Collagen can be plentiful in corneas, blood vessels, the intestine, intervertebral discs, and the dentin in tooth.[3] In muscle tissue, it serves as a serious element of the endomysium. Collagen constitutes one to 2 p.c of muscle tissue and accounts for six% of the burden of robust, tendinous muscle mass.[4] The fibroblast is the most typical cell that creates collagen. Relying upon the diploma of mineralization, collagen tissues could also be inflexible (bone) or compliant (tendon) or have a gradient from inflexible to compliant (cartilage).
(*5*)Contents
(*5*)Etymology[edit]
The title collagen comes from the Greek κόλλα (kólla), that means “glue”, and suffix -γέν, -gen, denoting “producing”.[6][7]
(*5*)Human varieties[edit]
The 5 commonest varieties are:[11]
(*5*)Medical makes use of[edit]
All through the 4 phases of wound therapeutic, collagen performs the next features in wound therapeutic:
(*5*)Fundamental analysis[edit]
Collagen is utilized in laboratory research for cell tradition, finding out cell habits and mobile interactions with the extracellular setting.[25]
(*5*)Biology[edit]
The commonest motifs within the amino acid sequence of collagen are glycine-proline-X and glycine-X-hydroxyproline, the place X is any amino acid apart from glycine, proline or hydroxyproline. The collagen protein consists of a triple helix, which usually consists of two similar chains (α1) and a further chain that differs barely in its chemical composition (α2).[26] The amino acid composition of collagen is atypical for proteins, notably with respect to its excessive hydroxyproline content material. The typical amino acid composition for fish and mammal pores and skin is given.[27]
(*5*)Synthesis[edit]
Many micro organism and viruses secrete virulence components, such because the enzyme collagenase, which destroys collagen or interferes with its manufacturing.