improve follicle outcomes
Cacciottola, L., Donnez, J., & Dolmans, M. (2021) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2021.06.019 · Cited by 45 · see citing works
Umaña-Diaz, C., Pichol-Thievend, C., Marchand, M. F., Atlas, Y., Salza, R., Malbouyres, M., Barret, A., Teillon, J., Ardidie‐Robouant, C., Ruggiero, F., et al. (2019) · Matrix Biology · doi:10.1016/j.matbio.2019.11.003 · Cited by 44 · see citing works
Self-citationSaio, S., Konishi, K., Hohjoh, H., Tamura, Y., Masutani, T., Iddamalgoda, A., Ichihashi, M., Hasegawa, H., & Mizutani, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011169 · Cited by 43 · see citing works
He, J., Pang, Q., Huang, C., Xie, J., Hu, J., Wang, L., Wang, C., Meng, L., & Fan, R. (2021) · Toxicology in Vitro · doi:10.1016/j.tiv.2021.105296 · Cited by 43 · see citing works
Emerging role of interactions between tumor angiogenesis and cancer stem cells
Lv, S., Liu, Y., Xie, C., Xue, C., Du, S., & Yao, J. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.06.036 · Cited by 45 · see citing works
Organ-On-A-Chip Technologies for Advanced Blood–Retinal Barrier Models
Ragelle, H., Gonçalves, A., Kustermann, S., Antonetti, D. A., & Jayagopal, A. (2019) · Journal of Ocular Pharmacology and Therapeutics · doi:10.1089/jop.2019.0017 · Cited by 42 · see citing works
CircRNA in ocular neovascular diseases: Fundamental mechanism and clinical potential
Zhang, W., He, Y., & Zhang, Y. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106946 · Cited by 42 · see citing works
The role of laminins in cancer pathobiology: a comprehensive review
Nonnast, E., Mira, E., & Mañes, S. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06079-0 · Cited by 40 · see citing works
Mechanical regulation of the early stages of angiogenesis
Barrasa-Ramos, S., Dessalles, C. A., Hautefeuille, M., & Barakat, A. I. (2022) · Journal of The Royal Society Interface · doi:10.1098/rsif.2022.0360 · Cited by 38 · see citing works
Kremheller, J., Vuong, A., Schrefler, B. A., & Wall, W. A. (2019) · International Journal for Numerical Methods in Biomedical Engineering · doi:10.1002/cnm.3253 · Cited by 38 · see citing works
Atlas, Y., Gorin, C., Novais, A., Marchand, M. F., Chatzopoulou, E., Lesieur, J., Bascetin, R., Binet-Moussy, C., Sadoine, J., Lesage, M., et al. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120594 · Cited by 38 · see citing works
Self-citationThe Extracellular Matrix Protein ABI3BP in Cardiovascular Health and Disease
Delfín, D. A., DeAguero, J. L., & McKown, E. N. (2019) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00023 · Cited by 34 · see citing works
The Role of IGF/IGF-IR-Signaling and Extracellular Matrix Effectors in Bone Sarcoma Pathogenesis
Tzanakakis, G. N., Giatagana, E.-M., Berdiaki, A., Spyridaki, I., Hida, K., Neagu, M. T., Tsatsakis, A. M., & Nikitovic, D. (2021) · Cancers · doi:10.3390/cancers13102478 · Cited by 37 · see citing works
Asega, A. F., Menezes, M. C., Trevisan-Silva, D., Cajado-Carvalho, D., Nasciben, L. B., Oliveira, A. K., Zelanis, A., & Serrano, S. M. T. (2020) · Scientific Reports · doi:10.1038/s41598-020-69396-y · Cited by 35 · see citing works
Mechanism and application of fibrous proteins in diabetic wound healing: a literature review
Yan, L., Wang, Y., Feng, J., Ni, Y., Zhang, T., Cao, Y., Zhou, M., & Zhao, C. J. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1430543 · Cited by 31 · see citing works
The role of extracellular matrix in mouse and human corneal neovascularization
Barbariga, M., Vallone, F., Mosca, E., Bignami, F., Magagnotti, C., Fonteyne, P., Chiappori, F., Milanesi, L., Rama, P., Andolfo, A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-50718-8 · Cited by 30 · see citing works
