PMID: 9524362Apr 3, 1998Paper

Alternative splicing of VWFA modules generates variants of type VI collagen alpha 3 chain with a distinctive expression pattern in embryonic chicken tissues and potentially different adhesive function

Matrix Biology : Journal of the International Society for Matrix Biology
R DolianaA Colombatti

Abstract

Type VI collagen, a ubiquitous extracellular cell adhesion molecule, is formed by heterotrimeric monomers which associate into dimers and tetramers and assemble into larger oligomers constituting the 100 nm-long periodic microfilaments of connective tissues. One distinctive structural characteristic of type VI collagen is represented by an alpha 3 chain with a much larger molecular mass compared to the other two chains and with an extensive size heterogeneity, exemplified by the separation into up to five polypeptides in SDS-PAGE. There is evidence that the alpha 3(VI) mRNA can undergo alternative splicing of three VWFA modules at the 5'-end, potentially resulting in the expression of protein variants. Here we report that alternative splicing of alpha 3(VI) mRNA in chicken embryo did not result in the absolute predominance of a particular alpha 3(VI) form in any tissue; instead, the expression of variants including exons A9, A8 and A6 increased with age. In addition, these variants had a more restricted tissue distribution pattern compared to variants including only constitutive exons: A9+ were the rarest and were present almost exclusively in skin and skeletal muscle; A6+ were expressed in several of the examined tissues with ...Continue Reading

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Citations

May 16, 2002·Matrix Biology : Journal of the International Society for Matrix Biology·Marie DziadekMon-Li Chu
Nov 18, 1998·Current Opinion in Cell Biology·J P Gorski, B R Olsen

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