Abstract
This review is a brief summary of the history of the development of the Prothrombinase complex paradigm and its incorporation into the “extrinsic pathway”. It summarizes my laboratory’s research from 1968 to 2012 and identifies many of the key players in these efforts.
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References
Mann KG, Batt CW (1969) The Molecular Weights of Bovine Thrombin and its Primary Autolysis Products. J Biol Chem 244:6555–6557
Mann KG, Heldebrant CM, Fass DN (1971) Multiple Active Forms of Thrombin. II. Mechanism of Production From Prothrombin. J. Biol. Chem. 246:6106–6114
Nesheim ME, Prendergast FG, Mann KG (1979) Interactions of a Fluorescent Active-site-directed Inhibitor of Thrombin: Dansylarginine N-(3-ethyl-1,5-pentanediyl)amide. Biochemistry 18:996–1003
Nesheim ME, Myrmel K, Hibbard L, Mann KG (1979) Isolation and Characterization of Single Chain Bovine Factor V. J Biol Chem 254:508–517
Butkowski RJ, Elion J, Downing MR, Mann KG (1977) Primary Structure of Human Prethrombin 2 and α-thrombin. J Biol Chem 252:4942–4957
Tracy PB, Nesheim ME, Mann KG (1981) Coordinate Binding of Factor Va and Factor Xa to the Unstimulated Platelet. J Biol Chem 256:743–751
Nesheim ME, Tracy RP, Mann KG (1984) “Clotspeed,” a Mathematical Simulation of the Functional Properties of Prothrombinase. J Biol Chem 259:1447–1453
Krishnaswamy S, Jones KC, Mann KG (1988) Prothrombinase Complex Assembly: Kinetic Mechanism of Enzyme Assembly on Phospholipid Vesicles. J Biol Chem 263:3823–3834
Haynes LM, Bouchard BA, Tracy PB, Mann KG (2012) Prothrombin activation by platelet-associated prothrombinase proceeds through the prethrombin-2 pathway via a concerted mechanism. J. Biol. Chem. 287:38647–38655
Katzmann JA, Nesheim ME, Hibbard LS, Mann KG (1981) Isolation of Functional Human Coagulation Factor V Using a Hybridoma Antibody. Proc Natl Acad Sci USA 78:162–166
Jenny RJ, Pittman DD, Toole JJ, Kriz RW, Aldape RA, Hewick RM, Kaufman RJ, Mann KG (1987) Complete cDNA and Derived Amino Acid Sequence of Human Factor V. Proc Natl Acad Sci USA 84:4846–4850
Adams TE, Hockin M, Mann KG, Everse SJ (2004) The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function. PNAS 101(24):8918–8923
Reviews which contain numerous references to the work of other laboratories
Mann KG, Kalafatis M (2003) Factor V: A combination of Dr. Jekyll and Mr Hyde Blood 1–1:1–11
Mann KG, Nesheim ME, Church WR, Haley P, Krishnaswamy S (1990) Surface-Dependent Reactions of the Vitamin K-dependent Enzyme Complexes. Blood 76:1–16
Lawson JH, Kalafatis M, Stram S, Mann KG (1994) A Model for the Tissue Factor Pathway to Thrombin: 1. An Empirical Study J Biol Chem 269:23357–23366
Jones KC, Mann KG (1994) A Model for the Tissue Factor Pathway to Thrombin: 2. A Mathematical Simulation J Biol Chem 269:23367–23373
Rand MD, Lock JB (1996) van’t Veer C, Gaffney DP and Mann KG: Blood Clotting in Minimally Altered Whole Blood. Blood 88:3432–3445
Whelihan MF, Zachary V, Orfeo T, Mann KG (2012) Prothrombin activation in blood coagulation: the erythrocyte contribution to thrombin generation. Blood 120:3837–3845
Hockin MF, Kalafatis M, Shatos M, Mann KG (1997) Protein C Activation and Factor Va Inactivation on Human Umbilical Vein Endothelial Cells. Arterioscler Thromb Vasc Biol 17:2765–2775
Campbell JE, Brummel-Ziedins KE, Butenas S, Mann KG (2010) Cellular regulation of blood coagulation: A model for venous stasis. Blood 116:6082–6091
Undas A, Brummel KE, Musial J, Mann KG, Szczeklik A (2001) Simvastatin Depresses Blood Clotting by Inhibiting Activation of Prothrombin, Factor V, and Factor XIII and by Enhancing Factor Va Inactivation. Circulation 103:2248–2253
Adams TE, Everse SJ, Mann KG (2003) Predicting the pharmacology of thrombin inhibitors. J Thromb Haemost 1:1024–1027
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This review covers 44 years of research and over 400 publications from my laboratory. I do not have any conflict of interest, nor any of my family members, dealing with this research.
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Mann, K.G. Prothrombinase: the paradigm for membrane bound enzyme complexes; a memoir. J Thromb Thrombolysis 52, 379–382 (2021). https://doi.org/10.1007/s11239-021-02402-w
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DOI: https://doi.org/10.1007/s11239-021-02402-w