Fibulin-4 and latent-transforming growth factor beta-binding protein-4 interactions with syndecan-2 and syndecan-3 are required for elastogenesis.

ABSTRACT: Elastogenesis is a cell surface-located hierarchical process that requires the core components tropoelastin and fibrillins and several accessory proteins, including fibulin-4 (FBLN4) and latent TGF-β binding protein-4 (LTBP4). FBLN4 and LTBP4 interact with cells, but their cell receptors and associated molecular elastogenic mechanisms remain unknown. Primary skin fibroblasts and several vascular smooth muscle cells bound strongly to FBLN4 multimers and LTBP4 monomers. We identified two cell interaction epitopes on FBLN4 located in cbEGF2-3 and the C-terminal domain, whereas FBLN4 multimerization sites were mapped to cbEGF4-5 and the C-terminal domain. We also determined a novel cell interaction site in the N-terminal half of LTBP4. Cell binding to FBLN4 and LTBP4 was strongly inhibited in

SUBMITTER: Hakami H 

PROVIDER: S-EPMC11960800 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature