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Blood, 15 June 2004, Vol. 103, No. 12, pp. 4554-4561. Prepublished online as a Blood First Edition Paper on March 2, 2004; DOI 10.1182/blood-2003-07-2510. This Article Full Text (PDF) All Versions of this Article: 2003-07-2510v1 103/12/4554    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Shariat-Madar, Z. Articles by Schmaier, A. H Search for Related Content PubMed PubMed Citation Articles by Shariat-Madar, Z. Articles by Schmaier, A. H Social Bookmarking                   What's this? Submitted July 28, 2003 Accepted February 19, 2004 Recombinant prolylcarboxypeptidase activates plasma prekallikrein Zia Shariat-Madar, Fakhri Mahdi, and Alvin H Schmaier* Internal Medicine and Pathology, University of Michigan, Ann Arbor, MI, USA * Corresponding author; email: aschmaie{at}umich.edu. The serine protease prolylcarboxypeptidase (PRCP) isolated from endothelial cells (HUVEC) is a plasma prekallikrein (PK) activator. PRCP cDNA was cloned in pMT/BIP/V5-HIS-C, transfected into S2 Schneider insect cells, and purified from serum-free media. Full-length recombinant PRCP (rPRCP) activates PK when bound to high molecular weight kininogen (HK). Recombinant PRCP is inhibited by leupeptin, angiotensin II, bradykinin, anti-PRCP, DFP, PMSF, Z-Pro-Pro-aldehyde-dimethyl acetate, but not by 1 mM EDTA, bradykinin 1-5, or angiotensin 1-7. Corn trypsin inhibitor binds to kallikrein to prevent rPRCP activation, but does not directly inhibit the active site of either enzyme. Unlike factor XIIa, ability of PRCP to activate PK is blocked by angiotensin II and not neutralizing antibody to factor XIIa. PRCP antigen is on HUVEC membranes on flow cytometry and laser scanning confocal microscopy. PRCP antigen does not co-localize with LAMP1 on non-permeabilized HUVEC, but partially co-localizes in permeabilized cells. PRCP co-localizes with all of the HK receptors, gC1qR, uPAR, and cytokeratin 1 antigen, on non-permeabilized HUVEC. PRCP activity and antigen expression on cultured HUVEC are blocked by a morpholino antisense oligonucleotide. These investigations indicate that rPRCP is functionally identical to isolated HUVEC PRCP and is a major HUVEC membrane-expressed PK activating enzyme in the intravascular compartment. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. M. Astern, W. F. Pendergraft III, R. J. Falk, J. C. Jennette, A. H. Schmaier, F. Mahdi, and G. A. Preston Myeloperoxidase Interacts with Endothelial Cell-Surface Cytokeratin 1 and Modulates Bradykinin Production by the Plasma Kallikrein-Kinin System Am. J. Pathol., July 1, 2007; 171(1): 349 - 360. [Abstract] [Full Text] [PDF] Z. Shariat-Madar, F. Mahdi, M. Warnock, J. W. Homeister, S. Srikanth, Y. Krijanovski, L. J. Murphey, A. A. Jaffa, and A. H. Schmaier Bradykinin B2 receptor knockout mice are protected from thrombosis by increased nitric oxide and prostacyclin Blood, July 1, 2006; 108(1): 192 - 199. [Abstract] [Full Text] [PDF] Z. Shariat-Madar, E. Rahimy, F. Mahdi, and A. H. Schmaier Overexpression of prolylcarboxypeptidase enhances plasma prekallikrein activation on Chinese hamster ovary cells Am J Physiol Heart Circ Physiol, December 1, 2005; 289(6): H2697 - H2703. [Abstract] [Full Text] [PDF] Z. Shariat-Madar, E. Rahimy, F. Mahdi, and A. H. Schmaier Over-Expression of Prolylcarboxypeptidase Enhances Plasma Prekallikrein Activation on Chinese Hamster Ovary Cell Membranes. Blood (ASH Annual Meeting Abstracts), November 16, 2005; 106(11): 3698 - 3698. [Abstract] N. Kato, T. Okayama, H. Isawa, M. Yuda, Y. Chinzei, and S. Iwanaga Contribution of the N-Terminal and C-Terminal Domains of Haemaphysalin to Inhibition of Activation of Plasma Kallikrein-Kinin System J. Biochem., September 1, 2005; 138(3): 225 - 235. [Abstract] [Full Text] [PDF]

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