Artigo Acesso aberto Revisado por pares

Aggregation of plasma Z type α 1 ‐antitrypsin suggests basic defect for the deficiency

1986; Wiley; Volume: 205; Issue: 2 Linguagem: Inglês

10.1016/0014-5793(86)80908-5

ISSN

1873-3468

Autores

D W Cox, G D Billingsley, John W. Callahan,

Tópico(s)

Peptidase Inhibition and Analysis

Resumo

The abnormal type of α 1 ‐antitrypsin, PI (protease inhibitor) type Z, is associated with inclusion bodies in the liver, which contain non‐secreted α 1 ‐antitrypsin. Our studies show that Z protein has an inherent tendency to aggregate, even in plasma. Depending upon conditions, from 15 to 70% of the Z protein in plasma was in a high‐ M r form, compared with 1.5% of M type α 1 ‐antitrypsin. The high‐ M r complex in plasma cannot be disaggregated using Triton X detergent or reducing conditions. This increased tendency to aggregate can be explained by the mutation affecting, tertiary structure and salt bridge formation in Z protein. We have observed this same tendency to aggregate for Mmalton α 1 ‐antitrypsin, a rarer variant also associated with a plasma deficiency.

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