Molecular pathways of cell-mediated degradation of fibrillar collagen

Sprangers, Sara; Everts, Vincent

doi:10.1016/j.matbio.2017.11.008

Cited by 102Protease and Inhibitor MechanismsCollagen: Extraction and CharacterizationTGF-β signaling in diseases

Molecular pathways of cell-mediated degradation of fibrillar collagen

Sprangers, Sara, Everts, Vincent·2019·Matrix Biology

DOI 10.1016/j.matbio.2017.11.008

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Abstract

Fibrillar collagens are the most abundant components of the extracellular matrix and provide stability to connective tissues, such as bone, cartilage and skin. An imbalance in collagen turnover inevitably affects the function of these tissues. Therefore, the molecular and cellular mechanisms involved in the synthesis and degradation of collagen have received increasing attention. This short review attempts to summarize our present understanding of how different pathways of collagen degradation are used by different cell types.

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To be degraded, fibrillary collagen usually requires the activation of the cysteine protease cathepsin K and members of the matrix metalloproteinase (MMP) family.
“To be degraded, fibrillary collagen usually requires the activation of the cysteine protease cathepsin K and members of the matrix metalloproteinase (MMP) family.119”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [119]

Remodelling the extracellular matrix in development and disease
Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367 · see citing works
Collagens—structure, function, and biosynthesis
Gelse, K. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.08.002 · Cited by 2,663 · see citing works
Extracellular Matrix Assembly: A Multiscale Deconstruction
Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534 · see citing works
Collagen fibril formation
Kadler, K. E., Holmes, D. F., Trotter, J. A., & Chapman, J. A. (1996) · Biochemical Journal · doi:10.1042/bj3160001 · Cited by 1,452 · see citing works
MT1-MMP-Deficient Mice Develop Dwarfism, Osteopenia, Arthritis, and Connective Tissue Disease due to Inadequate Collagen Turnover
Holmbeck, K., Bianco, P., Caterina, J., Yamada, S., Kromer, M., Kuznetsov, S. A., Mankani, M., Gehron Robey, P., Poole, A. R., Pidoux, I., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80064-1 · Cited by 1,298 · see citing works
Collagens, modifying enzymes and their mutations in humans, flies and worms
Myllyharju, J. (2003) · Trends in Genetics · doi:10.1016/j.tig.2003.11.004 · Cited by 1,179 · see citing works
Extracellular matrix remodelling: the role of matrix metalloproteinases
Stamenkovic, I. (2003) · The Journal of Pathology · doi:10.1002/path.1400 · Cited by 1,142 · see citing works
Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products
Verzijl, N., DeGroot, J., Thorpe, S. R., Bank, R. A., Shaw, J., Lyons, T. J., Bijlsma, J. W. J., Lafeber, F. P. J. G., Baynes, J., & TeKoppele, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006700200 · Cited by 964 · see citing works
Matrix Metalloproteinase-2 Is an Interstitial Collagenase
Aimes, R. T., & Quigley, J. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.5872 · Cited by 944 · see citing works
Collagens at a glance
Kadler, K., Baldock, C., Bella, J., & Boot-Handford, R. (2007) · Journal of Cell Science · doi:10.1242/jcs.03453 · Cited by 903 · see citing works
Physiology and pathophysiology of matrix metalloproteases
Klein, T., & Bischoff, R. (2010) · Amino Acids · doi:10.1007/s00726-010-0689-x · Cited by 834 · see citing works
Matrix metalloproteinases (MMPs): Chemical–biological functions and (Q)SARs
Verma, R. P., & Hansch, C. H. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.01.011 · Cited by 783 · see citing works
Biological role of matrix metalloproteinases: a critical balance
Löffek, S., Schilling, O., & Franzke, C.-W. (2010) · European Respiratory Journal · doi:10.1183/09031936.00146510 · Cited by 763 · see citing works
Osteoclasts: What Do They Do and How Do They Do It?
Teitelbaum, S. L. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.060834 · Cited by 730 · see citing works
The Use of Biochemical Markers of Bone Turnover in Osteoporosis
Delmas, P. D., Eastell, R., Garnero, P., Seibel, M. J., & Stepan, J. J. (2000) · Osteoporosis International · doi:10.1007/s001980070002 · Cited by 717 · see citing works
Outcomes of total hip and knee replacement: Preoperative functional status predicts outcomes at six months after surgery
Fortin, P. R., Clarke, A. E., Joseph, L., Liang, M. H., Tänzer, M., Ferland, D., Phillips, C., Partridge, A. J., B�lisle, P., Fossel, A. H., et al. (1999) · Arthritis & Rheumatism · doi:10.1002/1529-0131(199908)42:8 · Cited by 708 · see citing works
Collagenase unwinds triple‐helical collagen prior to peptide bond hydrolysis
Chung, L., Dinakarpandian, D., Yoshida, N., Lauer‐Fields, J. L., Fields, G. B., Visse, R., & Nagase, H. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600318 · Cited by 677 · see citing works
Collagen self-assembly and the development of tendon mechanical properties
Silver, F. H., Freeman, J. W., & Seehra, G. P. (2003) · Journal of Biomechanics · doi:10.1016/s0021-9290(03)00135-0 · Cited by 646 · see citing works
