Evidence map›Paper›PMID 11238954›Full record

ArticleMolecular and cellular biology2001

Disruption of the mouse mu-calpain gene reveals an essential role in platelet function.

M Azam, S S Andrabi, K E Sahr, L Kamath, A Kuliopulos, A H Chishti

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

90 citing papers in PubMed, 238 citations in OpenAlex.

  1. Trial
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  7. Therapeutic use of calpeptin in COVID-19 infection.Clinical science (London, England : 1979) · 2022
    Article
  8. Review
  9. Article
  10. Calpains as Potential Therapeutic Targets for Myocardial Hypertrophy.International journal of molecular sciences · 2022
    Review
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30 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

M AzamSection of Hematology-Oncology Research, Departments of Medicine, Anatomy, and Cellular Biology, St. Elizabeth's Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02135, USA.
S S Andrabi
K E Sahr
L Kamath
A Kuliopulos
A H Chishti
Tufts University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conventional calpains are ubiquitous calcium-regulated cysteine proteases that have been implicated in cytoskeletal organization, cell proliferation, apoptosis, cell motility, and hemostasis. There are two forms of conventional calpains: the mu-calpain, or calpain I, which requires micromolar calcium for half-maximal activation, and the m-calpain, or calpain II, which functions at millimolar calcium concentrations. We evaluated the functional role of the 80-kDa catalytic subunit of mu-calpain by genetic inactivation using homologous recombination in embryonic stem cells. The mu-calpain-deficient mice are viable and fertile. The complete deficiency of mu-calpain causes significant reduction in platelet aggregation and clot retraction but surprisingly the mutant mice display normal bleeding times. No detectable differences were observed in the cleavage pattern and kinetics of calpain substrates such as the beta3 subunit of alphaIIbbeta3 integrin, talin, and ABP-280 (filamin). However, mu-calpain null platelets exhibit impaired tyrosine phosphorylation of several proteins including the beta3 subunit of alphaIIbbeta3 integrin, correlating with the agonist-induced reduction in platelet aggregation. These results provide the first direct evidence that mu-calpain is essential for normal platelet function, not by affecting the cleavage of cytoskeletal proteins but by potentially regulating the state of tyrosine phosphorylation of the platelet proteins.

Indexed as

Signal TransductionAdenosine DiphosphateAnimalsAntigens, CDBlood PlateletsBlood ProteinsBlotting, WesternCalcimycinCalpainCollagenContractile ProteinsEnzyme PrecursorsFilaminsGene SilencingIntegrin beta3MiceAdenosine DiphosphateAntigens, CDBlood ProteinsCalcimycinCalpainCollagenContractile ProteinsEnzyme PrecursorsFilaminsIntegrin beta3Microfilament Proteinsmu-calpain proenzymePlatelet Membrane GlycoproteinsTalinThrombinTyrosine

Identifiers

PMID11238954
PMCPMC86855
OpenAlexW2140061120

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.