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Platelet activation biochemistry

Essex, D. W., Li, M., Miller, A., Feinman, R. D., Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation, Biochemistry (2001), p. 6070-6075... [Pg.104]

Bodin S, Giuriato S, Ragab J, Humbel BM, Viala C, Vieu C, Chap H, Payrastre B. Production of phosphatidylinositol 3,4,5-trisphosphate and phosphatidic acid in platelet rafts evidence for a critical role of cholesterol-enriched domains in human platelet activation. Biochemistry 2001 40 15290-15299. [Pg.881]

Leong L, Henriksen RA, Kermode JC, Rittenhouse SE, Tracy PB The thrombin high-affinity binding site on platelets is a negative regulator of thrombin-induced platelet activation. Structure-function studies using two mutant thrcanbins, Quick I and Quidc II. Biochemistry 31 2567,1992... [Pg.33]

RothGJ. (1986). Platelet arachidonic acid metabolism and platelet-activating factor. In Biochemistry of Platelets (niillips DR, and Shuman MA, eds.). Academic Press Inc. (London) Ltd. [Pg.306]

Platelet activating factor (PAF) has been identified as 1-0-alkyl-2-0-acetyl-sn-glycero-3-phosphocholine. Many different types of mammalian cells have been reported to release PAF upon stimulation. F. H. Chilton et al., Journal of Biochemistry, 257 5402-5407 (1982). [Pg.95]

Calvete, J.J., Schaefer, W., Soszka,T.,Lu, W., Cook, J.J., Jameson, B.A., and Niewiarowski, S. (1991). Identification of the disulfide bond pattern in albolabrin, an RGD-containing peptide from the venom of Trimeserus albolabris Significance for the expression of the platelet inhibitory activity. Biochemistry. 30 5225-5229. [Pg.191]

Sugiura, T., Tokumura, A., Gregory, L, Nouchi, T., Weintraub, S.T., and Hanahan, D.J. (1994) Biochemical characterization of the interaction of lipid phosphoric acids with human platelets comparison with platelet activating factor, Archives of Biochemistry and Biophysics 311 358-368. [Pg.212]

Antonopoulou, S. Demopoulos, C.A. latrou, C. Moustakas, G. Zirogiarmis, P. (1994). Platelet-activating factor acetylhydrolase (PAF-AH) in human kidney. International Journal of Biochemistry, Vol.26, No.9, (September 2994), pp. 1157-1162, ISSN 1357-2725. [Pg.301]

Alkyl-2-acetyl-sn-glycerophosphorylcholine or "platelet-activating factor" (commonly abbreviated to PAF) is present in minute concentrations in platelets and certain other cells, yet exerts profound physiological effects. Its chemistry and biochemistry have been reviewed [353,866]. It is such a polar molecule that HPLC in the adsorption mode is required for its isolation. As the author and others [107,168] have reviewed these methods in some detail. It need only be mentioned here as an example that It elutes between sphingomyelin and lysophosphatidylcholine from a column of silica gel with a gradient of hexane-isopropanol-water in which the water content is increased [110]. No existing method is sufficiently sensitive to demonstrate the... [Pg.158]

Kulikov, V.l. and Muzya, G.l. (1997) Ether lipids and platelet-activating factor evolution and cellular fimction. Biochemistry, 62,1103—1108. [Pg.88]

Kini, R.M., and Evans, H.J., 1989, Role of cationic residues in cytolytic activity modification fxomNaja nigricollis and correlation between cytolytic and anti-platelet effect. Biochemistry 28 295-301. [Pg.126]

An enormous number of publications has emerged over the past 16 years on various aspects of PAF chemistry, biochemistry, and physiology. Certainly the field has expanded tremendously from the days when its behavior on rabbit platelets was a major experimental outlet. Currently the biological activities of PAF (the alkyl form) can be separated into the following two classes ... [Pg.167]

Kim DK, Kudo I, and Inoue K. (1988). Detection in human platelets of phospholipase A2 activity whidi preferentially hydixdyzes an aradiidonoyl residue. J. Biochemistry. 104,492-494. [Pg.308]

Fig. 11.4 Mechanism of clotting factor localization to an activated platelet surface. Left After synthesis in the liver, certain blood clotting proteins are posttranslationally modified in the endoplasmic reticulum by a vitamin K-dependent Vit K carboxylase. This enzyme forms carboxyglutamate residues (top center) that chelate calcium ions. Right In the bloodstream, clotting factor-bound calcium ions attach to negatively charged phosphatidylserine that appears on the surface of activated platelets. Certain therapeutic drugs or acquired deficiencies inhibit this process - see text (Original figure submitted by Dr Paul DeAngelis, Department of Biochemistry, University of Oklahoma HSC, Oklahoma City, OK, USA)... Fig. 11.4 Mechanism of clotting factor localization to an activated platelet surface. Left After synthesis in the liver, certain blood clotting proteins are posttranslationally modified in the endoplasmic reticulum by a vitamin K-dependent Vit K carboxylase. This enzyme forms carboxyglutamate residues (top center) that chelate calcium ions. Right In the bloodstream, clotting factor-bound calcium ions attach to negatively charged phosphatidylserine that appears on the surface of activated platelets. Certain therapeutic drugs or acquired deficiencies inhibit this process - see text (Original figure submitted by Dr Paul DeAngelis, Department of Biochemistry, University of Oklahoma HSC, Oklahoma City, OK, USA)...
Maccarrone, M., Bari, M., Menichelli, A., Giuliani, E., Del Principe, D., and Finazzi-Agro, A. (2001) Human platelets bind and degrade 2-arachidonoylglycerol, which activates these cells through a cannabinoid receptor, European Journal oj Biochemistry 268 819-825. [Pg.208]

C3HJO3, Mr 90.08. The racemate and the enantiomers occur in nature. (/f)-Form, mp. 53 °C, [0] -2.6° (HjO), pK 3.83. Prismatic platelets, soluble in water, ethanol, and ether, insoluble in chloroform. (/ )-(-)-L. is formed in the fermentation of glucose by Lactobacillus leichmannii and L. delbrueckii with 1 - and 2-valent metal ions it forms dextrorotatory salts and laevorotatory salts with 3-valent metal ions, e.g., zinc D-(+)-lactate 2H2O, [alo" -i-8.18° (HjO). (5)-form (sarcolactic acid, paralactic acid), mp. 53 °C, [ajp l 3.82° (H2O), pKg 3.79 (25 °C), is highly hygroscopic, occurs in blo, muscles serum, bile, kidneys, and other organs. The content of L. increases after strenuous muscle activity (lactate acidosis). The racemate, oil.mp. 17°C,bp. 122 °C(1.86 kPa), steam distillable, is widely distributed in nature, e. g., in sour milk products, in molasses as a result of partial fermentation of the sugars from apples and other fruits. For biochemistry and preparation, see Ut.. ... [Pg.345]

Yatomi, Y, Rnan, E, Megidish, T, Toyokuni, T, Hakomori, S and Igarashi, Y (1996) N,N-dimethylsphingosine inhibition of sphingosine kinase and sphingosine 1 -phosphate activity in hnman platelets. Biochemistry, 35, 626-633. [Pg.166]


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See also in sourсe #XX -- [ Pg.2 , Pg.188 ]




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