Liver Matrix in Benign and Malignant Biliary Tract Disease
Fabris, L., Cadamuro, M., Cagnin, S., Strazzabosco, M., & Gores, G. J. (2020) · Seminars in Liver Disease · doi:10.1055/s-0040-1705109 · Cited by 30 · see citing works
Extracellular Matrix-Derived Hydrogels to Augment Dermal Wound Healing: A Systematic Review
Vriend, L., Sinkunas, V., Camargo, C. P., van der Lei, B., Harmsen, M. C., & van Dongen, J. A. (2021) · Tissue Engineering Part B Reviews · doi:10.1089/ten.teb.2021.0120 · Cited by 30 · see citing works
Extracellular Matrix Coatings on Cardiovascular Materials—A Review
Yao, S., Cui, J., Chen, S., Zhou, X., Li, J., & Zhang, K. (2022) · Coatings · doi:10.3390/coatings12081039 · Cited by 30 · see citing works
Cell-Based Strain Remodeling of a Nonfibrous Matrix as an Organizing Principle for Vasculogenesis
Rüdiger, D., Kick, K., Goychuk, A., Vollmar, A. M., Frey, E., & Zahler, S. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108015 · Cited by 30 · see citing works
Martínez, S. B., Kohler, B., Rodrı́guez, M., Izco, J. M., Recalde, J. I., & Pascual, G. (2022) · Biomedicines · doi:10.3390/biomedicines10050960 · Cited by 29 · see citing works
Ostadi, Y., Khanali, J., Tehrani, F. A., Yazdanpanah, G., Bahrami, S., Niazi, F., & Niknejad, H. (2024) · Biomaterials Research · doi:10.34133/bmr.0071 · Cited by 30 · see citing works
Biofabrication of tissue engineering vascular systems
Zhang, Q., Bosch-Rué, È., Pérez, R. A., & Truskey, G. A. (2021) · APL Bioengineering · doi:10.1063/5.0039628 · Cited by 29 · see citing works
Somasekhar, L., & Griffiths, L. G. (2023) · Stem Cells Translational Medicine · doi:10.1093/stcltm/szad046 · Cited by 27 · see citing works
Endothelial depletion of Atg7 triggers astrocyte–microvascular disassociation at blood–brain barrier
Liu, H., Wei, J., Li, Y., Ban, M., Sun, Q., Wang, H.-J., Zhao, D., Tong, P., Wang, L., Wang, K.-J., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202103098 · Cited by 27 · see citing works
Han, I., Thakor, D. K., Ropper, A. E., Yu, D., Wang, L., Kabataş, S., Zeng, X., Kim, S., ZAFONTE, R. D., & Teng, Y. D. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.112980 · Cited by 27 · see citing works
Yao, X., He, Z., Qin, C., Zhang, P., Sui, C., Deng, X., Fang, Y., Li, G., & Shi, J. (2022) · British Journal of Cancer · doi:10.1038/s41416-022-01834-2 · Cited by 26 · see citing works
Ghosh, S., Chaudhuri, S., Roy, P., & Debrupa Lahiri, A. (2022) · Regenerative Engineering and Translational Medicine · doi:10.1007/s40883-022-00288-5 · Cited by 26 · see citing works
Kong, F., Mehwish, N., Niu, X., Lin, M., Rong, X., Hu, F., & Lee, B. H. (2021) · Materials Today Chemistry · doi:10.1016/j.mtchem.2021.100612 · Cited by 25 · see citing works
Zheng, P., Huang, Z., Tong, D.-C., Zhou, Q., Tian, S., Chen, B., Ning, D.-M., Guo, Y., Zhu, W., Long, Y., et al. (2022) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v14.i2.450 · Cited by 25 · see citing works
Wang, Z., Tang, X., Swaminathan, S. K., Kandimalla, K. K., & Kalari, K. R. (2022) · npj Systems Biology and Applications · doi:10.1038/s41540-022-00235-8 · Cited by 24 · see citing works
Gnanaguru, G., Tabor, S. J., Bonilla, G. M., Sadreyev, R. I., Yuda, K., Köhl, J., & Connor, K. M. (2023) · Development · doi:10.1242/dev.201047 · Cited by 27 · see citing works
Wang, D., Zhu, Y. X., Huang, Y. H., Zhu, J., Zhu, B., Zhao, Y., Lu, Y., Wang, Z., & Guo, Y. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.1c00269 · Cited by 24 · see citing works
Ruan, Q., Tan, S., Guo, L., Ma, D., & Wen, J. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1186030 · Cited by 24 · see citing works
