Identification of alternatively spliced variants of type II procollagen in vitreous.
Adult and foetal bovine vitreous were analyzed for the presence of unprocessed and partially processed forms of type II procollagen. Type II procollagen can exist in two alternatively spliced forms: a short form which lacks a large part of the N-propeptide due to the splicing out of exon 2 and a long form in which exon 2 is expressed and which has a full-sized N-propeptide. Both splice variants were demonstrated and analyses of type II pN-collagen demonstrated that the long form predominated, the ratio of the long form to the short form being 5:1 in foetal vitreous and 1.5:1 in adult vitreous. In foetal vitreous 35% of the type II collagen extracted was in the pN form, but there was very little unprocessed type II procollagen or type II pC-collagen. In contrast, adult vitreous extracts contained relatively less type II pN-collagen, but contained larger amounts of type II pC-collagen and unprocessed type II procollagen.
Bishop
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PN
Division of Biochemistry, School of Biological Sciences, University of Manchester, U.K.
Reardon
A J
AJ
McLeod
D
D
Ayad
S
S
D017398:Alternative Splicing; D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005314:Embryonic and Fetal Development; D005260:Female; D005333:Fetus; D014644:Genetic Variation; D005865:Gestational Age; D010434:Pepsin A; D010449:Peptide Mapping; D011247:Pregnancy; D011347:Procollagen / Q000096:biosynthesis* / Q000302:isolation & purification; D014822:Vitreous Body / Q000196:embryology / Q000378:metabolism*
D011347:Procollagen; D010434:Pepsin A