Evidence map›Paper›PMID 18337374›Full record

ArticleMolecular & cellular proteomics : MCP2008

Proteomics analysis identifies molecular targets related to diabetes mellitus-associated bladder dysfunction.

Elizabeth Yohannes, Jinsook Chang, George J Christ, Kelvin P Davies, Mark R Chance

Open access · hybridAbstract readValidation Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  4. Path of translational discovery of urological complications of obesity and diabetes.American journal of physiology. Renal physiology · 2017
    Review
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  14. Review
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  19. Urinary protein profiles in a rat model for diabetic complications.Molecular & cellular proteomics : MCP · 2009
    Article
  20. 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

5 authors at 3 institutions in 1 country.

Elizabeth YohannesCase Center for Proteomics, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Jinsook Chang
George J Christ
Kelvin P Davies
Mark R Chance
Case Western Reserve University · USAlbert Einstein College of Medicine · USWake Forest University · US

Funding

Whole Animal PhysiologyP01DK060037 · NIDDK · YESHIVA UNIVERSITY · PI MELMAN, ARNOLD · 2003 to 2007
$6.9M
Center for Synchrotron BiosciencesP41EB001979 · NIBIB · YESHIVA UNIVERSITY · PI CHANCE, MARK R · 2003 to 2008
$5.6M
Proteomic Approaches to Type l Diabetes ProgressionR21DK070229 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2004 to 2005
$637k
NIBIB NIH HHS P41 EB001979NIBIB NIH HHS P41-EB-1979NIDDK NIH HHS P01 DK060037NIDDK NIH HHS P01-DK060037NIDDK NIH HHS R21 DK-070229NIDDK NIH HHS R21 DK070229
6 · The paper itself

Abstract

Protein expression profiles in rat bladder smooth muscle were compared between animal models of streptozotocin-induced diabetes mellitus (STZ-DM) and age-matched controls at 1 week and 2 months after induction of hyperglycemia with STZ treatment. At each time point, protein samples from four STZ-DM and four age-matched control rat bladder tissues were prepared independently and analyzed together across multiple DIGE gels using a pooled internal standard sample to quantify expression changes with statistical confidence. A total of 100 spots were determined to be significantly changing among the four experimental groups. A subsequent mass spectrometry analysis of the 100 spots identified a total of 56 unique proteins. Of the proteins identified by two-dimensional DIGE/MS, 10 exhibited significant changes 1 week after STZ-induced hyperglycemia, whereas the rest showed differential expression after 2 months. A network analysis of these proteins using MetaCore suggested induction of transcriptional factors that are too low to be detected by two-dimensional DIGE and identified an enriched cluster of down-regulated proteins that are involved in cell adhesion, cell shape control, and motility, including vinculin, intermediate filaments, Ppp2r1a, and extracellular matrix proteins. The proteins that were up-regulated include proteins involved in muscle contraction (e.g. Mrlcb and Ly-GDI), in glycolysis (e.g. alpha-enolase and Taldo1), in mRNA processing (e.g. heterogeneous nuclear ribonucleoprotein A2/B1), in inflammatory response (e.g. S100A9, Annexin 1, and apoA-I), and in chromosome segregation and migration (e.g. Tuba1 and Vil2). Our results suggest that the development of diabetes-related complications in this model involves the down-regulation of structural and extracellular matrix proteins in smooth muscle that are essential for normal muscle contraction and relaxation but also induces proteins that are associated with cell proliferation and inflammation that may account for some of the functional deficits known to occur in diabetic complications of bladder.

Indexed as

ProteomicsAnimalsBiomarkersDiabetes Mellitus, ExperimentalHyperglycemiaMaleProteomeRatsRats, Inbred F344StreptozocinTime FactorsUrinary Bladder DiseasesBiomarkersProteomeStreptozocin

Identifiers

PMID18337374
PMCPMC2493381
OpenAlexW2002755192

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.