ADAMTS13: Biology and Disease by George M. Rodgers

By George M. Rodgers

This accomplished quantity discusses the protease ADAMTS13, summarizing the present prestige of simple and scientific examine. The 9 authoritative chapters start with a ancient standpoint via exploration of the biochemistry and structure-function relationships of ADAMTS13 in addition to its basic functionality in hemostasis (cleavage of von Willebrand factor). rising study topics for ADAMTS13 are coated, together with its power position in angiogenesis and different elements of cellphone biology. extra subject matters contain laboratory assays for ADAMTS13, inherited ADAMTS13 deficiency, and bought ADAMTS13 deficiency. A bankruptcy on comparable thrombotic microangiopathic (TMA) problems examines the variations among TMAs linked to ADAMTS13 deficiency and people now not linked to ADAMTS13 deficiency. a last bankruptcy stories the initial info on rising features of ADAMTS13, corresponding to the prestige of recombinant ADAMTS13 items and their strength utility.

 

Comprehensive in its exploration of the ADAMTS13 protease in disease, ADAMTS13: Biology and affliction is an important source for scientific hematologists, transfusion drugs physicians, and researchers drawn to hemostasis, vascular biology, biochemistry, and metalloproteases.

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Extra resources for ADAMTS13: Biology and Disease

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2005;16:1177–83. Noris M, Remuzzi G. Atypical hemolytic-uremic syndrome. N Engl J Med. 2009;361: 1676–87. Tsai HM, Chandler WL, Sarode R, Hoffman R, Jelacic S, Habeeb RL, Watkins SL, Wong CS, Williams GD, Tarr PI. Von Willebrand factor and von Willebrand factor-cleaving metalloprotease activity in Escherichia coli O157:H7-associated hemolytic uremic syndrome. Pediatr Res. 2001;49:653–9. Hosler GA, Cusumano AM, Hutchins GM. Thrombotic thrombocytopenic purpura and hemolytic uremic syndrome are distinct pathologic entities.

Cleavage of the ADAMTS13 propeptide is not required for protease activity. J Biol Chem. 2003;278(47):46643–8. 25. Kubota Y, Sano M, Goda S, Suzuki N, Nishiwaki K. The conserved oligomeric Golgi complex acts in organ morphogenesis via glycosylation of an ADAM protease in C. elegans. Development. 2006;133(2):263–73. 26. Nishiwaki K, Kubota Y, Chigira Y, Roy SK, Suzuki M, Schvarzstein M, Jigami Y, Hisamoto N, Matsumoto K. An NDPase links ADAM protease glycosylation with organ morphogenesis in C. elegans.

J Biol Chem. 2006;281(18):12485–94. 38. Longpre JM, Leduc R. Identification of prodomain determinants involved in ADAMTS-1 biosynthesis. J Biol Chem. 2004;279(32):33237–45. 39. Longpre JM, McCulloch DR, Koo BH, Alexander JP, Apte SS, Leduc R. Characterization of proADAMTS5 processing by proprotein convertases. Int J Biochem Cell Biol. 2009; 41(5):1116–26. pii: S1357-2725(08)00414-7. 008. Epub 2008/11/11. 40. Tortorella MD, Arner EC, Hills R, Gormley J, Fok K, Pegg L, Munie G, Malfait AM. ADAMTS-4 (aggrecanase-1): N-terminal activation mechanisms.

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