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This Article Full Text Full Text (PDF) Erratum (v99,p2290) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Pinotti, M. Articles by Bernardi, F. Search for Related Content PubMed PubMed Citation Articles by Pinotti, M. Articles by Bernardi, F. Related Collections Hemostasis, Thrombosis, and Vascular Biology Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 February 2002, Vol. 99, No. 4, pp. 1495-1497 BRIEF REPORT Residual factor VII activity and different hemorrhagic phenotypes in CRM+ factor VII deficiencies (Gly331Ser and Gly283Ser) Mirko Pinotti, Daniela Etro, Debora Bindini, Maria Luisa Papa, Giuseppina Rodorigo, Angiola Rocino, Guglielmo Mariani, Nicola Ciavarella, and Francesco Bernardi From the Dipartimento di Biochimica e Biologia Molecolare-CIBF, University of Ferrara, Italy; Centro Emofilia e Trombosi, Ospedale Nuovo Pellegrini, Naples, Italy; Divisione di Angiologia, Azienda Ospedaliera, Policlinico S Orsola-Malpighi, Bologna, Italy; Divisione di Ematologia, University of Palermo, Italy; Centro Emofilia e Trombosi, Ospedale Consorziale, Policlinico, Bari, Italy. Two cross-reacting material-positive (CRM+) factor VII (FVII) mutations, associated with similar reductions in coagulant activity (2.5%) but with mild to asymptomatic (Gly331Ser, c184 [in chymotrypsin numbering]) or severe (Gly283Ser, c140) hemorrhagic phenotypes, were investigated. The affected glycines belong to structurally conserved regions in the c184 through c193 and c140s activation domain loops, respectively. The natural mutants 331Ser-FVII and 283Ser-FVII were expressed, and in addition 331Ala-FVII and 283Ala-FVII were expressed because 3 functional serine-proteases bear alanine at these positions. The 331Ser-FVII, present in several asymptomatic subjects, showed detectable factor Xa generation activity in patient plasma (0.7% ± 0.2%) and in reconstituted system with the recombinant molecules (2.7% ± 1.1%). The reduced activity of recombinant 283Ala-FVII (7.2% ± 2.2%) indicates that the full function of FVII requires glycine at this position, and the undetectable activity of 283Ser-FVII suggests that the oxydrile group of Ser283 participates in causing severe CRM+ deficiency. Furthermore, in a plasma system with limiting thromboplastin concentration, 283Ser-FVII inhibited wild-type FVIIa activity in a dose-dependent manner. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. Pinotti, D. Balestra, L. Rizzotto, I. Maestri, F. Pagani, and F. Bernardi Rescue of coagulation factor VII function by the U1+5A snRNA Blood, June 18, 2009; 113(25): 6461 - 6464. [Abstract] [Full Text] [PDF] C. Bertolucci, M. Pinotti, I. Colognesi, A. Foa, F. Bernardi, and F. Portaluppi Circadian Rhythms in Mouse Blood Coagulation J Biol Rhythms, June 1, 2005; 20(3): 219 - 224. [Abstract] [PDF] M. Pinotti, C. Bertolucci, F. Portaluppi, I. Colognesi, E. Frigato, A. Foa, and F. Bernardi Daily and Circadian Rhythms of Tissue Factor Pathway Inhibitor and Factor VII Activity Arterioscler. Thromb. Vasc. Biol., March 1, 2005; 25(3): 646 - 649. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020