title: Identification of alternatively spliced variants of type II procollagen in vitreous.
abstract: 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.
authors.affiliation: Division of Biochemistry, School of Biological Sciences, University of Manchester, U.K.
authors.forename: P N
authors.initials: PN
authors.lastname: Bishop
authors.forename: A J
authors.initials: AJ
authors.lastname: Reardon
authors.forename: D
authors.initials: D
authors.lastname: McLeod
authors.forename: S
authors.initials: S
authors.lastname: Ayad
mesh_terms: 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*
chemical_list: D011347:Procollagen; D010434:Pepsin A