Building Collagen Molecules, Fibrils, and Suprafibrillar Structures
HULMES, D. J. S. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4450 · Cited by 591 · see citing works
Type V collagen controls the initiation of collagen fibril assembly
Wenstrup, R. J., Florer, J. B., Brunskill, E. W., Bell, S. M., Chervoneva, I., & Birk, D. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409622200 · Cited by 545 · see citing works
A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation
Weathington, N. M., van Houwelingen, A. H., Noerager, B. D., Jackson, P. L., Kraneveld, A. D., Galin, F. S., Folkerts, G., Nijkamp, F. P., & Blalock, J. E. (2006) · Nature Medicine · doi:10.1038/nm1361 · Cited by 497 · see citing works
Identification of the Second Membrane-type Matrix Metalloproteinase (MT-MMP-2) Gene from a Human Placenta cDNA Library
Takino, T., Sato, H., Shinagawa, A., & Seiki, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.23013 · Cited by 471 · see citing works
Matrix metalloproteinase interactions with collagen and elastin
Doren, S. R. V. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.005 · Cited by 463 · see citing works
Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly
Birk, D. E. (2001) · Micron · doi:10.1016/s0968-4328(00)00043-3 · Cited by 429 · see citing works
The collagen superfamily: from the extracellular matrix to the cell membrane
Ricard‐Blum, S., & Ruggiero, F. (2005) · Pathologie Biologie · doi:10.1016/j.patbio.2004.12.024 · Cited by 428 · see citing works
The Bone Lining Cell: Its Role in Cleaning Howship's Lacunae and Initiating Bone Formation
Everts, V., Delaissé, J. M., Korper, W., Jansen, D. C., Tigchelaar-Gutter, W., Saftig, P., & Beertsen, W. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.1.77 · Cited by 411 · see citing works
Self-citation
Cathepsin B1. A lysosomal enzyme that degrades native collagen
Burleigh, M. C., Barrett, A. J., & Lazarus, G. S. (1974) · Biochemical Journal · doi:10.1042/bj1370387 · Cited by 407 · see citing works
Leptin in hepatic fibrosis: evidence for increased collagen production in stellate cells and lean littermates of ob/ob mice
Saxena, N. K., Ikeda, K., Rockey, D. C., Friedman, S. L., & Anania, F. A. (2002) · Hepatology · doi:10.1053/jhep.2002.32029 · Cited by 382 · see citing works
Integrin-mediated Cell Adhesion to Type I Collagen Fibrils
Jokinen, J., Dadu, E., Nykvist, P., Käpylä, J., White, D. J., Ivaska, J., Vehviläinen, P., Reunanen, H., Larjava, H., Häkkinen, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401409200 · Cited by 380 · see citing works
Fragments of extracellular matrix as mediators of inflammation
Adair-Kirk, T. L., & Senior, R. M. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.12.005 · Cited by 362 · see citing works
M2-like macrophages are responsible for collagen degradation through a mannose receptor–mediated pathway
Madsen, D. H., Leonard, D., Masedunskas, A., Moyer, A. B., Jürgensen, H. J., Peters, D. E., Amornphimoltham, P., Selvaraj, A., Yamada, S. S., Brenner, D. A., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201301081 · Cited by 350 · see citing works
Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor.
Haigler, H. T., McKanna, J. A., & Cohen, S. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.83.1.82 · Cited by 330 · see citing works
Structural properties of matrix metalloproteinases
Bode, W., Fernandez-Catalan, C., Tschesche, F. G. H., & H. Nagase, K. M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050320 · Cited by 328 · see citing works
Human lung cancer cells express functionally active Toll-like receptor 9
Droemann, D., Albrecht, D., Gerdes, J., Ulmer, A., Branscheid, D., Vollmer, E., Dalhoff, K., Zabel, P., & Goldmann, T. (2005) · Respiratory Research · doi:10.1186/1465-9921-6-1 · Cited by 327 · see citing works
Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
Nagase, H., & Fields, G. B. (1996) · Biopolymers · doi:10.1002/(sici)1097-0282(1996)40:4 · Cited by 318 · see citing works
The Fibrillar Collagen Family
Exposito, J., Valcourt, U., Cluzel, C., & Lethias, C. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11020407 · Cited by 310 · see citing works
Relating matrix metalloproteinase structure to function: Why the “hemopexin” domain?
Murphy, G., & Knäuper, V. (1997) · Matrix Biology · doi:10.1016/s0945-053x(97)90025-1 · Cited by 306 · see citing works
MATRIX METALLOPROTEINASE-2 (MMP-2) AND MMP-9 IN PULMONARY PATHOLOGY
Chakrabarti, S., & Patel, K. D. (2005) · Experimental Lung Research · doi:10.1080/019021490944232 · Cited by 281 · see citing works
Active macropinocytosis induction by stimulation of epidermal growth factor receptor and oncogenic Ras expression potentiates cellular uptake efficacy of exosomes
Nakase, I., Kobayashi, N. B., Takatani‐Nakase, T., & Yoshida, T. (2015) · Scientific Reports · doi:10.1038/srep10300 · Cited by 271 · see citing works
Always cleave up your mess: targeting collagen degradation to treat tissue fibrosis
McKleroy, W., Lee, T., & Atabai, K. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00418.2012 · Cited by 263 · see citing works
Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains
Tulla, M., Pentikäinen, O. T., Viitasalo, T., Käpylä, J., Impola, U., Nykvist, P., Nissinen, L. M., Johnson, M. S., & Heino, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104058200 · Cited by 257 · see citing works
