Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assembly |
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Authors: | Laetitia Sabatier Jelena Djokic Dirk Hubmacher Dzaner Dzafik Valentin Nelea Dieter P. Reinhardt |
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Affiliation: | 1. Faculty of Medicine, Department of Anatomy and Cell Biology, McGill University, Montreal, QC H3A 0C7, Canada;2. Faculty of Dentistry, McGill University, Montreal, QC H3A 0C7, Canada |
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Abstract: | Fibrillins form multifunctional microfibrils in most connective tissues. Deficiencies in fibrillin assembly can result in fibrillinopathies, such as Marfan syndrome. We demonstrate the presence of heparin/heparan sulfate binding sites in fibrillin-2 and -3. Multimerization of all three fibrillins drastically increased the apparent affinity of their interaction with heparin/heparan sulfate. Surprisingly, contrary to other reports heparin/heparan sulfate strongly inhibited homo- and heterotypic N-to-C-terminal fibrillin interactions. These data suggest that heparin/heparan sulfate controls the formation of microfibrils at the bead interaction stage. |
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Keywords: | BSA, bovine serum albumin cbEGF, calcium-binding epidermal growth factor-like domain MAGP-1, microfibril-associated glycoprotein-1 TB, transforming growth factor-β binding domain TBS, Tris-buffered saline TBST, TBS/Tween-20 |
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