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High molecular weight kininogen

Factor XI. Factor XI is a Hver-synthesized glycoprotein that circulates in a zymogen form as a dimer. It is converted to its active serine protease form by Factor Xlla in the presence of high molecular weight kininogen. Calcium is not required for this activation step. [Pg.174]

Factor Xlla is a serine protease that activates FXI to FXIa (Fig. 5). This system is not of physiologic relevance since patients with hereditary deficiencies of factor XII, prekallikrein, and high-molecular weight kininogen do not present with bleeding symptoms. [Pg.377]

Mandle R, Colman R, Kaplan A Identification of prekallikrein and high-molecular-weight kininogen as a complex in human plasma. Proc Natl Acad Sci USA 1976 73 4179-4183. [Pg.80]

Thompson RE, Mandle R Jr, Kaplan AP Studies of 30 binding of prekallikrein and factor XI to high molecular weight kininogen and its light chain. Proc Natl Acad Sci USA 1979 76 4862-4866. [Pg.81]

Tail JF, Fujikawa K Primary structure requirements 31 for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. J Biol Chem 1987 262 11651-11656. [Pg.81]

Reddigari S, Kaplan AP Cleavage of human high-molecular-weight kininogen by purified kaUikreins and upon contact activation of plasma. Blood 1988 71 1334-1340. [Pg.81]

Wiggins RC. Bouma BN. Cochrane CG. Griffin JH Role of high-molecular-weight kininogen in surface-binding and activation of coagulation factor XI and prekallikrein. Proc Natl Acad Sci USA 1977 74 4636-4640. [Pg.81]

Schmaier AH. Silver L. Adams AL, Fischer GC, Munoz PC, Vroman L, et al The effect of high molecular weight kininogen on surface-adsorbed fibrinogen. Thromb Res 1984 33 51-67. [Pg.81]

Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB The expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 1988 263 16327-16333. [Pg.81]

Reddigari SR, Shibayama Y. Brunnee T. Kaplan AP Human Hageman factor (factor Xll) and high molecular weight kininogen compete for the same binding site on human umbihcal vein endothelial cells. J Biol Chem 1993 268 11982-11987. [Pg.81]

Joseph K, Ghebrehiwet B. Peerschke El. Reid KB. Kaplan AP Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor Xll identity with the receptor that binds to the globular heads of Clq (gClq-R). Proc Natl Acad Sci USA 1996 93 8552-8557. [Pg.81]

Joseph K, Ghebrehiwet B, Kaplan AP Cytokeratin 1 and gClqR mediate high molecular weight kininogen binding to endothelial cells. Clin Immunol 1999 92 246-255. [Pg.81]

Joseph K, Tholanikunnel BG, Ghebrehiwet B, Kaplan AP Interaction of high molecular weight kininogen binding proteins on endothelial cells. Thromb Haemost 2004 91 61-70. 55... [Pg.82]

Motta G, Rojkjser R, Hasan AA, Cines DB, Schmaier AH High molecular weight kininogen regulates prekallikrein assembly and activation on endothe- 57 lial cells a novel mechanism for contact activation. [Pg.82]

Activation of factor XII and cleavage of high molecular weight kininogen during acute attacks in hereditary and acquired Cl-inhibitor deficiencies. Immunopharmacology 1996 33 361-364. [Pg.83]

HMWK high-molecular-weight kininogen TS thromboxane synthetase... [Pg.159]


See other pages where High molecular weight kininogen is mentioned: [Pg.170]    [Pg.170]    [Pg.172]    [Pg.172]    [Pg.174]    [Pg.178]    [Pg.377]    [Pg.67]    [Pg.68]    [Pg.81]    [Pg.81]    [Pg.81]    [Pg.81]    [Pg.81]    [Pg.81]    [Pg.82]    [Pg.350]    [Pg.137]    [Pg.988]    [Pg.76]    [Pg.78]    [Pg.138]    [Pg.146]    [Pg.177]    [Pg.164]    [Pg.119]    [Pg.170]    [Pg.170]    [Pg.172]    [Pg.172]    [Pg.174]   
See also in sourсe #XX -- [ Pg.599 , Pg.600 ]

See also in sourсe #XX -- [ Pg.847 ]




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