Page 2150 - Hematology_ Basic Principles and Practice ( PDFDrive )

1905.e6 Part XII Hemostasis and Thrombosis

251. Chung DW, Davie EW: gamma and gamma’ chains of human fibrinogen 277. Huber K: Plasminogen activator inhibitor type-1 (part two): role for
are produced by alternative mRNA processing. Biochemistry 23:4232, failure of thrombolytic therapy. PAI-1 resistance as a potential benefit
1984. for new fibrinolytic agents. J Thromb Thrombolysis 11:195, 2001.
252. Laki K, Lorand L: On the solubility of fibrin clots. Science 108:280, 278. Nesheim M, Bajzar L: The discovery of TAFI. J Thromb Haemost
1948. 3:2139, 2005.
253. Lorand L: A study on the solubility of fibrin clots in urea. Hung Acta 279. Bertina RM, van Tilburg NH, Haverkate F, et al: Discovery of throm-
Physiol 1:192, 1948. bin activatable fibrinolysis inhibitor (TAFI). J Thromb Haemost 4:256,
254. Lorand L: Factor XIII: structure, activation, and interactions with 2006.
fibrinogen and fibrin. Ann N Y Acad Sci 936:291, 2001. 280. Boffa MB, Koschinsky ML: Curiouser and curiouser: recent advances in
255. Sakharov DV, Plow EF, Rijken DC: On the mechanism of the antifibri- measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and
nolytic activity of plasma carboxypeptidase B. J Biol Chem 272:14477, in understanding its molecular genetics, gene regulation, and biological
1997. roles. Clin Biochem 40:431, 2007.
256. Wang W, Boffa MB, Bajzar L, et al: A study of the mechanism of 281. Bajzar L, Morser J, Nesheim M: TAFI, or plasma procarboxypeptidase
inhibition of fibrinolysis by activated thrombin-activable fibrinolysis B, couples the coagulation and fibrinolytic cascades through the
inhibitor. J Biol Chem 273:27176, 1998. thrombin-thrombomodulin complex. J Biol Chem 271:16603, 1996.
257. Broze GJ, Jr, Higuchi DA: Coagulation-dependent inhibition of fibri- 282. Minnema MC, Friederich PW, Levi M, et al: Enhancement of rabbit
nolysis: role of carboxypeptidase-U and the premature lysis of clots from jugular vein thrombolysis by neutralization of factor XI. In vivo evi-
hemophilic plasma. Blood 88:3815, 1996. dence for a role of factor XI as an anti-fibrinolytic factor. J Clin Invest
258. de Maat MP: Effects of diet, drugs, and genes on plasma fibrinogen 101:10, 1998.
levels. Ann N Y Acad Sci 936:509, 2001. 283. Bouma BN, Mosnier LO, Meijers JC, et al: Factor XI dependent and
259. Danesh J, Lewington S, Thompson SG, et al: Plasma fibrinogen level independent activation of thrombin activatable fibrinolysis inhibitor
and the risk of major cardiovascular diseases and nonvascular mortality: (TAFI) in plasma associated with clot formation. Thromb Haemost
an individual participant meta-analysis. JAMA 294:1799, 2005. 82:1703, 1999.
260. Sriramarao P, Languino LR, Altieri DC: Fibrinogen mediates leukocyte- 284. Mann KG: Thrombin generation in hemorrhage control and vascular
endothelium bridging in vivo at low shear forces. Blood 88:3416, 1996. occlusion. Circulation 124:225, 2011.
261. Weisel JW: Fibrinogen and fibrin. Adv Protein Chem 70:247, 2005. 285. Mann KG: Coagulation Explosion, Part I—Initiation 2010. Available
262. Wright SD, Weitz JI, Huang AJ, et al: Complement receptor type three from: <http://www.youtube.com/watch?v=RP1eLdkdJKg>, (cited
(CD11b/CD18) of human polymorphonuclear leukocytes recognizes 18.01.12.)
fibrinogen. Proc Natl Acad Sci USA 85:7734, 1988. 286. Mann KG: Coagulation Explosion, Part II—Propagation 2010. Avail-
263. Mosesson MW: The roles of fibrinogen and fibrin in hemostasis and able from: <http://www.youtube.com/watch?v=oj9E33BZMsI>, (cited
thrombosis. Semin Hematol 29:177, 1992. 18.01.12.)
264. Martinez J, Ferber A, Bach TL, et al: Interaction of fibrin with 287. Bouchard BA, Tracy PB: Platelets, leukocytes, and coagulation. Curr
VE-cadherin. Ann N Y Acad Sci 936:386, 2001. Opin Hematol 8:263, 2001.