Collagen interactions: Drug design and delivery
An, B., Lin, Y., & Brodsky, B. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.013 · Cited by 245 · see citing works
Loss of MMP-2 disrupts skeletal and craniofacial development and results in decreased bone mineralization, joint erosion and defects in osteoblast and osteoclast growth
Mosig, R., Dowling, O., DiFeo, A. V., Ramirez, M. C. M., Parker, I. C., Abe, E., Diouri, J., Aqeel, A. A., Wylie, J. D., Oblander, S. A., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm060 · Cited by 240 · see citing works
Matrix metalloproteinases and collagen catabolism
Lauer‐Fields, J. L., Juska, D., & Fields, G. B. (2002) · Biopolymers · doi:10.1002/bip.10201 · Cited by 239 · see citing works
Generation of membrane structures during phagocytosis and chemotaxis of macrophages: role and regulation of the actin cytoskeleton
Rougerie, P., Miskolci, V., & Cox, D. (2013) · Immunological Reviews · doi:10.1111/imr.12118 · Cited by 237 · see citing works
Regulation of Collagenase Activities of Human Cathepsins by Glycosaminoglycans
Li, Z., Yasuda, Y., Li, W., Bogyo, M. S., Katz, N., Gordon, R. E., Fields, G. B., & Brömme, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310349200 · Cited by 235 · see citing works
Autophagy Promotes Intracellular Degradation of Type I Collagen Induced by Transforming Growth Factor (TGF)-β1
Kim, S. I., Na, H.-J., Ding, Y., Wang, Z., Lee, S., & Choi, M. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308460 · Cited by 233 · see citing works
Constitutive Macropinocytosis in Oncogene-transformed Fibroblasts Depends on Sequential Permanent Activation of Phosphoinositide 3-Kinase and Phospholipase C
Amyere, M., Payrastre, B., Krause, U., Smissen, P. V. D., Veithen, A., & Courtoy, P. J. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.10.3453 · Cited by 233 · see citing works
Action of rat liver cathepsin L on collagen and other substrates.
Kirschke, H., Kembhavi, A. A., Bohley, P., et al. (1982) · Biochemical Journal · doi:10.1042/bj2010367 · Cited by 223 · see citing works
Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1
Manka, S. W., Carafoli, F., Visse, R., Bihan, D. G., Raynal, N., Farndale, R. W., Murphy, G., Enghild, J. J., Hohenester, E., & Nagase, H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204991109 · Cited by 219 · see citing works
Fragments of human fibroblast collagenase. Purification and characterization
Clark, I. M., & Cawston, T. E. (1989) · Biochemical Journal · doi:10.1042/bj2630201 · Cited by 210 · see citing works
Autophagosomes, phagosomes, autolysosomes, phagolysosomes, autophagolysosomes… Wait, I’m confused
Klionsky, D. J., Eskelinen, E., & Deretic, V. P. (2014) · Autophagy · doi:10.4161/auto.28448 · Cited by 210 · see citing works
Interstitial Collagen Catabolism
Fields, G. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.451211 · Cited by 205 · see citing works
Pivotal Role of Cathepsin K in Lung Fibrosis
Bühling, F., Röcken, C., Brasch, F. E., Hartig, R., Yasuda, Y., Säftig, P., Brömme, D., & Welte, T. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63777-7 · Cited by 198 · see citing works
A Crucial Role for Matrix Metalloproteinase 2 in Osteocytic Canalicular Formation and Bone Metabolism
Inoue, K., Mikuni‐Takagaki, Y., Oikawa, K., Itoh, T., Inada, M., Noguchi, T., Park, J., Onodera, T., Krane, S. M., Noda, M., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607290200 · Cited by 197 · see citing works
Cathepsin K Is a Critical Protease in Synovial Fibroblast-Mediated Collagen Degradation
Hou, W.-S., Li, Z., Gordon, R. E., Chan, K. W. H., Klein, M. J., Levy, R., Keysser, M., Keyszer, G. M., & Brömme, D. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63068-4 · Cited by 190 · see citing works
uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion
Engelholm, L. H., List, K., Netzel–Arnett, S., Cukierman, E., Mitola, D. J., Aaronson, H., Kjøller, L., Larsen, J. K., Yamada, K. M., Strickland, D. K., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211091 · Cited by 183 · see citing works
Osteoclastic Bone Degradation and the Role of Different Cysteine Proteinases and Matrix Metalloproteinases: Differences Between Calvaria and Long Bone
Everts, V. E., Korper, W., Hoeben, K. A., Jansen, I. D. C., Brömme, D., Cleutjens, K. B. J. M., Heeneman, S., Peters, C., Reinheckel, T., Säftig, P., et al. (2006) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.060614 · Cited by 183 · see citing works
Self-citation
Radiocarbon dating reveals minimal collagen turnover in both healthy and osteoarthritic human cartilage
Heinemeier, K. M., Schjerling, P., Heinemeier, J., Møller, M. B., Krogsgaard, M. R., Grum-Schwensen, T. A., Petersen, M. M., & Kjær, M. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad8335 · Cited by 182 · see citing works
α11β1 Integrin Recognizes the GFOGER Sequence in Interstitial Collagens
Zhang, W., Käpylä, J., Puranen, J. S., Knight, C. G., Tiger, C., Pentikäinen, O. T., Johnson, M. S., Farndale, R. W., Heino, J., & Gullberg, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210313200 · Cited by 180 · see citing works
Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions
