Literature DB >> 12524238

The serpin protease-nexin 1 is present in rat aortic smooth muscle cells and is upregulated in L-NAME hypertensive rats.

Marie-Christine Bouton1, Benjamin Richard, Patrick Rossignol, Monique Philippe, Marie-Claude Guillin, Jean-Baptiste Michel, Martine Jandrot-Perrus.   

Abstract

OBJECTIVE: Protease-nexin 1 (PN-1) belongs to the serpin superfamily and behaves as a specific thrombin inhibitor in the pericellular environment. Little is known about PN-1 expression and its regulation in the vascular system. In this study, we examined the expression of functionally active PN-1 in vitro in rat aortic smooth muscle cells and in vivo in rat arterial media and its regulation in hypertensive rats. METHODS AND
RESULTS: The vascular PN-1 formed specific covalent complexes with thrombin involving the catalytic site of the protease, and heparin increased the formation of these complexes. We also demonstrated PN-1 in rat arterial media by immunohistochemical staining. Moreover, we examined in vivo vascular expression of PN-1 in a model of chronic hypertension induced by long-term administration of N(G)-nitro-L-arginine methyl ester (L-NAME). Marked increases in PN-1 mRNA (3-fold) and protein (2-fold) were observed after 2 months of hypertension. Increased expression of PN-1 in the vascular wall was associated with an increase in the formation of complexes between radiolabeled-thrombin and PN-1, indicating that PN-1 was functional.
CONCLUSIONS: PN-1 may thus participate in the mechanisms that regulate thrombin activity in the vessel wall.

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Year:  2003        PMID: 12524238     DOI: 10.1161/01.atv.0000047867.98019.2d

Source DB:  PubMed          Journal:  Arterioscler Thromb Vasc Biol        ISSN: 1079-5642            Impact factor:   8.311


  11 in total

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Journal:  Front Physiol       Date:  2016-06-30       Impact factor: 4.566

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