Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum.

American journal of physiology. Gastrointestinal and liver physiology - 1 Sept 2005

Schmidt Bela Z, Perlmutter David H

Abstract excerpt

In alpha1-antitrypsin (alpha1-AT) deficiency, a mutant form of alpha1-AT polymerizes in the endoplasmic reticulum (ER) of liver cells resulting in chronic hepatitis and hepatocellular carcinoma by a gain of toxic function mechanism. Although some aspects of the cellular response to mutant alpha1-AT Z have been partially characterized, including the involvement of several proteasomal and nonproteasomal mechanisms...

Topics

Cell Culture Techniques
Endoplasmic Reticulum
Endoplasmic Reticulum Chaperone BiP
Fibroblasts
Glycoproteins
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Humans
Membrane Proteins
Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Solubility

alpha 1-Antitrypsin

alpha 1-Antitrypsin Deficiency

Source

Identifiers

PMID: 15845869
DOI: 10.1152/ajpgi.00237.2004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum.PMID 15845869Read ↗

Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response.Semantic proximity Read ↗

Regulator of G Signaling 16 is a marker for the distinct endoplasmic reticulum stress state associated with aggregated mutant alpha1-antitrypsin Z in the classical form of alpha1-antitrypsin deficiency.Semantic proximity Read ↗

Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency.Semantic proximity Read ↗

A naturally occurring nonpolymerogenic mutant of alpha 1-antitrypsin characterized by prolonged retention in the endoplasmic reticulum.Semantic proximity Read ↗

Activation of the c-Jun N-terminal kinase pathway aggravates proteotoxicity of hepatic mutant Z alpha1-antitrypsin.Semantic proximity Read ↗

New Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Semantic proximity Read ↗

SVIP regulates Z variant alpha-1 antitrypsin retro-translocation by inhibiting ubiquitin ligase gp78.Semantic proximity Read ↗

Molecular characterization of the new defective P(brescia) alpha1-antitrypsin allele.Semantic proximity Read ↗

Endoplasmic reticulum stress--a double edged sword for Z alpha-1 antitrypsin deficiency hepatoxicity.Semantic proximity Read ↗

Alpha-1 Antitrypsin Inclusions Sequester GRP78 in a Bile Acid-Inducible Manner.Semantic proximity Read ↗

Mitochondrial autophagy and injury in the liver in alpha 1-antitrypsin deficiency.Semantic proximity Read ↗

The endoplasmic reticulum remains functionally connected by vesicular transport after its fragmentation in cells expressing Z-α1-antitrypsin.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.