Mittal, R., Patel, A. P., Debs, L. H., Nguyen, D., Patel, K., Grati, M., Mittal, J., Yan, D., Chapagain, P., & Liu, X. Z. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25430 · Cited by 179 · see citing works
Detection of gingival crevicular fluid MMP-8 levels with different laboratory and chair-side methods
Sorsa, T. A., HernÃ¡ndez, M., Leppilahti, J. M., Munjal, S., Netuschil, L., & Mäntylä, P. (2009) · Oral Diseases · doi:10.1111/j.1601-0825.2009.01603.x · Cited by 177 · see citing works
Functional heterogeneity of osteoclasts: matrix metalloproteinases participate in osteoclastic resorption of calvarial bone but not in resorption of long bone
Everts, V. E., Korper, W., Jansen, D. C., Steinfort, J., Lammerse, I., Heera, S., Docherty, A. J. P., & Beertsen, W. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.10.1219 · Cited by 174 · see citing works
Self-citation
Collagenase Activity of Cathepsin K Depends on Complex Formation with Chondroitin Sulfate
Li, Z., Hou, W.-S., Escalante-Torres, C. R., Gelb, B. D., & Brömme, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204004200 · Cited by 172 · see citing works
Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor
Sheikh, H., Yarwood, H., Ashworth, A., & Isacke, C. M. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.6.1021 · Cited by 170 · see citing works
Transforming Growth Factor (TGF)-β Promotes de Novo Serine Synthesis for Collagen Production
Nigdelioglu, R., Hamanaka, R. B., Meliton, A. Y., O'Leary, E., Witt, L. J., Cho, T., Sun, K., Bonham, C., Wu, D., Woods, P. S., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.756247 · Cited by 169 · see citing works
Regulation of Membrane-type-1 Matrix Metalloproteinase Activity by Its Cytoplasmic Domain
Lehti, K., Valtanen, H., Wickström, S. A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910220199 · Cited by 165 · see citing works
Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase
Elkins, P. A., Ho, Y. S., Smith, W. W., Janson, C. A., D'Alessio, K. J., McQueney, M. S., Cummings, M. D., & Romanic, A. M. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902007849 · Cited by 158 · see citing works
Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains
Annabi, B., Lachambre, M., Bousquet-Gagnon, N., Pagé, M., Gingras, D., & Béliveau, R. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530547 · Cited by 154 · see citing works
Pathologic gene expression in Gaucher disease: up-regulation of cysteine proteinases including osteoclastic cathepsin K
Moran, M. T., Schofield, J. P., Hayman, A. R., Shi, G., Young, E. P., & Cox, T. M. (2000) · Blood · doi:10.1182/blood.v96.5.1969 · Cited by 153 · see citing works
Structural basis of collagen fiber degradation by cathepsin K
Aguda, A. H., Panwar, P., Du, X., Nguyen, N. T., Brayer, G. D., & Brömme, D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414126111 · Cited by 151 · see citing works
Calcium-sensing receptors signal constitutive macropinocytosis and facilitate the uptake of NOD2 ligands in macrophages
Canton, J., Schlam, D., Breuer, C., Gütschow, M., Glogauer, M., & Grinstein, S. (2016) · Nature Communications · doi:10.1038/ncomms11284 · Cited by 148 · see citing works
Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy
Curino, A. C., Engelholm, L. H., Yamada, S. S., Holmbeck, K., Lund, L. R., Molinolo, A. A., Behrendt, N., Nielsen, B. S., & Bugge, T. H. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200411153 · Cited by 146 · see citing works
Phagocytosis and digestion of collagen by gingival fibroblasts in vivo: A study of serial sections
Melcher, A. H., & Chan, J. (1981) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(81)80064-0 · Cited by 144 · see citing works
Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.
Exposito, J., & Garrone, R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.17.6669 · Cited by 142 · see citing works
Identification and Characterization of the Endocytic Transmembrane Glycoprotein Endo180 as a Novel Collagen Receptor
Wienke, D., MacFadyen, J. R., & Isacke, C. M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0814 · Cited by 142 · see citing works
A Urokinase Receptor-associated Protein with Specific Collagen Binding Properties
Behrendt, N., Jensen, O. N., Engelholm, L. H., Mørtz, E., Mann, M., & Danø, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.1993 · Cited by 141 · see citing works
Differential Expression of Matrix Metalloproteases in Human Fibroblasts with Different Origins
Lindner, D., Zietsch, C., Becher, P. M., Schulze, K., Schultheiss, H., Tschöpe, C., & Westermann, D. (2012) · Biochemistry Research International · doi:10.1155/2012/875742 · Cited by 138 · see citing works
Beta2-adrenergic receptor regulates cardiac fibroblast autophagy and collagen degradation
Aránguiz, P., Canales, J., Copaja, M., Troncoso, R., Vicencio, J. M., Carrillo, C., Lara, H., Lavandero, S., & Dı́az-Araya, G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.07.003 · Cited by 137 · see citing works
Matrix Metalloproteinase-14 Deficiency in Bone Marrow–Derived Cells Promotes Collagen Accumulation in Mouse Atherosclerotic Plaques
Schneider, F. M., Sukhova, G. K., Aikawa, M., et al. (2008) · Circulation · doi:10.1161/circulationaha.107.707448 · Cited by 134 · see citing works
