The ubiquitin-proteasome system and its role in ethanol-induced disorders

Research output: Contribution to journalReview article

34 Citations (Scopus)

Abstract

Some of the most fundamental yet important cellular activities such as cell division and gene expression are controlled by short-lived regulatory proteins. The levels of these proteins are controlled by their rates of degradation. Similarly, protein catabolism plays a crucial role in prolonging cellular life by destroying damaged proteins that are potentially cytotoxic. A major player in these catabolic reactions is the ubiquitin-proteasome system, a novel proteolytic system that has become the primary proteolytic pathway in eukaryotic cells. Ubiquitin-mediated proteolysis is now regarded as the major pathway by which most intracellular proteins are destroyed. Equally important, from a toxicological standpoint, is that the ubiquitin-proteasome system is also widely considered to be a cellular defense mechanism, since it is involved in the removal of damaged proteins generated by adduct formation and oxidative stress. This review describes the history and the components of the ubiquitin-proteasome system, its regulation and its role in pathological states, with the major emphasis on ethanol-induced organ injury. The available literature cited here deals mainly with the effects of ethanol consumption on the ubiquitin-proteasome pathway in the liver. However, since this proteolytic system is an essential pathway in all cells it is an attractive experimental model and therapeutic target in extrahepatic organs such as the brain and heart that are also affected by excessive alcohol consumption.

Original languageEnglish (US)
Pages (from-to)15-28
Number of pages14
JournalAddiction Biology
Volume7
Issue number1
DOIs
StatePublished - Feb 2 2002

Fingerprint

Proteasome Endopeptidase Complex
Ubiquitin
Ethanol
Proteins
Eukaryotic Cells
Defense Mechanisms
Alcohol Drinking
Cell Division
Toxicology
Proteolysis
Oxidative Stress
Theoretical Models
History
Gene Expression
Liver
Wounds and Injuries
Brain

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Pharmacology
  • Psychiatry and Mental health

Cite this

The ubiquitin-proteasome system and its role in ethanol-induced disorders. / Donohue, Terrence.

In: Addiction Biology, Vol. 7, No. 1, 02.02.2002, p. 15-28.

Research output: Contribution to journalReview article

@article{d34663f4e6c5495591132565fa20b20c,
title = "The ubiquitin-proteasome system and its role in ethanol-induced disorders",
abstract = "Some of the most fundamental yet important cellular activities such as cell division and gene expression are controlled by short-lived regulatory proteins. The levels of these proteins are controlled by their rates of degradation. Similarly, protein catabolism plays a crucial role in prolonging cellular life by destroying damaged proteins that are potentially cytotoxic. A major player in these catabolic reactions is the ubiquitin-proteasome system, a novel proteolytic system that has become the primary proteolytic pathway in eukaryotic cells. Ubiquitin-mediated proteolysis is now regarded as the major pathway by which most intracellular proteins are destroyed. Equally important, from a toxicological standpoint, is that the ubiquitin-proteasome system is also widely considered to be a cellular defense mechanism, since it is involved in the removal of damaged proteins generated by adduct formation and oxidative stress. This review describes the history and the components of the ubiquitin-proteasome system, its regulation and its role in pathological states, with the major emphasis on ethanol-induced organ injury. The available literature cited here deals mainly with the effects of ethanol consumption on the ubiquitin-proteasome pathway in the liver. However, since this proteolytic system is an essential pathway in all cells it is an attractive experimental model and therapeutic target in extrahepatic organs such as the brain and heart that are also affected by excessive alcohol consumption.",
author = "Terrence Donohue",
year = "2002",
month = "2",
day = "2",
doi = "10.1080/135562101200100562",
language = "English (US)",
volume = "7",
pages = "15--28",
journal = "Addiction Biology",
issn = "1355-6215",
publisher = "Wiley-Blackwell",
number = "1",

}

TY - JOUR

T1 - The ubiquitin-proteasome system and its role in ethanol-induced disorders

AU - Donohue, Terrence

PY - 2002/2/2

Y1 - 2002/2/2

N2 - Some of the most fundamental yet important cellular activities such as cell division and gene expression are controlled by short-lived regulatory proteins. The levels of these proteins are controlled by their rates of degradation. Similarly, protein catabolism plays a crucial role in prolonging cellular life by destroying damaged proteins that are potentially cytotoxic. A major player in these catabolic reactions is the ubiquitin-proteasome system, a novel proteolytic system that has become the primary proteolytic pathway in eukaryotic cells. Ubiquitin-mediated proteolysis is now regarded as the major pathway by which most intracellular proteins are destroyed. Equally important, from a toxicological standpoint, is that the ubiquitin-proteasome system is also widely considered to be a cellular defense mechanism, since it is involved in the removal of damaged proteins generated by adduct formation and oxidative stress. This review describes the history and the components of the ubiquitin-proteasome system, its regulation and its role in pathological states, with the major emphasis on ethanol-induced organ injury. The available literature cited here deals mainly with the effects of ethanol consumption on the ubiquitin-proteasome pathway in the liver. However, since this proteolytic system is an essential pathway in all cells it is an attractive experimental model and therapeutic target in extrahepatic organs such as the brain and heart that are also affected by excessive alcohol consumption.

AB - Some of the most fundamental yet important cellular activities such as cell division and gene expression are controlled by short-lived regulatory proteins. The levels of these proteins are controlled by their rates of degradation. Similarly, protein catabolism plays a crucial role in prolonging cellular life by destroying damaged proteins that are potentially cytotoxic. A major player in these catabolic reactions is the ubiquitin-proteasome system, a novel proteolytic system that has become the primary proteolytic pathway in eukaryotic cells. Ubiquitin-mediated proteolysis is now regarded as the major pathway by which most intracellular proteins are destroyed. Equally important, from a toxicological standpoint, is that the ubiquitin-proteasome system is also widely considered to be a cellular defense mechanism, since it is involved in the removal of damaged proteins generated by adduct formation and oxidative stress. This review describes the history and the components of the ubiquitin-proteasome system, its regulation and its role in pathological states, with the major emphasis on ethanol-induced organ injury. The available literature cited here deals mainly with the effects of ethanol consumption on the ubiquitin-proteasome pathway in the liver. However, since this proteolytic system is an essential pathway in all cells it is an attractive experimental model and therapeutic target in extrahepatic organs such as the brain and heart that are also affected by excessive alcohol consumption.

UR - http://www.scopus.com/inward/record.url?scp=0036150886&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036150886&partnerID=8YFLogxK

U2 - 10.1080/135562101200100562

DO - 10.1080/135562101200100562

M3 - Review article

C2 - 11900619

AN - SCOPUS:0036150886

VL - 7

SP - 15

EP - 28

JO - Addiction Biology

JF - Addiction Biology

SN - 1355-6215

IS - 1

ER -