Collagen VI Microfibril Formation Is Abolished by an alpha 2(VI) von Willebrand Factor Type A Domain Mutation in a Patient with Ullrich Congenital Muscular Dystrophy
Leona D Tooley, Laura K Zamurs, Nicola Beecher, Naomi L Baker, Rachel A Peat, Naomi E Adams, John F Bateman, Kathryn N North, Clair Baldock, Shireen R Lamande
JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2010
Collagen VI is an extracellular protein that most often contains the three genetically distinct polypeptide chains, α1(VI), α2(VI), and α3(VI), although three recently identified chains, α4(VI), α5(VI), and α6(VI), may replace α3(VI) in some situations. Each chain has a triple helix flanked by N- and C-terminal globular domains that share homology with the von Willebrand factor type A (VWA) domains. During biosynthesis, the three chains come together to form triple helical monomers, which then assemble into dimers and tetramers. Tetramers are secreted from the cell and align end-to-end to form microfibrils. The precise molecular mechanisms responsible for assembly are unclear. Mutations in t..View full abstract
Awarded by National Health and Medical Research Council of Australia
Awarded by Biotechnology and Biological Sciences Research Council
This work was supported by National Health and Medical Research Council of Australia Grant 491252 (to S. R. L. and J. F. B.), Biotechnology and Biological Sciences Research Council Grant BB/D008662/1 (to N. B.), and the Murdoch Childrens Research Institute.Supported by a Melbourne University Research Scholarship.