Osteoclast formation and differentiation: an overview.
Soysa, N. S., Alles, N., Aoki, K., & Ohya, K. (2012) · PubMed · Cited by 126 · see citing works
Synthesis and secretion of collagen by cells of connective tissue, bone, and dentin
Leblond, C. P. (1989) · The Anatomical Record · doi:10.1002/ar.1092240204 · Cited by 126 · see citing works
TNF-α inactivation of collagen receptors: implications for fibroblast function and fibrosis
Chou, D., Lee, W., & McCulloch, C. A. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.11.4354 · Cited by 125 · see citing works
STUDIES ON CARTILAGE
Sheldon, H., & Fb, K. (1962) · The Journal of Cell Biology · doi:10.1083/jcb.12.3.599 · Cited by 119 · see citing works
A Novel Model System for Characterization of Phagosomal Maturation, Acidification, and Intracellular Collagen Degradation in Fibroblasts
Arora, P. D., Manolson, M. F., Downey, G. P., Sodek, J., & McCulloch, C. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003221200 · Cited by 115 · see citing works
The Non-phagocytic Route of Collagen Uptake
Madsen, D. H., Ingvarsen, S. Z., Jürgensen, H. J., Melander, M. C., Kjøller, L., Moyer, A., Honoré, C., Madsen, C. A., Garred, P., Burgdorf, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208033 · Cited by 113 · see citing works
Cell Surface Collagenolysis Requires Homodimerization of the Membrane-bound Collagenase MT1-MMP
Itoh, Y., Ito, N., Nagase, H., et al. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-08-0740 · Cited by 112 · see citing works
A Critical Role for the Membrane-type 1 Matrix Metalloproteinase in Collagen Phagocytosis
Lee, H., Overall, C. M., McCulloch, C. A., & Sodek, J. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-06-0486 · Cited by 111 · see citing works
Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains
Annabi, B., Lachambre, M., Bousquet-Gagnon, N., et al. (2001) · Biochemical Journal · doi:10.1042/bj3530547 · Cited by 111 · see citing works
Collagen and tissue turnover as a function of age: Implications for fibrosis
Karsdal, M. A., Genovese, F., Madsen, E. A., et al. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.08.014 · Cited by 107 · see citing works
Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis
Shi, J., Son, M.-Y., Yamada, S., Szabova, L., Kahan, S., Chrysovergis, K., Wolf, L., Surmak, A., & Holmbeck, K. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2007.10.017 · Cited by 107 · see citing works
A helping hand for collagenases: the haemopexin-like domain
Bode, W. (1995) · Structure · doi:10.1016/s0969-2126(01)00185-x · Cited by 107 · see citing works
uPARAP/endo180 directs lysosomal delivery and degradation of collagen IV
Kjøller, L., Engelholm, L. H., Høyer-Hansen, M. H., et al. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.008 · Cited by 106 · see citing works
Characterization of a truncated recombinant form of human membrane type 3 matrix metalloproteinase
Shimada, T., Nakamura, H., Ohuchi, E., Fujii, Y., Murakami, Y., Sato, H., Seiki, M., & Okada, Y. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00459.x · Cited by 103 · see citing works
Obituary Notice
Russell, E. J. (1921) · Biochemical Journal · doi:10.1042/bj0150001 · Cited by 103 · see citing works
Effects of the proteinase inhibitors leupeptin and E-64 on osteoclastic bone resorption
Everts, V. E., Beertsen, W., & Schröder, R. (1988) · Calcified Tissue International · doi:10.1007/bf02571316 · Cited by 98 · see citing works
Self-citation
Clara cell adhesion and migration to extracellular matrix
Atkinson, J. J., Adair-Kirk, T. L., Kelley, D. G., deMello, D. E., & Senior, R. M. (2008) · Respiratory Research · doi:10.1186/1465-9921-9-1 · Cited by 94 · see citing works
Role of Cathepsin K in the Turnover of the Dermal Extracellular Matrix during Scar Formation
Rünger, T. M., Quintanilla‐Dieck, M. J., & Bhawan, J. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700535 · Cited by 92 · see citing works
The Digestion of Phagocytosed Collagen is Inhibited by the Proteinase Inhibitors Leupeptin and E-64
Everts, V. E., Beertsen, W., & Tigchelaar‐Gutter, W. (1985) · Collagen and Related Research · doi:10.1016/s0174-173x(85)80021-2 · Cited by 91 · see citing works
Self-citation
Inflammatory Stimuli Reprogram Macrophage Phagocytosis to Macropinocytosis for the Rapid Elimination of Pathogens
Dasgupta, S. B., & Pieters, J. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003879 · Cited by 90 · see citing works
Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis
Morko, J. P., Söderström, M., Säämänen, A.-M. K., Salminen, H. J., & Vuorio, E. I. (2004) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2002.004671 · Cited by 89 · see citing works
Molecular basis for MMP9 induction and disruption of epithelial cell-cell contacts by galectin-3
Mauris, J., Woodward, A. M., Cao, Z., Panjwani, N., & Argüeso, P. (2014) · Journal of Cell Science · doi:10.1242/jcs.148510 · Cited by 89 · see citing works
Complementary Roles of Intracellular and Pericellular Collagen Degradation Pathways In Vivo
Wagenaar-Miller, R. A., Engelholm, L. H., Gavard, J., Yamada, S. S., Gutkind, J. S., Behrendt, N., Bugge, T. H., & Holmbeck, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00291-07 · Cited by 85 · see citing works