Martínez-Rey, D., Carmona‐Rodríguez, L., Fernández‐Aceñero, M. J., Mira, E., & Mañes, S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.579552 · Cited by 21 · see citing works
Hydrogel biomaterials to support and guide vascularization
Chapla, R., & West, J. L. (2020) · Progress in Biomedical Engineering · doi:10.1088/2516-1091/abc947 · Cited by 22 · see citing works
Interaction of non‑parenchymal hepatocytes in the process of hepatic fibrosis (Review)
Cheng, Q.-N., Yang, X. Y., Wu, J., Ai, W., & Ni, Y. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12003 · Cited by 22 · see citing works
Role of Heparan Sulfate in Vasculogenesis of Dental Pulp Stem Cells
Li, A., Sasaki, J., Inubushi, T., Abe, G. L., Nor, J. E., Yamashiro, T., & Imazato, S. (2022) · Journal of Dental Research · doi:10.1177/00220345221130682 · Cited by 22 · see citing works
Targeting RORγ inhibits the growth and metastasis of hepatocellular carcinoma
Liu, Q., Wang, J., Sun, H., Zhang, Z., Wang, H., Ma, S., Zhang, C., Wang, Q., Cai, G., Zheng, J., et al. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.01.032 · Cited by 19 · see citing works
Biological role of heparan sulfate in osteogenesis: A review
Xu, Z., Chen, S., Feng, D., Liu, Y., Wang, Q., Gao, T., Liu, Z., Zhang, Y., Chen, J., & Qiu, L. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118490 · Cited by 21 · see citing works
Song, S., Guo, L., Wu, D., Shi, J., Duan, Y., He, X., Liu, Y., Ding, Y., Ji, X., & Meng, R. (2021) · Biomolecules · doi:10.3390/biom11081164 · Cited by 19 · see citing works
Nicosia, A., Salamone, M., Costa, S., Ragusa, M. A., & Ghersi, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512314 · Cited by 18 · see citing works
Wang, W., Su, L., Wang, Y., Li, C., Ji, F., & Jiao, J. (2022) · Advanced Science · doi:10.1002/advs.202105208 · Cited by 17 · see citing works
Zhang, F., Xu, M., Yang, Q. Z., Hua, B., Xia, B., Lin, Z.-Y., Xiao, X., Monahan, P. E., & Sun, J. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm9010075 · Cited by 17 · see citing works
Zhang, M., Zhao, F., Zhang, X., Brouwer, L. A., Burgess, J. K., & Harmsen, M. C. (2023) · Materials Today Bio · doi:10.1016/j.mtbio.2023.100842 · Cited by 17 · see citing works
Nidogen in development and disease
Töpfer, U., & Holz, A. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1380542 · Cited by 17 · see citing works
Miyake, K., Miyagawa, S., Harada, A., & Sawa, Y. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.01.008 · Cited by 17 · see citing works
Trends in protein derived materials for wound care applications
Zubair, M., Hussain, S., Rehman, M. U., Hussain, A. S., Akram, M., Shahzad, S., Rauf, Z., Mujahid, M., & Ullah, A. (2024) · Biomaterials Science · doi:10.1039/d4bm01099j · Cited by 17 · see citing works
Differential Expression of Extracellular Matrix Components in Nasal Polyp Endotypes
Feng, X., Payne, S. C., Borish, L., & Steinke, J. W. (2019) · American Journal of Rhinology and Allergy · doi:10.1177/1945892419860634 · Cited by 16 · see citing works
Nakakura, T., Suzuki, T., Tanaka, H., Arisawa, K., Miyashita, T., Nekooki-Machida, Y., Kurosawa, T., Tega, Y., Deguchi, Y., & Hagiwara, H. (2020) · Cell and Tissue Research · doi:10.1007/s00441-020-03273-y · Cited by 16 · see citing works
Microvascularization in 3D Human Engineered Tissue and Organoids
Shin, Y. J., Safina, D., Zheng, Y. Y., & Levenberg, S. (2025) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-103023-115236 · Cited by 17 · see citing works
Han, L., Yang, Y., Hou, C., Zheng, J., Lv, G., Mao, R., Xu, P., Chen, S., Zhou, Y., Wang, P., et al. (2021) · Genetic Testing and Molecular Biomarkers · doi:10.1089/gtmb.2020.0279 · Cited by 15 · see citing works
