Hageman factor fragment inhibitor in corn seeds: Purification and characterization

Hojima, Yoshio; Pierce, Jack V.; Pisano, John J.

doi:10.1016/0049-3848(80)90381-3

Cited by 170 publications

(107 citation statements)

References 22 publications

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“…The inhibitors used were the kallikrein-specific Kunitz domain inhibitor KALI-DY (35), the FXIaspecific Kunitz domain inhibitor APPI (34), and the FXIIa-specific inhibitor corn trypsin inhibitor (36). After 4 h the reaction was stopped, and the inhibition of HGF conversion was analyzed by SDS-PAGE under reducing conditions as described.…”

Section: I-labeling Of Pro-hgf-formentioning

confidence: 99%

Unusual Proteolytic Activation of Pro-hepatocyte Growth Factor by Plasma Kallikrein and Coagulation Factor XIa

Peek¹,

Moran²,

Mendoza

et al. 2002

Journal of Biological Chemistry

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Section: I-labeling Of Pro-hgf-formentioning

confidence: 99%

Unusual Proteolytic Activation of Pro-hepatocyte Growth Factor by Plasma Kallikrein and Coagulation Factor XIa

Peek¹,

Moran²,

Mendoza

et al. 2002

Journal of Biological Chemistry

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“…7,34 Healthy individuals (aged [22][23][24][25][26][27][28][29][30][31][32][33][34][35][36] were selected so as to exclude donors with a personal or familial history of thrombosis/hemorrhage, or regular aspirin or drug use. All individuals exhibited values in the normal range for the prothrombin time (PT; 11.6-13.8 seconds), activated partial thromboplastin time (aPTT; 27-36 seconds), and platelet counts (172 000-376 000/L).…”

Section: Human Donorsmentioning

confidence: 99%

Antiplatelet agents in tissue factor–induced blood coagulation

Butenas

Cawthern

Veer

et al. 2001

Blood

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IntroductionThe importance of the platelet in normal hemostasis and in disease states, such as atherosclerosis and thrombosis, is well established. [1][2][3][4][5] A particularly germane example is the platelet-rich thrombus, which forms on fissured or ruptured atherosclerotic plaques. [3][4][5] Although the slow formation of the underlying plaques is a progressive disease that serves to narrow the lumen of the vessel over an extended period of time, it is the sudden and catastrophic superposition of the platelet-rich thrombotic occlusion on these lesions that is central to nearly all ischemic coronary events. General acceptance that the ultimate occlusive event is thrombotic in nature has led to the development of strategies that attempt to ameliorate, inhibit, or reverse this final phase of the coronary disease process. Some of the newest strategies focus on inhibition of platelet functions, which contribute to the formation of the thrombotic occlusion.The generation of thrombin during the blood clotting process can be divided into 2 semidiscrete intervals, the initiation and propagation phases. 6 During the initiation phase nanomolar amounts of thrombin and picomolar amounts of other coagulation enzymes are generated. Clot occurs at the inception of the propagation phase, which is characterized by rapid and near quantitative thrombin generation. By this point activation of platelets and cleavage of factor V and factor VIII are almost complete. 7 In normal blood, the thrombin activation process is independent of platelet or factor V activation, but is limited by the generation of factor Xa. 6,7 Normal platelet function has been divided into 3 processes: adhesion, aggregation, and activation (including surface phospholipid rearrangements and secretory pathways [8][9][10][11] ). These functions bestow on the platelet its antihemorrhagic qualities and are regulated by a variety of mechanisms. 12 The most potent platelet agonist is ␣-thrombin, the central enzyme of coagulation that controls hemorrhage in vivo. Thrombin is generated from the inactive circulating precursor prothrombin via the tissue factor (TF) pathway of coagulation [13][14][15][16] ; this serine protease activates platelets via specific cell surface receptors, leading to secretion, aggregation, changes in platelet morphology, and expression of a procoagulant, phospholipid-equivalent, surface. 9-11 Aggregated thrombin-activated platelets form the basis of the thrombus in normal hemostasis and provide the surface on which the complexdependent reactions of the TF pathway are localized. Furthermore, thrombin amplifies its own generation by activating circulating plasma procofactors (factor V and factor VIII), critical components of the pathway's proteolytic complex catalysts, which also serve to localize proteolytic activity to the surface of the activated platelet. 6,17 Thrombin converts fibrinogen by limited proteolysis to fibrin, which polymerizes throughout the growing thrombus rendering added stability. [18][19][20] The importance of TF-induced t...

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“…Protein inhibitors of trypsin and activated Hageman factor were isolated from pumpkin (Cucurbita maxima) seeds by Polanowski et al [l] and Hojima et al [2,3], independently. Elaborate work by the former group led to the isolation of 3 iso-inhibitors (& -3OOO), termed CMTI-I, CMTI-III, and CMTI-IV, and the determination of their amino acid sequences [4].…”

Section: Introductionmentioning

confidence: 99%

A new protein inhibitor of trypsin and activated hageman factor from pumpkin (Cucurbita maxima) seeds

1990

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A protein inhibitor (CMTI-V; && 7106) of trypsin and activated Hageman factor (Factor XII,), a serine protease involved in blood coagulation, has been isolated for the first time from pumpkin (Cuca&~n maxima) seeds by means of trypsin-afhnity chromatography and reverse phase high performance liquid chromatography (HPLC). The dissociation constants of the inhibitor complexes with trypsin and Factor XII. have been determined to be 1.6 x 10-a and 4.1 x 1Om8 M, respectively. The primary structure of CMTI-V is reported. The protein has 68 amino acid residues and one disulfide bridge and shows a high level of sequence homology to the Potato I inhibitor family. Furthermore, its amino terminus consists of an N-acetylates Ser. The reactive site has been established to be the peptide bond between LY$~-As~~~. The moditied inhibitor which has the reactive site peptide bond hydrolyzed inhibits trypsin but not the Hageman factor.

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Hageman factor fragment inhibitor in corn seeds: Purification and characterization

Cited by 170 publications

References 22 publications

Unusual Proteolytic Activation of Pro-hepatocyte Growth Factor by Plasma Kallikrein and Coagulation Factor XIa

Unusual Proteolytic Activation of Pro-hepatocyte Growth Factor by Plasma Kallikrein and Coagulation Factor XIa

Antiplatelet agents in tissue factor–induced blood coagulation

A new protein inhibitor of trypsin and activated hageman factor from pumpkin (Cucurbita maxima) seeds

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