Evidence map›Paper›PMID 18931337›Full record

ArticleMolecular & cellular proteomics : MCP2009

Contrasting proteome biology and functional heterogeneity of the 20 S proteasome complexes in mammalian tissues.

Aldrin V Gomes, Glen W Young, Yueju Wang, Chenggong Zong, Mansoureh Eghbali, Oliver Drews, Haojie Lu, Enrico Stefani, Peipei Ping

Abstract readComparative Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
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

52 citing papers in PubMed.

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  14. Proteasome dysfunction in cardiomyopathies.The Journal of physiology · 2017
    Review
  15. 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

9 authors.

Aldrin V GomesDepartment of Physiology and Medicine, Cardiac Proteomics and Signaling Laboratory at Cardiovascular Research Laboratory, University of California Los Angeles, School of Medicine, Los Angeles, CA 90095, USA.
Glen W Young
Yueju Wang
Chenggong Zong
Mansoureh Eghbali
Oliver Drews
Haojie Lu
Enrico Stefani
Peipei Ping

Funding

ROLE OF P38 MAPK AND PP2C IN ISCHEMIC INJURY AND PROTECTIONP01HL080111 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WEISS, JAMES N · 2005 to 2009
$11.6M
Revealing Cardiovascular Stress Regulation beyond the Diffraction LimitR01HL088640 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI STEFANI, ENRICO · 2007 to 2011
$5.3M
PKC EPSILON AND SRC PTK SIGNALING IN PRECONDITIONINGR01HL063901 · NHLBI · UNIVERSITY OF LOUISVILLE · PI PING, PEIPEI · 2000 to 2009
$3.3M
SIGNALING MECHANISMS IN PHARMACOLOGIC PRECONDITIONINGR01HL065431 · NHLBI · UNIVERSITY OF LOUISVILLE · PI PING, PEIPEI · 2000 to 2008
$2.1M
NHLBI NIH HHS HL BRG 088640NHLBI NIH HHS HL P01-80111NHLBI NIH HHS HL R01-63901NHLBI NIH HHS HL R01-65431
6 · The paper itself

Abstract

The 20 S proteasome complexes are major contributors to the intracellular protein degradation machinery in mammalian cells. Systematic administration of proteasome inhibitors to combat disease (e.g. cancer) has resulted in positive outcomes as well as adversary effects. The latter was attributed to, at least in part, a lack of understanding in the organ-specific responses to inhibitors and the potential diversity of proteomes of these complexes in different tissues. Accordingly, we conducted a proteomic study to characterize the 20 S proteasome complexes and their postulated organ-specific responses in the heart and liver. The cardiac and hepatic 20 S proteasomes were isolated from the same mouse strain with identical genetic background. We examined the molecular composition, complex assembly, post-translational modifications and associating partners of these proteasome complexes. Our results revealed an organ-specific molecular organization of the 20 S proteasomes with distinguished patterns of post-translational modifications as well as unique complex assembly characteristics. Furthermore, the proteome diversities are concomitant with a functional heterogeneity of the proteolytic patterns exhibited by these two organs. In particular, the heart and liver displayed distinct activity profiles to two proteasome inhibitors, epoxomicin and Z-Pro-Nle-Asp-H. Finally, the heart and liver demonstrated contrasting regulatory mechanisms from the associating partners of these proteasomes. The functional heterogeneity of the mammalian 20 S proteasome complexes underscores the concept of divergent proteomes among organs in the context of an identical genome.

Indexed as

Amino Acid SequenceAnimalsEnzyme InhibitorsImmunoblottingLiverMiceMice, Inbred ICRMicroscopy, ConfocalMolecular Sequence DataMyocardiumProteasome Endopeptidase ComplexProteasome InhibitorsProtein Processing, Post-TranslationalProtein SubunitsProteomeReproducibility of ResultsEnzyme InhibitorsProteasome Endopeptidase ComplexProteasome InhibitorsProtein SubunitsProteome

Identifiers

PMID18931337
PMCPMC2634581

What OpenQuestion holds

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Registered trials

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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.