Evidence map›Paper›PMID 26512890›Full record

ArticlePloS one2015

Deficient and Null Variants of SERPINA1 Are Proteotoxic in a Caenorhabditis elegans Model of α1-Antitrypsin Deficiency.

Erin E Cummings, Linda P O'Reilly, Dale E King, Richard M Silverman, Mark T Miedel, Cliff J Luke, David H Perlmutter, Gary A Silverman, Stephen C Pak

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Alpha-1 Asthma Overlap Syndrome: a Clinical Overview.Current allergy and asthma reports · 2022
    Review
  4. Review
  5. Article
  6. Cellular clearance of circulating transthyretin decreases cell-nonautonomous proteotoxicity inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Erin E CummingsDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.
Linda P O'ReillyDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.
Dale E KingDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.
Richard M SilvermanDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.
Mark T MiedelDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.
Cliff J LukeDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.
David H PerlmutterDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America; Department of Cell Biology and Molecular Physiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Gary A SilvermanDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America; Department of Cell Biology and Molecular Physiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Stephen C PakDepartment of Pediatrics, University of Pittsburgh School of Medicine, Children's Hospital of Pittsburgh of UPMC, Pittsburgh, Pennsylvania, United States of America.

Funding

Pediatric Scientist Development Program (PSDP) [K12]K12HD000850 · NICHD · YALE UNIVERSITY · PI Sallie R. Permar · 1987 to 2026
$44.1M
Treating AT Deficiency with Drugs that Modulate the Proteostasis NetworkP01DK096990 · NIDDK · WASHINGTON UNIVERSITY · PI SILVERMAN, GARY ARTHUR · 2012 to 2023
$18.3M
Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
High Throughput Genetic and Drug Screens for Alph-1-Antitrypsin DeficiencyR01DK079806 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SILVERMAN, GARY ARTHUR · 2008 to 2011
$2.4M
Intracellular Serpin Regulation of Intestinal Cell NecrosisR01DK081422 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SILVERMAN, GARY ARTHUR · 2009 to 2012
$1.6M
NICHD NIH HHS K12 HD000850NICHD NIH HHS K12-HD000850NIDDK NIH HHS DK079806NIDDK NIH HHS DK081422NIDDK NIH HHS P01 DK096990NIDDK NIH HHS R01 DK079806NIDDK NIH HHS R01 DK081422NIH HHS P40 OD010440
6 · The paper itself

Abstract

α1-antitrypsin deficiency (ATD) predisposes patients to both loss-of-function (emphysema) and gain-of-function (liver cirrhosis) phenotypes depending on the type of mutation. Although the Z mutation (ATZ) is the most prevalent cause of ATD, >120 mutant alleles have been identified. In general, these mutations are classified as deficient (<20% normal plasma levels) or null (<1% normal levels) alleles. The deficient alleles, like ATZ, misfold in the ER where they accumulate as toxic monomers, oligomers and aggregates. Thus, deficient alleles may predispose to both gain- and loss-of-function phenotypes. Null variants, if translated, typically yield truncated proteins that are efficiently degraded after being transiently retained in the ER. Clinically, null alleles are only associated with the loss-of-function phenotype. We recently developed a C. elegans model of ATD in order to further elucidate the mechanisms of proteotoxicity (gain-of-function phenotype) induced by the aggregation-prone deficient allele, ATZ. The goal of this study was to use this C. elegans model to determine whether different types of deficient and null alleles, which differentially affect polymerization and secretion rates, correlated to any extent with proteotoxicity. Animals expressing the deficient alleles, Mmalton, Siiyama and S (ATS), showed overall toxicity comparable to that observed in patients. Interestingly, Siiyama expressing animals had smaller intracellular inclusions than ATZ yet appeared to have a greater negative effect on animal fitness. Surprisingly, the null mutants, although efficiently degraded, showed a relatively mild gain-of-function proteotoxic phenotype. However, since null variant proteins are degraded differently and do not appear to accumulate, their mechanism of proteotoxicity is likely to be different to that of polymerizing, deficient mutants. Taken together, these studies showed that C. elegans is an inexpensive tool to assess the proteotoxicity of different AT variants using a transgenic approach.

Indexed as

MutationAllelesalpha 1-Antitrypsin DeficiencyAmino Acid SequenceAnimalsCaenorhabditis elegansMolecular Sequence DataProtein TransportProteolysisSerpinsSerpins

Identifiers

PMID26512890
PMCPMC4626213

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.