Fibulin-3,-4, and-5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers

Abstract

Background: Fibulin-3,-4, and-5 (short fibulins) participate in elastogenesis, although the molecular mechanism remains unknown. Results: Short fibulins are cleaved by MMPs and bind cells and heparin, and fibulin-4 dimerizes and multimerizes. Conclusion: Short fibulins have a proteolytically susceptible linker and can bind cells independently of the RGD motif, and fibulin-4 multimerization is crucial for heparin binding. Significance: The uncovered properties will advance understanding of elastogenesis. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.