6533b82dfe1ef96bd1290fae

RESEARCH PRODUCT

Type-II transmembrane prolyl dipeptidases and matrix metalloproteinases in membrane vesicles of active endothelial cells.

Monica SalamoneM. SiragusaM. NascaL. PitarresiM. L. VittorelliW. T. ChenG. Ghersi

subject

TUMOR-CELLSCell MembraneBREAST-CARCINOMA CELLSEndothelial CellsUP-REGULATIONANGIOGENESISMatrix MetalloproteinasesExtracellular MatrixACTIVATIONEnzyme ActivationNEUROPEPTIDE-YCell MovementSEPRASESettore BIO/10 - BiochimicaMETASTASISPEPTIDASE-IVHumansDipeptidyl-Peptidases and Tripeptidyl-PeptidasesINTEGRINCells Cultured

description

Conclusions: Endothelia cells in sparse culture are migratory and increase the production of gelatinases of serine- and metallo-classes in membrane vesicles. Collectively, proteases associated with membrane vesicles degrade extracellular matrix components including type-I and type-IV collagens, laminin and fibronectin. Inhibitor studies suggest the existence of small gelatinases that were derived from these serine- and metallo-proteases. Thus, further studies are warranted to demonstrate the cooperative action of metallo- and serine proteases on cell surfaces and in extracellular vesicles during endothelial cell migration in 3D collagenous matrices, and potential proteolytic activation mechanism for these cell surface proteases.

10.1007/0-387-32824-6_22https://pubmed.ncbi.nlm.nih.gov/16700524