Evidence map›Paper›PMID 21071702›Full record

ArticleArteriosclerosis, thrombosis, and vascular biology2011

Protein kinase C upregulates intercellular adhesion molecule-1 and leukocyte-endothelium interactions in hyperglycemia via activation of endothelial expressed calpain.

Amanda R Smolock, Gourav Mishra, Kunie Eguchi, Satoru Eguchi, Rosario Scalia

Open access · bronzeAbstract read
In one paragraph

Article in Arteriosclerosis, thrombosis, and vascular biology, 2011. 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
1.2field-weighted citation impact, top 23% 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, 38 citations in OpenAlex.

  1. Article
  2. HDL metabolism and function in diabetes mellitus.Nature reviews. Endocrinology · 2026
    Review
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  12. Kinase-SUMO networks in diabetes-mediated cardiovascular disease.Metabolism: clinical and experimental · 2016
    Review
  13. μ-Calpain as a Novel Target for Impairment of Nitric Oxide-Mediated Vascular Relaxation in Diabetes: A Mini Review.Journal of molecular and genetic medicine : an international journal of biomedical research · 2015
    Article
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  15. Article
  16. Article
  17. Review
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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

5 authors at 1 institution in 1 country.

Amanda R SmolockDepartment of Physiology and the Cardiovascular Research Center, School of Medicine, Temple University, 3500 N Broad St., Philadelphia, PA 19041, USA.
Gourav Mishra
Kunie Eguchi
Satoru Eguchi
Rosario Scalia
Thomas Jefferson University · US

Funding

ErbB Activation via a Metalloprotease by Angiotensin IIR01HL076770 · NHLBI · VANDERBILT UNIVERSITY · PI EGUCHI, SATORU · 2004 to 2012
$2.8M
Role of Calpain in Diabetic Endothelial DysfunctionR01DK064344 · NIDDK · THOMAS JEFFERSON UNIVERSITY · PI SCALIA, ROSARIO G · 2003 to 2011
$2.7M
NHLBI NIH HHS HL076770NHLBI NIH HHS R01 HL076770NIDDK NIH HHS DK064344NIDDK NIH HHS R01 DK064344
6 · The paper itself

Abstract

objectiveWe tested the hypothesis of a role for the calcium-dependent protease calpain in the endothelial dysfunction induced by hyperglycemic activation of protein kinase C (PKC). METHODS AND

resultsChronic hyperglycemia with insulin deficiency (type 1 diabetes) was induced in rats by streptozotocin. Total PKC and calpain activities, along with activity and expression level of the 2 endothelial-expressed calpains isoforms, μ- and m-calpain, were measured in vascular tissue homogenates by enzymatic assays and Western blot analysis, respectively. Intravital microscopy was used to measure and correlate leukocyte-endothelium interactions with calpain activity in the microcirculation. Expression levels and endothelial localization of the inflammatory adhesion molecule intercellular adhesion molecule-1 were studied by Western blot analysis and immunofluorescence, respectively. The mechanistic role of hyperglycemia alone in the process of PKC-induced calpain activation and actions was also investigated. We found that in the type 1 diabetic vasculature, PKC selectively upregulates the activity of the μ-calpain isoform. Mechanistic studies confirmed a role for hyperglycemia and PKCβ in this process. The functional implications of PKC-induced calpain activation were upregulation of endothelial expressed intercellular adhesion molecule-1 and leukocyte-endothelium interactions.

conclusionsOur results uncover the role of μ-calpain in the endothelial dysfunction of PKC. Calpain may represent a novel molecular target for the treatment of PKC-associated diabetic vascular disease.

Indexed as

AnimalsCalpainCell CommunicationDiabetes Mellitus, ExperimentalDiabetic AngiopathiesDisease Models, AnimalEndothelium, VascularHyperglycemiaIntercellular Adhesion Molecule-1LeukocytesMaleMesenteric ArteriesMicrocirculationProtein Kinase CRatsRats, Sprague-DawleyCalpainIntercellular Adhesion Molecule-1Protein Kinase CStreptozocin

Identifiers

PMID21071702
PMCPMC3086836
OpenAlexW2134289175

What OpenQuestion holds

Textmetadata
LicenceTDM
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.