|
|
 Previous Article | Table of Contents | Next Article 
Mutations in the Human Factor XII Gene
Manfred Schloesser,
Sacha Zeerleder,
Gerd Lutze,
Walter-Michael Halbmayer,
Sigrun Hofferbert,
Bernd Hinney,
Heinz Koestering,
Bernhard Lämmle,
Gerhard Pindur,
Karsten Thies,
Michael Köhler, and
Wolfgang Engel
From the Institut fuer Humangenetik der Universitaet Goettingen, Goettingen, Germany; Haematologisches Zentrallabor, Inselspital Universitaetsspital Bern, Bern, Switzerland; Institut fuer Klinische Chemie, Universitaet Magdeburg, Magdeburg, Germany; Institut fuer Laboratoriumsmedizin, Krankenhaus der Stadt Wien-Lainz, Wien, Austria; Frauenklinik der Universitaet Goettingen, Goettingen, Germany; Abteilung fuer Haematologie und Onkologie der Universitaet Goettingen, Goettingen, Germany; Klinische Haemostasiologie, Universitaetsklinik des Saarlands, Homburg/Saar, Germany; Institut fuer Transfusionsmedizin der Universitaet Goettingen, Goettingen, Germany; and Institut fuer Transfusionsmedizin, Ludwigshafen, Germany.
The factor XII gene from 31 unrelated factor XII-deficient patients from Germany, Switzerland, and Austria was screened for mutations at the genomic level. Several novel mutations were detected and their absence in a control group of 74 healthy unrelated individuals was checked. Most changes are in the serine protease domain affecting the catalytic triad His-393-Asp-442-Ser-544; two missense mutations, R398Q (arginine 398 to glutamine; gene bank accession no. U71276) and L395M (leucine 395 to methionine; gene bank accession no. U71277), are close to the active site histidine at position 393. Another mutation detected in a cross-reacting material (CRM)-positive female with a history of three abortions affects the active site aspartic acid by changing it to asparagine (D442N; gene bank accession no. U71275). The novel mutation G570R (glycine 570 to arginine; gene bank accession no. U71274) giving rise to a CRM-positive phenotype is located next to Cys571, which forms a vital disulfide bridge. Two mutations are causing reading frame shifts: one single basepair deletion in exon 12 [exon 12: 10590(DelC); gene bank accession no. U71278] and one acceptor splice site mutation [exon 14: 11397(G  A); gene bank accession no. L43615]. The putative regulatory mutation exon 1:-8 (g c) in the upstream region of the gene is associated with an aberrant Taq I restriction site allele in intron B of the gene (gene bank accession no. X80393).
Blood, Vol. 90 No. 10 (November 15), 1997:
pp. 3967-3977
© 1997 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:
|
|
|
|
 
N. Fujihara, M. Tozuka, K. Yamauchi, I. Ueno, N. Urasawa, S. Ishikawa, M. Hirota-Kawadobora, N. Okumura, H. Hidaka, and T. Katsuyama
Characterization of Factor XII Tenri, a Rare CRM-Negative Factor XII Deficiency
Ann. Clin. Lab. Sci.,
April 1, 2004;
34(2):
218 - 225.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Kondo, F. Tokunaga, S. Kawano, Y. Oono, S. Kumagai, and T. Koide
Factor XII Tenri, a Novel Cross-Reacting Material Negative Factor XII Deficiency, Occurs Through a Proteasome-Mediated Degradation
Blood,
June 15, 1999;
93(12):
4300 - 4308.
[Abstract]
[Full Text]
[PDF]
|
|
|
| |
