Molecular basis of alpha 1-antitrypsin deficiency and emphysema associated with the alpha 1-antitrypsin M sub(mineral springs) allele

Evaluation of M(mineral springs) alpha 1AT as an inhibitor of neutrophil elastase, its natural substrate, demonstrated markedly lower than normal function. Characterization of the alpha 1AT M(mineral springs) gene demonstrated that it differed from the common normal M1(Ala super(213)) allele by a si...

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Published inMolecular and cellular biology Vol. 10; no. 1; pp. 47 - 56
Main Authors Curiel, D T, Vogelmeier, C, Hubbard, R C, Stier, LE, Crystal, R G
Format Journal Article
LanguageEnglish
Published 01.01.1990
Subjects
emphysema
genes
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Summary:Evaluation of M(mineral springs) alpha 1AT as an inhibitor of neutrophil elastase, its natural substrate, demonstrated markedly lower than normal function. Characterization of the alpha 1AT M(mineral springs) gene demonstrated that it differed from the common normal M1(Ala super(213)) allele by a single-base substitution causing the amino acid substitution Gly-67 (GG_G) arrow right Glu-67 (GA_G). Capitalizing on the fact that this mutation creates a polymorphism for the restriction endonuclease AvaII, family analysis demonstrated that the M(mineral springs) alpha 1AT allele was transmitted in an autosomal-codominant fashion. Evaluation fo genomic DNA showed that the index case was homozygous for the alpha 1AT M(mineral springs) allele.
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ISSN:0270-7306