Type III collagen COL3
Type III collagen(COL3) is a fibrillar-forming collagen comprising 3 alpha-1(III) chains and is expressed in early embryos and throughout embryogenesis.
In adult, type III collagen is a major component of the extracellular matrix in a variety of internal organs and skin.
Type III collagen, first identified and described in 1971 (Miller et al., 1971), is an important structural protein.
Classified as one of the major fibrillar collagens (Prockop and Kivirikko, 1995).
It constitutes about 5–20% of the entire collagen content in the human body (Miller, 1988).
Type III collagen is a fibrillar collagen, and it consists of only one collagen α chain, in contrast to most other collagens.
It is a homotrimer containing three A1(III) chains supercoiled around each other in a right-handed triple helix.
Type III collagen is secreted by fibroblasts and other mesenchymal cell types, thus making it a major player in various inflammation-associated pathologies such as lung injury, viral and nonviral liver diseases, kidney fibrosis, hernia, and vascular disorders. Type III collagen together with type I collagen are the main constituents of the interstitial matrix.
Type III collagen mutations are associated with Ehlers–Danlos syndrome, vascular deficiency, and aortic and arterial aneurysms.
Several biomarkers for type III collagen formation and degradation have been developed and used extensively.
In particular, for fibrosis, type III collagen formations have proven valuable.
ELISA kits are a quick, convenient, and accurate research tool for the detection and quantitation of targets of interest in cultures and samples. …
These ELISA kits include pre-coated plates with capture/detection antibodies, standards, buffers and accessory reagents.
This gene encodes the pro-alpha1 chains of type III collagen (COL3A1). A fibrillar collagen that is found in extensible connective tissues such as skin, lung, uterus, intestine and the vascular system, frequently in association with type I collagen.
Mutations in this gene are associated with Ehlers-Danlos syndrome types IV, and with aortic and arterial aneurysms.
Jorgensen et al. (2015) noted that the fourth exon in the COL3A1 gene (residues 112 to 149 of the protein).Appears to have fused the sequences equivalent to exons 4 and 5 in other fibrillar collagens.
Thus, it is named exon 4/5 and the subsequent exon is designated exon 6.