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Article

Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-antitrypsin deficiency.

Hepatology (Baltimore, Md.) - 1 May 2013

Ordóñez Adriana, Snapp Erik L, Tan Lu, Miranda Elena, Marciniak Stefan J, Lomas David A

Abstract excerpt

UNLABELLED: Point mutants of alpha1 -antitrypsin (α1AT) form ordered polymers that are retained as inclusions within the endoplasmic reticulum (ER) of hepatocytes in association with neonatal hepatitis, cirrhosis, and hepatocellular carcinoma. These inclusions cause cell damage and predispose to ER stress in the absence of the classical unfolded protein response (UPR). The pathophysiology underlying this ER...

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Identifiers

PMID: 23197448
DOI: 10.1002/hep.26173
PMCID: PMC3871212

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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