|collagen, type I, alpha 1|
|Locus||Chr. 17 q21.3-q22|
|collagen, type I, alpha 2|
|Locus||Chr. 7 q21.3-22.1|
Type I collagen is the most abundant collagen of the human body. It forms large, eosinophilic fibers known as collagen fibers. It is present in scar tissue, the end product when tissue heals by repair, as well as tendons, ligaments, the endomysium of myofibrils, the organic part of bone, the dermis, the dentin, and organ capsules.
The COL1A1 gene produces the pro-alpha1(I) chain. This chain combines with another pro-alpha1(I) chain and also with a pro-alpha2(I) chain (produced by the COL1A2 gene) to make a molecule of type I pro-collagen. These triple-stranded, rope-like pro-collagen molecules must be processed by enzymes outside the cell. Once these molecules are processed, they arrange themselves into long, thin fibrils that cross-link to one another in the spaces around cells. The cross-links result in the formation of very strong mature type I collagen fiber.
Markers used to measure bone loss are not easily testable. Degradation of type 1 collagen releases metabolites that can be used to monitor resorption.
- Type II collagen
- Collagen, type I, alpha 1
- Collagen, type I, alpha 2
- Collagen, type III, alpha 1
- Ting, Kay R. (2016). "Clinical Utility of C‐Terminal Telopeptide of Type 1 Collagen in Multiple Myeloma". British Journal of Haematology. 173 (1): 82–88. doi:10.1111/bjh.13928. PMID 26787413.