The collagen receptor uPARAP/Endo180 in tissue degradation and cancer (Review)
Melander, M. C., Jürgensen, H. J., Madsen, D. H., et al. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3120 · Cited by 81 · see citing works
The C-type Lectin Receptor Endo180 Displays Internalization and Recycling Properties Distinct from Other Members of the Mannose Receptor Family
Howard, M. J., & Isacke, C. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203631200 · Cited by 81 · see citing works
Diffusion of MMPs on the Surface of Collagen Fibrils: The Mobile Cell Surface – Collagen Substratum Interface
Collier, I. E., Legant, W. R., Marmer, B. L., Lubman, O., Saffarian, S., Wakatsuki, T., Elson, E. L., & Goldberg, G. I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024029 · Cited by 80 · see citing works
Physiology and pathology of collagen receptors
Popova, S. N., Evy Lundgren-akerlund, B., Wiig, H., & Gullberg, D. (2007) · Acta Physiologica · doi:10.1111/j.1748-1716.2007.01718.x · Cited by 79 · see citing works
Direct Visualization of Protease Action on Collagen Triple Helical Structure
Rosenblum, G., den Steen, P. E. V., Cohen, S., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011043 · Cited by 78 · see citing works
Defining Requirements for Collagenase Cleavage in Collagen Type III Using a Bacterial Collagen System
Yu, Z., Visse, R., Inouye, M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348979 · Cited by 78 · see citing works
Overexpression of cathepsin K during silica-induced lung fibrosis and control by TGF-β
van den Brûle, S., Misson, P., Bühling, F., Lison, D., & Huaux, F. (2005) · Respiratory Research · doi:10.1186/1465-9921-6-84 · Cited by 74 · see citing works
Astragaloside IV controls collagen reduction in photoaging skin by improving transforming growth factor-β/Smad signaling suppression and inhibiting matrix metalloproteinase-1
Chen, B., Li, R., YAN, N., CHEN, G., Qian, W., JIANG, H.-L., Ji, C., & Bi, Z. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3212 · Cited by 69 · see citing works
Matrix Metalloproteinase Dependent and Independent Collagen Degradation
Song, F. (2006) · Frontiers in bioscience · doi:10.2741/2036 · Cited by 67 · see citing works
Characterisation of Cathepsin B and Collagenolytic Cathepsin from Human Placenta
Evans, P., & Etherington, D. J. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12071.x · Cited by 66 · see citing works
Spontaneous development of synovitis and cartilage degeneration in transgenic mice overexpressing cathepsin K
Morko, J. P., Kiviranta, R., Joronen, K. M., et al. (2005) · Arthritis & Rheumatism · doi:10.1002/art.21423 · Cited by 66 · see citing works
Overexpression of cathepsin K in mice decreases collagen deposition and lung resistance in response to bleomycin-induced pulmonary fibrosis
Srivastava, M., Steinwede, K., Kiviranta, R., et al. (2008) · Respiratory Research · doi:10.1186/1465-9921-9-54 · Cited by 66 · see citing works
Gelatin-binding Region of Human Matrix Metalloproteinase-2
Briknarová, K., Gehrmann, M. L., Bányai, L., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101105200 · Cited by 60 · see citing works
Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
Wavre-Shapton, S. T., Meschede, I. P., Seabra, M. C., & Futter, C. E. (2014) · Journal of Cell Science · doi:10.1242/jcs.154757 · Cited by 60 · see citing works
Does collagen trigger the recruitment of osteoblasts into vacated bone resorption lacunae during bone remodeling?
Abdelgawad, M. E., Søe, K., Andersen, T. L., Merrild, D. M. H., Christiansen, P., Kjærsgaard‐Andersen, P., & Delaissé, J. (2014) · Bone · doi:10.1016/j.bone.2014.07.012 · Cited by 58 · see citing works
Membrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model
Atkinson, S. J., Patterson, M. L., Butler, M. J., & Murphy, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02204-9 · Cited by 55 · see citing works
Endocytic collagen degradation: a novel mechanism involved in protection against liver fibrosis
Madsen, D. H., Jürgensen, H. J., Ingvarsen, S., Melander, M. C., Vainer, B., Egerod, K. L., Hald, A., Rønø, B., Madsen, C. A., Bugge, T. H., et al. (2012) · The Journal of Pathology · doi:10.1002/path.3981 · Cited by 53 · see citing works
The “love–hate” relationship between osteoclasts and bone matrix
Rucci, N., & Teti, A. M. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.02.009 · Cited by 51 · see citing works
Insight into the Degradation of Type-I Collagen Fibrils by MMP-8
Lu, K. G., & Stultz, C. M. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.002 · Cited by 44 · see citing works
Changes in collagen cross‐linking in bleomycin‐induced pulmonary fibrosis
Reiser, K. M., Tryka, A. F., Lindenschmidt, R. C., et al. (1986) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.2570010109 · Cited by 44 · see citing works
Inhibition of macropinocytosis blocks antigen presentation of type II collagen in vitro and in vivo in HLA-DR1 transgenic mice
von Delwig, A., Hilkens, C., Altmann, D., Holmdahl, R., Isaacs, J., Harding, C., Robertson, H., Mckie, N., & Robinson, J. (2006) · Arthritis Research & Therapy · doi:10.1186/ar1964 · Cited by 42 · see citing works
Neutrophil Response following Intratracheal Instillation of Collagen Peptides into Rat Lungs
