Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators

By K. Kadler, Adele Hill, E. Canty-Laird. Current Opinion in Cell Biology, 2008

741 citations recorded by the source corpus.

Collagens are triple helical proteins that occur in the extracellular matrix (ECM) and at the cell–ECM interface. There are more than 30 collagens and collagen-related proteins but the most abundant are collagens I and II that exist as D-periodic (where D = 67 nm) fibrils. The fibrils are of broad biomedical importance and have central roles in embryogenesis, arthritis, tissue repair, fibrosis, tumor invasion, and cardiovascular disease. Collagens I and II spontaneously form fibrils in vitro, which shows that collagen fibrillogenesis is a selfassembly process. However, the situation in vivo is not that simple; collagen I-containing fibrils do not form in the absence of fibronectin, fibronectin-binding and collagen-binding integrins, and collagen V. Likewise, the thin collagen II-containing fibrils in cartilage do not form in the absence of collagen XI. Thus, in vivo, cellular mechanisms are in place to control what is otherwise a protein self-assembly process. This review puts forward a working hypothesis for how fibronectin and integrins (the organizers) determine the site of fibril assembly, and collagens V and XI (the nucleators) initiate collagen fibrillogenesis.

Subfields: Biomaterials, Immunology and Allergy, Rheumatology

View Paper: https://www.semanticscholar.org/paper/f0d987c49cb2678490cd386efaf3d644a2639091

How researchers see this paper

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In Biomaterials

1. Lisa J. White
2. S. Velankar
3. Madeline C. Cramer
4. Lindsey T. Saldin
5. Sylvie Ricard-Blum
6. S. Badylak
7. P. Ma

In Immunology and Allergy

1. C. Carraher
2. Purva Singh
3. Sylvie Ricard-Blum
4. J. Schwarzbauer

Citations in the corpus

• Extracellular Matrix Hydrogels from Decellularized Tissues: Structure and Function (2016, positive): “contribute to collagen polymerization: fibronectin is known to organize collagen fibers, and minor collagens (collagen V and XI) are nucleation sites that must be present for collagen fibrillogenesis in vivo [48].”
• Tissue Stiffness Dictates Development, Homeostasis, and Disease Progression (2015, background): “Fibronectin fibrils incorporate directly into the ECM through specific heparin, fibrin, and collagen binding domains, and it has been shown that in vivo fibrillar collagen formation is dependent on binding and subsequent conformational changes in fibronectin.(74) This increases the percentage of lin”
• Assembly of Fibronectin Extracellular Matrix (2010, background): “Application of image reconstruction techniques further defined these compartments and, because of their role in collagen fibril deposition, the name “fibripositor” has been coined (Kadler et al. 2008).”
• Matrix MetalloProteinases (MMPs) andTissue Inhibitors of MetalloProteinases (TIMPs): positive and negative regulators intumor cell adhesion (2010, neutral): “Detailed description of matrix protein family members, their functions and role in human pathologies are provided in recent reviews [17–21].”
• The collagen family. (2011, background): “Fibronectin and integrins could act as organizers, and collagens Vand XI as nucleators for fibrillogenesis of collagens I and II (Kadler et al. 2008).”