Structure and variation of human α1–antitrypsin

@article{Carrell1982StructureAV,
  title={Structure and variation of human $\alpha$1–antitrypsin},
  author={Robin W. Carrell and Jan O. Jeppsson and Carl Bertil Laurell and Stephen O. Brennan and Maurice C. Owen and Lloyd Vaughan and D. R. Boswell},
  journal={Nature},
  year={1982},
  volume={298},
  pages={329-334}
}
The sequence of α1–antitrypsin is in keeping with its role as a tissue scavenger of leukocyte elastase. Two abnormal variants commonly present in Europeans cause a deficiency that predisposes them to a progressive loss of lung elasticity. The nature of the reactive centre helps explain why cigarette smoking greatly accelerates the onset and severity of this degenerative process to give the disease emphysema. 
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References

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TLDR
The proportion of the variant form, and family studies, strongly support a single autosomal locus for α-1-antitrypsin.
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TLDR
The results strongly suggest an abnormal amino acid sequence in the peptide chain of the deficient antitrypsin and the interference with glycosylation may be related to steric hindrance.
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TLDR
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TLDR
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TLDR
It is considered probable that heterozygous (PiMZ) alpha 1-antitrypsin deficiency is associated with an increased incidence of cirrhosis, hepatic fibrosis, and hepatocellular carcinoma.
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TLDR
Lower respiratory tract of non-smoking individuals with normal serum antiproteases and individuals with PiZ homozygous alpha 1-antitrypsin deficiency underwent bronchoalveolar lavage to evaluate the antiprotease screen of their lower respiratory tract, suggesting their vulnerability to neutrophil elastase is always present.
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A human alpha1-antitrypsin variant protein was purified to homogeneity from homozygous variant subjects (Pi-ZZ) who had a deficiency of plasma trypsin inhibitory capacity. Molecular weight, specific…
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