Proline hydroxylation of collagens synthesized at different temperatures in vivo by two poikilothermic species.
Extent of prolyl hydroxylation in newly synthesized viper collagen is decreased at 10 degrees C to approximately 23% of normal on skin and to approximately 57% of normal in bone collagen. At 20 degrees C, prolyl hydroxylation is approximately 50% of normal in skin and normal in bone. At 10 degrees C and 20 degrees C, prolyl hydroxylation is decreased approximately 32% in the skin collagen of carp. In contrast, prolyl hydroxylation is unchanged at 10 and 20 degrees C in bone, scale and lepidotrichia. Prolyl hydroxylation of cartilaginous endoskeleton showed an approximately 25% decrease at 20 degrees C.
D000064:Acclimatization; D000818:Animals; D001842:Bone and Bones / Q000378:metabolism*; D003094:Collagen / Q000096:biosynthesis*; D006909:Hydroxyproline / Q000032:analysis*; D009928:Organ Specificity; D011499:Protein Processing, Post-Translational; D012867:Skin / Q000378:metabolism*; D012911:Snakes / Q000378:metabolism*; D013045:Species Specificity; D013696:Temperature
D003094:Collagen; D006909:Hydroxyproline