Lower vertebrate collagen. Evidence for type I-like collagen in the skin of lamprey and shark.
The soluble skin collagens of the lamprey, Entosphenus japonicus, and the great blue shark, Prionace glauca, have been isolated and characterized with respect to their chain composition. Chromatography on CM-cellulose of the denatured skin collagens and agarose gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and chemical analysis of the chromatographic fractions revealed that the two distinct subunits, alpha 1 and alpha 2, were present in a molar ratio of about 2:1. Thus, the chain composition of both lower vertebrate collagens is designated by the formula (alpha 1)2 alpha 2, similar to that of Type I collagen in higher vertebrate tissues. However, electrophoresis of the collagens in sodium dodecyl sulfate showed mostly a single type of alpha component. This seems to be due to the preferential crosslinking of alpha 1 into beta 11 dimers for the lamprey collagen and of alpha 2 into beta 12 dimers for the shark protein. These composite findings indicate that Type I-like collagen is widely distributed in the skin of vertebrates ranging from cyclostomes to mammalians.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D003094:Collagen / Q000032:analysis*; D006901:Hydroxylysine / Q000032:analysis; D007798:Lampreys; D008970:Molecular Weight; D012754:Sharks; D012867:Skin / Q000032:analysis*; D013045:Species Specificity
D000596:Amino Acids; D002241:Carbohydrates; D006901:Hydroxylysine; D003094:Collagen