Evidence map›Paper›PMID 9326644›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Functional cleavage of the common cytokine receptor gamma chain (gammac) by calpain.

M Noguchi, A Sarin, M J Aman, H Nakajima, E W Shores, P A Henkart, W J Leonard

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
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

20 citing papers in PubMed, 74 citations in OpenAlex.

  1. PGENature · 2024
    Article
  2. The common γ-chain cytokine receptor: tricks-and-treats for T cells.Cellular and molecular life sciences : CMLS · 2016
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Calpain chronicle--an enzyme family under multidisciplinary characterization.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011
    Review
  10. Article
  11. Review
  12. WIP is a chaperone for Wiskott-Aldrich syndrome protein (WASP).Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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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

7 authors at 3 institutions in 1 country.

M NoguchiLaboratory of Molecular Immunology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
A Sarin
M J Aman
H Nakajima
E W Shores
P A Henkart
W J Leonard
National Cancer Institute · USNational Institutes of Health · USCenter for Biologics Evaluation and Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small subunit of calpain, a calcium-dependent cysteine protease, was found to interact with the cytoplasmic domain of the common cytokine receptor gamma chain (gammac) in a yeast two-hybrid interaction trap assay. This interaction was functional as demonstrated by the ability of calpain to cleave in vitro-translated wild-type gammac, but not gammac containing a mutation in the PEST (proline, glutamate, serine, and threonine) sequence in its cytoplasmic domain, as well as by the ability of endogenous calpain to mediate cleavage of gammac in a calcium-dependent fashion. In T cell receptor-stimulated murine thymocytes, calpain inhibitors decreased cleavage of gammac. Moreover, in single positive CD4(+) thymocytes, not only did a calpain inhibitor augment CD3-induced proliferation, but antibodies to gammac blocked this effect. Finally, treatment of cells with ionomycin could inhibit interleukin 2-induced STAT protein activation, but this inhibition could be reversed by calpain inhibitors. Together, these data suggest that calpain-mediated cleavage of gammac represents a mechanism by which gammac-dependent signaling can be controlled.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBase SequenceCalpainCD4-Positive T-LymphocytesCells, CulturedDNA PrimersGlutamic AcidHumansInterleukin-2IonomycinLymphocyte ActivationMacromolecular SubstancesMiceMice, Inbred C57BLCalpainDNA PrimersGlutamic AcidInterleukin-2IonomycinMacromolecular SubstancesProlineReceptor-CD3 Complex, Antigen, T-CellReceptors, CytokineRecombinant ProteinsSerineThreonine

Identifiers

PMID9326644
PMCPMC23528
OpenAlexW1986284147

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.