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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 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 Citation Map 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. Related Collections Hemostasis, Thrombosis, and Vascular Biology Signal Transduction Gene Expression Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Recombinant prolylcarboxypeptidase activates plasma prekallikrein Zia Shariat-Madar, Fakhri Mahdi, and Alvin H. Schmaier From the Departments of Internal Medicine and Pathology, Division of Hematology and Oncology, University of Michigan, Ann Arbor, MI. The serine protease prolylcarboxypeptidase (PRCP), isolated from human umbilical vein endothelial cells (HUVECs), is a plasma prekallikrein (PK) activator. PRCP cDNA was cloned in pMT/BIP/V5-HIS-C, transfected into Schneider insect (S2) 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, diisopropyl-fluorophosphonate (DFP), phenylmethylsulfonyl fluoride (PMSF), and Z-Pro-Proaldehyde-dimethyl acetate, but not by 1 mM EDTA (ethylenediaminetetraacetic acid), bradykinin 1-5, or angiotensin 1-7. Corn trypsin inhibitor binds to prekallikrein to prevent rPRCP activation, but it does not directly inhibit the active site of either enzyme. Unlike factor XIIa, the ability of rPRCP to activate PK is blocked by angiotensin II, not by neutralizing antibody to factor XIIa. PRCP antigen is detected on HUVEC membranes using flow cytometry and laser scanning confocal microscopy. PRCP antigen does not colocalize with LAMP1 on nonpermeabilized HUVECs, but it partially colocalizes in permeabilized cells. PRCP colocalizes with all the HK receptors, gC1qR, uPAR, and cytokeratin 1 antigen, on nonpermeabilized HUVECs. PRCP activity and antigen expression on cultured HUVECs 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 detected in the intravascular compartment. (Blood. 2004;103:4554-4561) 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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