Riley, D. J., Berg, R. A., Soltys, R. A., et al. (1988) · Experimental Lung Research · doi:10.3109/01902148809087827 · Cited by 42 · see citing works
Anti-inflammatory activities of Physalis alkekengi var. franchetii extract through the inhibition of MMP-9 and AP-1 activation
Hong, J., Kwon, O., Shin, I., et al. (2014) · Immunobiology · doi:10.1016/j.imbio.2014.10.004 · Cited by 42 · see citing works
Differential Expression of Chemokines, Chemokine Receptors and Proteinases by Foreign Body Giant Cells (FBGCs) and Osteoclasts
Khan, U. A., Hashimi, S. M., Khan, S., Quan, J., Bakr, M. M., Forwood, M. R., & Morrison, N. A. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24781 · Cited by 42 · see citing works
The binding capacity of α1β1-, α2β1- and α10β1-integrins depends on non-collagenous surface macromolecules rather than the collagens in cartilage fibrils
Woltersdorf, C., Bonk, M., Leitinger, B., Huhtala, M. T., Käpylä, J., Heino, J., Girol, C. G., Niland, S., Eble, J. A., Brückner, P., et al. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.02.001 · Cited by 40 · see citing works
Localization of cathepsin B activity in fibroblasts and chondrocytes by continuous monitoring of the formation of a final fluorescent reaction product using 5-nitrosalicylaldehyde
Noorden, C. J. F. V., Vogels, I. M. C., Everts, V. E., & Beertsen, W. (1987) · The Histochemical Journal · doi:10.1007/bf01675418 · Cited by 39 · see citing works
Self-citation
CXCL12-induced macropinocytosis modulates two distinct pathways to activate mTORC1 in macrophages
Pacitto, R., Gaeta, I., Swanson, J. A., & Yoshida, S. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.2a0316-141rr · Cited by 39 · see citing works
Increased collagen production in fibroblasts cultured from irradiated skin and effect of TGF β1– clinical study
Illsley, M. C., Peacock, J. H., McAnulty, R. J., et al. (2000) · British Journal of Cancer · doi:10.1054/bjoc.2000.1321 · Cited by 38 · see citing works
Insights into Collagen Uptake by C-type Mannose Receptors from the Crystal Structure of Endo180 Domains 1–4
Paracuellos, P., Briggs, D. C., Carafoli, F., et al. (2015) · Structure · doi:10.1016/j.str.2015.09.004 · Cited by 36 · see citing works
Cellular sensitivity to collagen in bleomycin-treated rats.
Schrier, D. J., Phan, S. H., & Ward, P. A. (1982) · The Journal of Immunology · doi:10.4049/jimmunol.129.5.2156 · Cited by 32 · see citing works
Differential Actions of the Endocytic Collagen Receptor uPARAP/Endo180 and the Collagenase MMP-2 in Bone Homeostasis
Madsen, D. H., Jürgensen, H. J., Ingvarsen, S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071261 · Cited by 32 · see citing works
Rap1 Activation in Collagen Phagocytosis Is Dependent on Nonmuscle Myosin II-A
Arora, P. D., Conti, M. A., Ravid, S., Sacks, D. B., Kapùs, A., Adelstein, R. S., Bresnick, A. R., & McCulloch, C. A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-04-0430 · Cited by 31 · see citing works
Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions
Arora, P. D., Wang, Y., Bresnick, A., Dawson, J. F., Janmey, P., & McCulloch, C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0754 · Cited by 30 · see citing works
Regulation of autophagy by extracellular matrix glycoproteins in HeLa cells
Tuloup-Minguez, V., Greffard, A., Codogno, P., et al. (2010) · Autophagy · doi:10.4161/auto.7.1.13851 · Cited by 29 · see citing works
Matrix metalloproteinases and their inhibitors in non-neoplastic otorhinolaryngological disease
De, S., Fenton, J. E., & Jones, A. S. (2005) · The Journal of Laryngology & Otology · doi:10.1258/0022215054273269 · Cited by 28 · see citing works
Distribution of Endo180 receptor and ligand in developing articular cartilage
Howard, M. J., Chambers, M. G., Mason, R. M., et al. (2003) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2003.07.001 · Cited by 28 · see citing works
An ultrastructural study of phagocytosis in bone by osteoblastic cells from fetal mouse calvaria in vitro
Takahashi, T., Kurihara, N., Takahashi, K., et al. (1986) · Archives of Oral Biology · doi:10.1016/0003-9969(86)90101-9 · Cited by 27 · see citing works
Diagnostic value of matrix metalloproteinase 9 and tissue inhibitor of matrix metalloproteinases 1 in cholesteatoma.
Olszewska, E., Matulka, M., Mroczko, B., et al. (2016) · PubMed · doi:10.14670/hh-11-677 · Cited by 23 · see citing works
Collagen phagocytosis by stimulated mouse periotoneal macrophages in vitro
Deporter, D. A. (1979) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1979.tb00796.x · Cited by 19 · see citing works
Endocytosis of collagen by hepatic stellate cells regulates extracellular matrix dynamics
Bi, Y., Mukhopadhyay, D., Drinane, M. C., Ji, B., Li, X., Cao, S., & Shah, V. H. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00086.2014 · Cited by 18 · see citing works
Phagocytosis of Collagen Fibrils by Fibroblasts In Vivo Is Independent of the uPARAP/Endo180 Receptor
Sprangers, S., Behrendt, N., Engelholm, L. H., Cao, Y., & Everts, V. E. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25821 · Cited by 17 · see citing works
Self-citation
Cysteine Cathepsins and the Skeleton
Brömme, D. (2011) · Clinical Reviews in Bone and Mineral Metabolism · doi:10.1007/s12018-011-9101-y · Cited by 7 · see citing works

