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| Collagen type I | |
|---|---|
| Name | Collagen type I |
| Location | Extracellular matrix |
Collagen type I Collagen type I is the most abundant fibrillar collagen in vertebrates, forming robust fibers that provide tensile strength to connective tissues such as skin, bone, tendon, and ligaments. It is a heterotrimer composed of two alpha-1 chains and one alpha-2 chain encoded by the human genes COL1A1 and COL1A2, with conserved triple-helical Gly-X-Y repeats crucial for its structural integrity.
Type I collagen assembles into right-handed triple helices from left-handed polyproline II-type chains, producing D-periodic banded fibrils visible by electron microscopy in specimens from Smithsonian Institution, The British Museum, Louvre, and Metropolitan Museum of Art collections of natural history. The primary sequence includes repeating Gly-X-Y motifs where X and Y are often proline and hydroxyproline; mutations affecting glycine residues were characterized in studies at University of Oxford, Harvard University, Stanford University, Massachusetts Institute of Technology and Max Planck Society. Fibrillogenesis is influenced by non-collagenous domains and crosslinking mediated by lysyl oxidase studied at Karolinska Institutet, Imperial College London, ETH Zurich, University of Tokyo and California Institute of Technology. Supramolecular organization into fibers integrates with extracellular matrices observed in specimens cataloged by Natural History Museum, London, American Museum of Natural History, and clinical imaging from Mayo Clinic, Cleveland Clinic, and Johns Hopkins Hospital.
The biosynthetic pathway in fibroblasts and osteoblasts involves transcriptional regulation at promoters analyzed by researchers at National Institutes of Health, Wellcome Trust, Howard Hughes Medical Institute, European Molecular Biology Laboratory and Cold Spring Harbor Laboratory. Translation generates procollagen molecules that undergo signal peptide cleavage, propeptide removal, and extensive hydroxylation of proline and lysine residues by prolyl-4-hydroxylase and lysyl hydroxylase enzymes characterized in work from Yale University, University of Cambridge, Johns Hopkins University, UCSF, and University of California, San Diego. Glycosylation of hydroxylysine, disulfide bond formation, and formation of intramolecular and intermolecular crosslinks catalyzed by Lysyl oxidase family members are implicated in pathologies investigated by teams at University College London, Duke University, Karolinska Institutet, University of Pennsylvania, and University of Zurich. Vitamin C (ascorbic acid) is an essential cofactor whose deficiency was linked to historical clinical descriptions by explorers in archives of Royal Society, British Library, Wellcome Collection, National Library of Medicine, and Bibliothèque nationale de France.
Type I collagen predominates in dermis, cortical bone, tendon, and ligaments; its distribution maps have been reported in atlases produced by World Health Organization, National Institutes of Health, European Society of Cardiology, American Heart Association, and International Osteoporosis Foundation. It forms the organic matrix for mineral deposition by osteoblasts in processes studied at Karolinska Institutet, University of Michigan, University of Toronto, University of Sydney, and Peking University. In wound healing, interactions with integrins and matricellular proteins were elucidated in collaborations including Fred Hutchinson Cancer Center, Memorial Sloan Kettering Cancer Center, Roswell Park Comprehensive Cancer Center, Dana-Farber Cancer Institute, and Salk Institute. Type I collagen also modulates cell behavior via mechanotransduction pathways explored at Massachusetts Institute of Technology, ETH Zurich, California Institute of Technology, Imperial College London, and University of California, Berkeley.
Mechanical characterization—tensile strength, stiffness, viscoelasticity—has been quantified using methods from laboratories at MIT, Caltech, ETH Zurich, Imperial College London, and University of Cambridge. Hierarchical structure, from molecular triple helix to fibril and fiber, confers high tensile modulus comparable to engineered composites studied at NASA, European Space Agency, Boeing, Airbus, and Siemens. Crosslink density and post-translational modification patterns alter fracture toughness and creep behavior reported in studies by National Aeronautics and Space Administration, Oak Ridge National Laboratory, Lawrence Berkeley National Laboratory, Argonne National Laboratory, and Sandia National Laboratories. Mechanical loading influences remodeling via signaling pathways investigated at Howard Hughes Medical Institute, Wellcome Trust Sanger Institute, Ragon Institute, GE Healthcare, and Philips research centers.
Mutations in COL1A1 and COL1A2 cause osteogenesis imperfecta and connective tissue disorders described in clinical series from Mayo Clinic, Cleveland Clinic, Great Ormond Street Hospital, Hospital for Special Surgery, and Boston Children's Hospital. Aberrant collagen deposition contributes to fibrosis in organs studied by National Cancer Institute, American Lung Association, European Respiratory Society, American Liver Foundation, and Kidney Research UK. Age-related changes in collagen influence skin aging and were analyzed in trials at Harvard Medical School, Stanford School of Medicine, University of Pennsylvania Perelman School of Medicine, Johns Hopkins School of Medicine, and Columbia University Irving Medical Center. Oncologic interactions with tumor microenvironments implicate collagen remodeling in metastasis research at MD Anderson Cancer Center, Memorial Sloan Kettering Cancer Center, Karolinska Institutet, Institut Curie, and German Cancer Research Center.
Type I collagen is used as biomaterial for scaffolds, grafts, and tissue engineering developed by companies and institutions including Johnson & Johnson, Medtronic, Stryker Corporation, Zimmer Biomet, and Baxter International. Recombinant and purified collagens are produced and tested in collaborations involving Genentech, Amgen, Novo Nordisk, Thermo Fisher Scientific, and GE Healthcare Life Sciences. Clinical applications include hemostatic sponges, dermal fillers, and bone graft substitutes approved in trials at Food and Drug Administration, European Medicines Agency, National Institute for Health and Care Excellence, Health Canada, and Therapeutic Goods Administration. Advanced research integrates collagen matrices with stem cell therapies from Wake Forest Institute for Regenerative Medicine, Salk Institute, Karolinska Institutet, Riken, and RIKEN Center for Integrative Medical Sciences for regenerative medicine, biofabrication, and soft robotics projects supported by National Science Foundation, European Commission, Horizon Europe, Wellcome Trust, and Bill & Melinda Gates Foundation.
Category:Collagens