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Antithrombin Dublin (-3 Val----Glu): an N-terminal variant which has an aberrant signal peptidase cleavage site.
Department of Haematology, MRC Centre, Cambridge, UK.
Antithrombin Dublin is an electrophoretically fast variant of antithrombin which has normal heparin affinity. Direct sequencing of amplified exon 2 revealed a Val----Glu substitution at position -3. N-terminal sequencing of antithrombin from two individuals, heterozygous for the Dublin mutation, showed the presence of a truncated antithrombin in which the N-terminal dipeptide is absent. We propose that the prepeptide mutation redirects signal peptidase cleavage to a site two amino acids downstream into the mature protein.
PMID: 1977621 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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Possible involvement of inefficient cleavage of preprovasopressin by signal peptidase as a cause for familial central diabetes insipidus.
Ito M, Oiso Y, Murase T, Kondo K, Saito H, Chinzei T, Racchi M, Lively MO.
J Clin Invest. 1993 Jun; 91(6):2565-71.
[J Clin Invest. 1993]
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A defective signal peptide in the maize high-lysine mutant floury 2.
Coleman CE, Lopes MA, Gillikin JW, Boston RS, Larkins BA.
Proc Natl Acad Sci U S A. 1995 Jul 18; 92(15):6828-31.
[Proc Natl Acad Sci U S A. 1995]
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Pleiotropic effects of antithrombin strand 1C substitution mutations.
Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, Abildgaard U, Ireland H, Thompson E, Sas G.
J Clin Invest. 1992 Dec; 90(6):2422-33.
[J Clin Invest. 1992]