Protein degradation by the 26S proteasome system in the normal and stressed myocardium

Aldrin V Gomes, Chenggong Zong, Peipei Ping

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

The 26S proteasome is a multicatalytic threonine protease complex responsible for degradation of the majority of proteins in eukaryotic cells. In the last two decades, the ubiquitin proteasome system (UPS) has been increasingly recognized as an integral component in numerous biologic processes including cell proliferation, adaptation to stress, and cell death. The turnover of intracellular proteins inevitably affects the contributions of these molecules to cellular networks and pathways in any given tissue or organ, including the myocardium. Perturbations in the protein-degradation process have been shown to affect protein turnover and thereby affect the cardiac cell functions thai these molecules are designated to carry out, engendering diseased cardiac phenotypes. Recent studies have implicated the role of proteasomes in stressed cardiac phenotypes including postischemia-reperfusion injury and cardiac remodeling (e.g., heart failure). The 26S proteasomes also appear to be susceptible to modulation by stresses (e.g., reactive oxygen species). This review focuses on roles of the 26S proteasome system in protein degradation; it provides an overview of the progress made in cardiac proteasome research as well as a discussion of recent controversies regarding the UPS system in diseased cardiac phenotypes.

Original languageEnglish (US)
Pages (from-to)1677-1691
Number of pages15
JournalAntioxidants and Redox Signaling
Volume8
Issue number9-10
DOIs
StatePublished - Sep 2006

Fingerprint

Proteasome Endopeptidase Complex
Proteolysis
Myocardium
Degradation
Ubiquitin
Phenotype
Heart Diseases
Proteins
Eukaryotic Cells
Threonine
Reperfusion Injury
Molecules
Cell proliferation
Cell death
Reactive Oxygen Species
Peptide Hydrolases
Cell Death
Heart Failure
Cell Proliferation
Modulation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Protein degradation by the 26S proteasome system in the normal and stressed myocardium. / Gomes, Aldrin V; Zong, Chenggong; Ping, Peipei.

In: Antioxidants and Redox Signaling, Vol. 8, No. 9-10, 09.2006, p. 1677-1691.

Research output: Contribution to journalArticle

Gomes, Aldrin V ; Zong, Chenggong ; Ping, Peipei. / Protein degradation by the 26S proteasome system in the normal and stressed myocardium. In: Antioxidants and Redox Signaling. 2006 ; Vol. 8, No. 9-10. pp. 1677-1691.
@article{667c6fd11cc149e98f15f2c40a9bee75,
title = "Protein degradation by the 26S proteasome system in the normal and stressed myocardium",
abstract = "The 26S proteasome is a multicatalytic threonine protease complex responsible for degradation of the majority of proteins in eukaryotic cells. In the last two decades, the ubiquitin proteasome system (UPS) has been increasingly recognized as an integral component in numerous biologic processes including cell proliferation, adaptation to stress, and cell death. The turnover of intracellular proteins inevitably affects the contributions of these molecules to cellular networks and pathways in any given tissue or organ, including the myocardium. Perturbations in the protein-degradation process have been shown to affect protein turnover and thereby affect the cardiac cell functions thai these molecules are designated to carry out, engendering diseased cardiac phenotypes. Recent studies have implicated the role of proteasomes in stressed cardiac phenotypes including postischemia-reperfusion injury and cardiac remodeling (e.g., heart failure). The 26S proteasomes also appear to be susceptible to modulation by stresses (e.g., reactive oxygen species). This review focuses on roles of the 26S proteasome system in protein degradation; it provides an overview of the progress made in cardiac proteasome research as well as a discussion of recent controversies regarding the UPS system in diseased cardiac phenotypes.",
author = "Gomes, {Aldrin V} and Chenggong Zong and Peipei Ping",
year = "2006",
month = "9",
doi = "10.1089/ars.2006.8.1677",
language = "English (US)",
volume = "8",
pages = "1677--1691",
journal = "Antioxidants and Redox Signaling",
issn = "1523-0864",
publisher = "Mary Ann Liebert Inc.",
number = "9-10",

}

TY - JOUR

T1 - Protein degradation by the 26S proteasome system in the normal and stressed myocardium

AU - Gomes, Aldrin V

AU - Zong, Chenggong

AU - Ping, Peipei

PY - 2006/9

Y1 - 2006/9

N2 - The 26S proteasome is a multicatalytic threonine protease complex responsible for degradation of the majority of proteins in eukaryotic cells. In the last two decades, the ubiquitin proteasome system (UPS) has been increasingly recognized as an integral component in numerous biologic processes including cell proliferation, adaptation to stress, and cell death. The turnover of intracellular proteins inevitably affects the contributions of these molecules to cellular networks and pathways in any given tissue or organ, including the myocardium. Perturbations in the protein-degradation process have been shown to affect protein turnover and thereby affect the cardiac cell functions thai these molecules are designated to carry out, engendering diseased cardiac phenotypes. Recent studies have implicated the role of proteasomes in stressed cardiac phenotypes including postischemia-reperfusion injury and cardiac remodeling (e.g., heart failure). The 26S proteasomes also appear to be susceptible to modulation by stresses (e.g., reactive oxygen species). This review focuses on roles of the 26S proteasome system in protein degradation; it provides an overview of the progress made in cardiac proteasome research as well as a discussion of recent controversies regarding the UPS system in diseased cardiac phenotypes.

AB - The 26S proteasome is a multicatalytic threonine protease complex responsible for degradation of the majority of proteins in eukaryotic cells. In the last two decades, the ubiquitin proteasome system (UPS) has been increasingly recognized as an integral component in numerous biologic processes including cell proliferation, adaptation to stress, and cell death. The turnover of intracellular proteins inevitably affects the contributions of these molecules to cellular networks and pathways in any given tissue or organ, including the myocardium. Perturbations in the protein-degradation process have been shown to affect protein turnover and thereby affect the cardiac cell functions thai these molecules are designated to carry out, engendering diseased cardiac phenotypes. Recent studies have implicated the role of proteasomes in stressed cardiac phenotypes including postischemia-reperfusion injury and cardiac remodeling (e.g., heart failure). The 26S proteasomes also appear to be susceptible to modulation by stresses (e.g., reactive oxygen species). This review focuses on roles of the 26S proteasome system in protein degradation; it provides an overview of the progress made in cardiac proteasome research as well as a discussion of recent controversies regarding the UPS system in diseased cardiac phenotypes.

UR - http://www.scopus.com/inward/record.url?scp=33750920449&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750920449&partnerID=8YFLogxK

U2 - 10.1089/ars.2006.8.1677

DO - 10.1089/ars.2006.8.1677

M3 - Article

C2 - 16987021

AN - SCOPUS:33750920449

VL - 8

SP - 1677

EP - 1691

JO - Antioxidants and Redox Signaling

JF - Antioxidants and Redox Signaling

SN - 1523-0864

IS - 9-10

ER -