Evidence map›Paper›PMID 12974673›Full record

ArticleThe Biochemical journal2003

Calpain facilitates GLUT4 vesicle translocation during insulin-stimulated glucose uptake in adipocytes.

David S Paul, Anne W Harmon, Courtney P Winston, Yashomati M Patel

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Calpain inhibition by calpeptin modulates adipocyte lipid metabolism and secretome-mediated inflammatory crosstalk with hepatocytes.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  4. Article
  5. Calpain and Cardiometabolic Diseases.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. The mTOR Complex Controls HIV Latency.Cell host & microbe · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Class II phosphoinositide 3-kinase C2alpha: what we learned so far.International journal of biochemistry and molecular biology · 2011
    Article
  20. Calpain chronicle--an enzyme family under multidisciplinary characterization.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011
    Review
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

4 authors at 1 institution in 1 country.

David S PaulDepartment of Nutrition, University of North Carolina School of Public Health, 2216A McGavran-Greenberg, Chapel Hill, NC 27599, USA.
Anne W Harmon
Courtney P Winston
Yashomati M Patel
University of North Carolina at Chapel Hill · US

Funding

UNIV OF NORTH CAROLINA CLINICAL NUTRITION RESEARCH UNITP30DK056350 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SUSAN M. SMITH · 1999 to 2026
$31.6M
NUTRITIONAL BIOCHEMISTRY AND EPIDEMIOLOGY OF CANCERT32CA072319 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZEISEL, STEVEN H · 1997 to 2006
$1.7M
NCI NIH HHS T32-CA72319NIDDK NIH HHS DK56350
6 · The paper itself

Abstract

Calpains are a family of non-lysosomal cysteine proteases. Recent studies have identified a member of the calpain family of proteases, calpain 10, as a putative diabetes-susceptibility gene that may be involved in the development of type 2 diabetes. Inhibition of calpain activity has been shown to reduce insulin-stimulated glucose uptake in isolated rat-muscle strips and adipocytes. In this report, we examine the mechanism by which calpain affects insulin-stimulated glucose uptake in 3T3-L1 adipocytes. Inhibition of calpain activity resulted in approx. a 60% decrease in insulin-stimulated glucose uptake. Furthermore, inhibition of calpain activity prevented the translocation of insulin-responsive glucose transporter 4 (GLUT4) vesicles to the plasma membrane, as demonstrated by fluorescent microscopy of whole cells and isolated plasma membranes; it did not, however, alter the total GLUT4 protein content. While inhibition of calpain did not affect the insulin-mediated proximal steps of the phosphoinositide 3-kinase pathway, it did prevent the insulin-stimulated cortical actin reorganization required for GLUT4 translocation. Specific inhibition of calpain 10 by antisense expression reduced insulin-stimulated GLUT4 translocation and actin reorganization. Based on these findings, we propose a role for calpain in the actin reorganization required for insulin-stimulated GLUT4 translocation to the plasma membrane in 3T3-L1 adipocytes. These studies identify calpain as a novel factor involved in GLUT4 vesicle trafficking and suggest a link between calpain activity and the development of type 2 diabetes.

Indexed as

Muscle ProteinsActin CytoskeletonAdipocytesAnimalsBiological TransportCalpainCell LineCell MembraneCysteine Proteinase InhibitorsGlucoseGlucose Transporter Type 4InsulinLeupeptinsMonosaccharide Transport ProteinsPhosphorylationProtein Transportacetylleucyl-leucyl-norleucinalCalpaincalpain 10Cysteine Proteinase InhibitorsGlucoseGlucose Transporter Type 4InsulinLeupeptinsMonosaccharide Transport ProteinsMuscle Proteins

Identifiers

PMID12974673
PMCPMC1223814
OpenAlexW2062459348

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.