Mościcka, P., Cwajda‐Białasik, J., Szewczyk, M. T., & Jawień, A. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph19127108 · Cited by 15 · see citing works
Zhou, Z., Zhong, H., Wang, H., Wang, S., Kridis, W. B., Wang, R., Shen, K., Wang, Z., & Huang, R. (2025) · Discover Oncology · doi:10.1007/s12672-025-03797-1 · Cited by 13 · see citing works
Shabani, Z., Schuerger, J., Zhu, X., Tang, C., Ma, L., Yadav, A., Liang, R., Press, K., Weinsheimer, S., Schmidt, A., et al. (2024) · Cells · doi:10.3390/cells13010092 · Cited by 13 · see citing works
He, J., Wang, X., Wang, Z., Xie, R., Zhang, Z., Liu, T., Cai, Y., & Chen, L. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.110110 · Cited by 13 · see citing works
Vermue, I. M., Begum, R., Castilho, M. D., Rookmaaker, M. B., Masereeuw, R., Bouten, C. V. C., Verhaar, M. C., & Cheng, C. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.1c00408 · Cited by 13 · see citing works
Yang, G., Zhu, J., Zhan, G., Fan, G., Deng, L., Tang, H., Jiang, X., Chen, B., & Yang, C. (2022) · Stem Cells International · doi:10.1155/2022/6450527 · Cited by 13 · see citing works
Zhang, M., Getova, V. E., Martinez-Garcia, F. D., Borghuis, T., Burgess, J. K., & Harmsen, M. C. (2022) · Gels · doi:10.3390/gels8110729 · Cited by 12 · see citing works
New insights into the role of ubiquitination in angiogenesis (Review)
Chen, T., Wang, K., & Sun, Z. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5473 · Cited by 13 · see citing works
Human adipose-derived stem cells promote seawater-immersed wound healing via proangiogenic effects
Xiong, J., Qiang, H., Li, T., Zhao, J., Wang, Z., Li, F., & Xu, J. (2021) · Aging · doi:10.18632/aging.202773 · Cited by 12 · see citing works
Zhu, J., Tang, Z., Ren, J., Geng, J., Guo, F., Xu, Z., Jia, J., Chen, L., & Jia, Y. (2021) · Journal of Vascular Surgery Venous and Lymphatic Disorders · doi:10.1016/j.jvsv.2021.08.020 · Cited by 11 · see citing works
Liu, Y.-J., Zeng, S.-H., Qian, W.-H., Tao, M.-X., Zhu, Y.-Y., & Li, J.-P. (2022) · Pharmacogenomics and Personalized Medicine · doi:10.2147/pgpm.s356326 · Cited by 12 · see citing works
Xue, J., Liao, Q., Luo, M., Hua, C., Zhao, J., Yu, G., Chen, X., Li, X., Zhang, X., Ran, R., et al. (2022) · Open Biology · doi:10.1098/rsob.210310 · Cited by 12 · see citing works
Shin, H. S., Thakore, A. D., Tada, Y., Pedroza, A. J., Ikeda, G., Chen, I. Y., Chan, D. C., Jaatinen, K. J., Yajima, S., Pfrender, E. M., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-21510-y · Cited by 12 · see citing works
- Authors
- Marchand, M., Monnot, C., Muller, L., & Germain, S.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Germain, Stéphane
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 89
- Pages
- 147-156
- ISSN
- 1084-9521 (ISSN-L)
- OpenAlex
- W2891724652
- Cited by
- 205
- References
- 139
- Citations by year
- 2026: 14 · 2025: 20 · 2024: 29 · 2023: 28 · 2022: 41 · 2021: 32 · 2020: 23 · 2019: 18
- FWCI
- 2.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Seminars in Cell and Developmental Biology (acceptedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by-nc)
- Funders
- Fondation pour la Recherche Médicale
- INSERM
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- extracellular matrix, angiogenesis, vascular basement membrane, type IV collagen, laminin, heparan sulfate proteoglycans, nidogen, collagen XVIII, fibronectin, pericytes, endothelial cells, capillary morphogenesis, vascular integrity
- MeSH terms
- Basement Membrane, Blood Vessels, Extracellular Matrix, Fibronectins, Humans, Laminin, Membrane Glycoproteins, Neovascularization, Pathologic, Neovascularization, Physiologic, Heparan Sulfate Proteoglycans, Pericytes, Endothelial Cells, Collagen Type XVIII
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