Prekallikrein in a complex with kininogen and C1q binding protein on the plasma membrane is cleaved to generate active kallikrein, which remains bound to the complex. In the body, this reaction appears to occur on the surfaces of endothelial cells and may require the presence of activated platelets. Recent work indicates that the protease that cleaves prekallikrein under these conditions is prolylcarboxypeptidase. Although this enzyme was originally isolated from lysosomes (Odya et al. 1978; Tan et al. 1993), it is associated with plasma membranes of cultured human endothelial cells in vitro (Moreira et al. 2002; Shariat-Madar et al. 2002), and the purified recombinant enzyme efficiently cleaves prekallikrein (Shariat-Madar et al. 2004). In contrast factor XII, despite its activity on prekallikrein in vitro, appears not to be responsible for prekallikrein activation on the cell surface (Rojkjaer et al. 1998).
Schmaier, AH, Shariat-Madar, Z, Mahdi, F
Skidgel, RA, Erdos, EG, Morris, PW, Tan, F
Marinkovic, DV, Odya, CE, Erdos, EG, Hammon, KJ, Stewart, TA
Schmaier, AH, Shariat-Madar, Z, Moreira, CR, Nader, HB, Motta, G, Mahdi, F
serine-type carboxypeptidase activity of prolylcarboxypeptidase dimer [plasma membrane]
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