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A novel cell adhesion region in tropoelastin mediates attachment to integrin ?V?5.


ABSTRACT: Tropoelastin protein monomers assemble to form elastin. Cellular integrin ?V?3 binds RKRK at the C-terminal tail of tropoelastin. We probed cell interactions with tropoelastin by deleting the RKRK sequence to identify other cell-binding interactions within tropoelastin. We found a novel human dermal fibroblast attachment and spreading site on tropoelastin that is located centrally in the molecule. Inhibition studies demonstrated that this cell adhesion was not mediated by either elastin-binding protein or glycosaminoglycans. Cell interactions were divalent cation-dependent, indicating integrin dependence. Function-blocking monoclonal antibodies revealed that ?V integrin(s) and integrin ?V?5 specifically were critical for cell adhesion to this part of tropoelastin. These data reveal a common ?V integrin-binding theme for tropoelastin: ?V?3 at the C terminus and ?V?5 at the central region of tropoelastin. Each ?V region contributes to fibroblast attachment and spreading, but they differ in their effects on cytoskeletal assembly.

SUBMITTER: Lee P 

PROVIDER: S-EPMC3894329 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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A novel cell adhesion region in tropoelastin mediates attachment to integrin αVβ5.

Lee Pearl P   Bax Daniel V DV   Bilek Marcela M M MM   Weiss Anthony S AS  

The Journal of biological chemistry 20131129 3


Tropoelastin protein monomers assemble to form elastin. Cellular integrin αVβ3 binds RKRK at the C-terminal tail of tropoelastin. We probed cell interactions with tropoelastin by deleting the RKRK sequence to identify other cell-binding interactions within tropoelastin. We found a novel human dermal fibroblast attachment and spreading site on tropoelastin that is located centrally in the molecule. Inhibition studies demonstrated that this cell adhesion was not mediated by either elastin-binding  ...[more]

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