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Meyer, M. (2019) · BioMedical Engineering OnLine · doi:10.1186/s12938-019-0647-0 · Cited by 539 · see citing works
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Bolamperti, S., Villa, I., & Rubinacci, A. (2022) · Bone Research · doi:10.1038/s41413-022-00219-8 · Cited by 482 · see citing works
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Bourgot, I., Primac, I., Louis, T., Noël, A., & Maquoi, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01488 · Cited by 113 · see citing works
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Zhao, P., Sun, T., Lyu, C., Liang, K., & Du, Y. (2023) · Cell Regeneration · doi:10.1186/s13619-023-00172-9 · Cited by 48 · see citing works
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Gan, C., Yaqoob, U., Lu, J., Xie, M., Anwar, A., Jalan-Sakrikar, N., Jerez, S., Sehrawat, T. S., Navarro-Corcuera, A., Kostallari, E., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.174775 · Cited by 21 · see citing works

Influence of extracellular ion concentration on the intracellular accumulation of adriamycin.
Nishikawa, K., Asaumi, J. I., Kawasaki, S., et al. (1998) · PubMed
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Caner, A., Bıtgen, N., & Önal, M. G. (2019) · International Journal of Medical Research & Health Sciences
Interaction of extracellular calcium and magnesium in the regulation of cytosolic calcium and PTH release in dispersed bovine parathyroid cells
Shoback, D., Thatcher, J., & Brown, E. M. (1984) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(84)90116-3 · Cited by 26 · see citing works
EXTRACELLULAR POTENTIALS FROM SINGLE SPINAL MOTONEURONS
Freygang, W. H., & Frank, K. (1959) · The Journal of General Physiology · doi:10.1085/jgp.42.4.749 · Cited by 113 · see citing works
Enhancement of intracellular calcium concentration by extracellular ATP and UTP in madin darby canine kidney cells
Paulmichl, M., & Lang, F. J. W. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80751-4 · Cited by 36 · see citing works

Authors: Sprangers, S., & Everts, V.
Affiliations: Academic Center for Dentistry Amsterdam (NL)
Corresponding author: Everts, Vincent
ORCID: Sprangers, Sara
Everts, Vincent
Venue: Matrix Biology
Publisher: Elsevier BV
Published: 2019-01
Volume: 75-76
Pages: 190-200
ISSN: 0945-053X (ISSN-L)
DOI: 10.1016/j.matbio.2017.11.008
OpenAlex: W2770784319
Cited by: 102
References: 145
Citations by year: 2026: 11 · 2025: 12 · 2024: 14 · 2023: 16 · 2022: 13 · 2021: 14 · 2020: 13 · 2019: 5 · 2018: 4
FWCI: 0.61
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Matrix Biology (publishedVersion)
PubMed (publishedVersion)
VU Research Portal (submittedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Keywords: fibrillar collagen, collagen degradation, extracellular matrix, collagen turnover, connective tissue, collagen synthesis, matrix metalloproteinases, cell types
MeSH terms: Cartilage, Connective Tissue, Extracellular Matrix, Humans, Skin, Fibrillar Collagens, Metabolic Networks and Pathways, Proteolysis

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Molecular pathways of cell-mediated degradation of fibrillar collagen

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