English
General description
Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Do not confuse Sigma type designations with recognized collagen classification types.
Collagen is made of three polypeptide chains.[1] Type 2 collagen is ubiquitously present in the hyaline cartilage. It is a homotrimer made of three α1[2] chains.[1] Type 2 collagen is also predominant in nucleus pulposus of the vertebral disc and vitreous body of the eye.[2] The proteoglycan obtained from the chicken sternal cartilage is similar to type nine collagen structure.[3]
Application
Collagen from chicken sternal cartilage has been used:
in enzyme–linked immunosorbent assay (ELISA).[4]
chondrocyte-mediated tissue production in vitro.[5]
induction, treatment, and assessment of collagenα induced arthritis (CIA). [6][7]
cell proliferation assay.[8]
as a coating for cell culture surfaces.[8]
Biochem/physiol Actions
Collagen breaks down metabolically in the body to release N-telopeptide, which is the N-terminus of collagen. There is also C-telopeptide, which is presumably the C-terminus. N-telopeptide is released in urine, and its detection in diagnostic tests is used to screen for osteoporosis.
Features and Benefits
This collagen has been tested in culture with mammalian cells to verify it is low in endotoxin content.
Preparation Note
Prepared by a modification of the method of Trentham, D.E., et al.
Other Notes
Major component of articular cartilage.
