Anti-Collagen V antibody [EPR23762-54]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Collagen V also known as collagen type V is a fibrillar collagen integral to the formation and structure of the extracellular matrix. It plays a mechanical role by regulating the assembly of other fibrillar collagens such as type I. Collagen V is a heterotrimer composed of three alpha chains—two α1(V) and one α2(V)—and demonstrates a molecular weight that typically ranges between 180-200 kDa. Expression of collagen type 5 is prominent in connective tissues especially those found in skin tendon and cornea where it ensures proper collagen fibril formation and tissue stability.

Biological function summary

Collagen V coordinates with other collagen types to control fibrillogenesis the process by which collagen molecules assemble into fibrils. It exists as part of a complex within the extracellular matrix often found interacting with collagen type I influencing its diameter and the organization of fibrils. This involvement is important for maintaining the structural integrity and mechanical properties of tissues that require a well-organized fibrillar network like the sclera and the dermis.

Pathways

Collagen V participates in the regulation of the collagen biosynthesis and degradation pathway as well as the TGF-β signaling pathway. It modulates the biosynthesis pathway by ensuring a controlled assembly and deposition of collagen fibrils which is essential for tissue repair and maintenance. Through its influence on the TGF-β signaling pathway collagen type V interacts with proteins such as decorin and biglycan which are also associated with modulating collagen fibril formation and tissue morphogenesis.

Associated diseases and disorders

Collagen V defects or imbalances can lead to conditions such as Ehlers-Danlos syndrome (EDS) and fibrosis. EDS is associated with mutations in the COL5A1 or COL5A2 genes leading to abnormal collagen V production which affects skin elasticity and joint integrity. Fibrosis involves excessive collagen deposition including collagen type V resulting in tissue stiffening and impaired function. In these disorders surrounding collagens and matrix proteins like decorin may be altered further exacerbating tissue dysfunction.