265. Podolnikova NP, Yakubenko VP, Volkov GL, et al: Identification of a 288. Morrissey JH, Macik BG, Neuenschwander PF, et al: Quantitation
novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) of activated factor VII levels in plasma using a tissue factor mutant
and alpha 5 beta 1 in the gamma C-domain of fibrinogen. J Biol Chem selectively deficient in promoting factor VII activation. Blood 81:734,
278:32251, 2003. 1993.
266. Quick AJ, Stanley-Brown M, Bancroft FW: A study of the coagulation 289. Komiyama Y, Pedersen AH, Kisiel W: Proteolytic activation of human
defect in hemophilia and in jaundice. J Med Sci 190:501, 1935. factors IX and X by recombinant human factor VIIa: effects of calcium,
267. Owren PA, Aas K: The control of dicumarol therapy and the quantita- phospholipids, and tissue factor. Biochemistry 29:9418, 1990.
tive determination of prothrombin and proconvertin. Scand J Clin Lab 290. van ’t Veer C, Golden NJ, Mann KG: Inhibition of thrombin generation
Invest 3:201, 1951. by the zymogen factor VII: implications for the treatment of hemophilia
268. Langdell RD, Wagner RH, Brinkhous KM: Effect of antihemophilic A by factor VIIa. Blood 95:1330, 2000.
factor on one-stage clotting tests; a presumptive test for hemophilia and 291. van’t Veer C, Mann KG: The regulation of the factor VII-dependent
a simple one-stage antihemophilic factor assay procedure. J Lab Clin coagulation pathway: rationale for the effectiveness of recombinant
Med 41:637, 1953. factor VIIa in refractory bleeding disorders. Semin Thromb Hemost
269. Marder VJ, Francis CW: Plasmin degradation of cross-linked fibrin. 26:367, 2000.
Ann N Y Acad Sci 408:397, 1983. 292. Choi-Miura NH, Tobe T, Sumiya J, et al: Purification and character-
270. Violand BN, Castellino FJ: Mechanism of the urokinase-catalyzed ization of a novel hyaluronan-binding protein (PHBP) from human
activation of human plasminogen. J Biol Chem 251:3906, 1976. plasma: it has three EGF, a kringle and a serine protease domain, similar
271. Hanna LS, Scheraga HA, Francis CW, et al: Comparison of structures to hepatocyte growth factor activator. J Biochem 119:1157, 1996.
of various human fibrinogens and a derivative thereof by a study of 293. Romisch J, Feussner A, Vermohlen S, et al: A protease isolated from
the kinetics of release of fibrinopeptides. Biochemistry 23:4681, human plasma activating factor VII independent of tissue factor. Blood
1984. Coagul Fibrinolysis 10:471, 1999.
272. Lewis SD, Shields PP, Shafer JA: Characterization of the kinetic pathway 294. Romisch J: Factor VII activating protease (FSAP): a novel protease in
for liberation of fibrinopeptides during assembly of fibrin. J Biol Chem hemostasis. Biol Chem 383:1119, 2002.
260:10192, 1985. 295. Stephan F, Aarden LA, Zeerleder S: FSAP, a new player in inflamma-
273. Mihalyi E: Clotting of bovine fibrinogen. Kinetic analysis of the release tion? Hamostaseologie 32:51, 2012.
of fibrinopeptides by thrombin and of the calcium uptake upon clotting 296. Osterud B, Rapaport SI: Activation of factor IX by the reaction product
at high fibrinogen concentrations. Biochemistry 27:976, 1988. of tissue factor and factor VII: additional pathway for initiating blood
274. Righini M, Perrier A, De Moerloose P, et al: D-Dimer for venous coagulation. Proc Natl Acad Sci USA 74:5260, 1977.
thromboembolism diagnosis: 20 years later. J Thromb Haemost 6:1059, 297. Jesty J, Silverberg SA: Kinetics of the tissue factor-dependent activation
2008. of coagulation Factors IX and X in a bovine plasma system. J Biol Chem
275. Kjoller L, Kanse SM, Kirkegaard T, et al: Plasminogen activator 254:12337, 1979.
inhibitor-1 represses integrin- and vitronectin-mediated cell migration 298. Bom VJ, Bertina RM: The contributions of Ca2+, phospholipids and
independently of its function as an inhibitor of plasminogen activation. tissue-factor apoprotein to the activation of human blood-coagulation
Exp Cell Res 232:420, 1997. factor X by activated factor VII. Biochem J 265:327, 1990.
276. Fay WP, Parker AC, Condrey LR, et al: Human plasminogen activator 299. Lawson JH, Mann KG: Cooperative activation of human factor IX
inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with by the human extrinsic pathway of blood coagulation. J Biol Chem
a null mutation in the PAI-1 gene. Blood 90:204, 1997. 266:11317, 1991.