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PMID: 8168153 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Peroxisome proliferator-activated receptor (PPAR): structure, mechanisms of activation and diverse functions.

Cell structure and function ·Vol. 18 ·No. 5 ·1993-10-00 ·Pages 267-77

Motojima K

Abstract

The structurally diverse xenobiotic peroxisome proliferators (PPs) increase the number of peroxisomes per cell and the levels of several enzymes, and cause hepatomegaly, often leading to hepatocarcinogenesis in a species- and tissue-specific manner. The deadlocked problems of the molecular mechanism of PP action and its physiological meanings have begun to be understood through cDNA cloning of a PP-activated receptor (PPAR). PPAR, a member of the steroid/thyroid/vitamin superfamily of nuclear receptors, has isoforms and differentially heterodimerizes with other nuclear receptors, providing potential mechanisms not only for species- and tissue-specific actions but also for diverse actions of PPs. Recent findings related to PPAR are summarized, and its possible role in lipid metabolism and involvement in PP-induced hepatocarcinogenesis are discussed.

MeSH Terms
Amino Acid Sequence Base Sequence Microbodies/metabolism Molecular Sequence Data Receptors, Cytoplasmic and Nuclear/chemistry,genetics,metabolism,physiology Transcription Factors/chemistry,genetics,metabolism,physiology
Chemicals
Receptors, Cytoplasmic and Nuclear Transcription Factors
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Motojima K
Department of Biochemistry, School of Pharmaceutical Sciences, Toho University, Chiba, Japan.
Article Info
Journal
Cell structure and function
Abbr.
Cell Struct Funct
ISSN
0386-7196
Published
1993-10-00
Pages
267-77
Language
English
Region
Japan
NLM ID
7608465
Subset
IM
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