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Heparin/heparan sulfate controls fibrillin‐1, ‐2 and ‐3 self‐interactions in microfibril assembly
Author(s) -
Sabatier Laetitia,
Djokic Jelena,
Hubmacher Dirk,
Dzafik Dzaner,
Nelea Valentin,
Reinhardt Dieter P.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.061
Subject(s) - heparan sulfate , fibrillin , heparin , microfibril , chemistry , glycosaminoglycan , extracellular matrix , microbiology and biotechnology , biochemistry , biophysics , biology , cellulose
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.