NDLI: Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism

Please wait, while we are loading the content...

Peroxisomal matrix protein import : Suppression of protein import defects in Hansenula polymorpha pex Mutants by Overproduction of the PTS1 Receptor Pex5p

Peroxisome biogenesis in the yeast Yarrowia lipolytica

ARF- and coatomer-mediated peroxisomal vesiculation

Three-dimensional ultrastructural analysis of peroxisomes in HepG2 cells : Absence of peroxisomal reticulum but evidence of close spatial association with the endoplasmic reticulum

Environmental response of yeast peroxisomes : Aspects of organelle assembly and degradation

Peroxisomal β-oxidation enzymes

Peroxisomal lipid degradation via β-and α-oxidation in Mammals

Peroxisomes, lipid metabolism, and human disease

New aspects of sterol carrier protein 2 (Nonspecific lipid-transfer protein) in fusion proteins and in peroxisomes

Alkyl-dihydroxyacetonephosphate synthase

Evolution of urate-degrading enzymes in animal peroxisomes

The 70-kDa peroxisomal membrane protein (PMP70) an ATP-binding cassette transporter

Sorting of peroxisomal and mitochondrial carnitine acetyltransferase isozymes in the diploid yeast, Candida tropicalis

A leaf-peroxisomal protein, hydroxypyruvate reductase, is produced by light-regulated alternative splicing

Peroxisome biogenesis and molecular defects in peroxisome assembly disorders

Temperature sensitivity in peroxisome assembly processes characterizes milder forms of peroxisome biogenesis disorders

Primary hyperoxaluria type 1 in Japan

Mutational analysis of X-linked adrenoleukodystrophy gene

Peroxisome proliferator-activated receptors, coactivators, and downstream targets

PPAR-Mediated diverse responses in various tissues of mouse

Relationship between signal transduction and PPARα-regulated genes of lipid metabolism in rat hepatic-derived Fao cells

Involvement of hepatocyte growth factor on hepatocarcinogenesis induced by peroxisome proliferators

Mouse models for peroxisome biogenesis disorders

Very-long-chain fatty acid metabolism in adrenoleukodystrophy protein-deficient mice

Molecular changes in the d-bifunctional protein cDNA sequence in australasian patients belonging to the bifunctional protein complementation group

Isolation of peroxisome-defective CHO mutant cells using green fluorescent protein

Peroxisomal proteins in rat gametes

Transport of peroxisomal proteins synthesized as large precursors in plants

Peroxisomal and mitochondrial targeting of serine: Pyruvate/alanine: Glyoxylate aminotransferase in rat liver

Hansenula polymorpha Pex14p phosphorylated in vivo

Genetic evaluation of peroxisomal and cytosolic acetoacetyl-CoA thiolase isozymes in n-alkane-assimilating diploid yeast, Candida tropicalis

Metabolic significance and expression of Caenorhabditis elegans type II 3-oxoacyl-CoA thiolase

Functional transformation of plant peroxisomes

Peroxisomes in permanent and provisional kidneys : Phylogenic and ontogenic considerations

The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases

Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism

Phosphorylation of 13 kDa nuclear protein in hepatocarcinomas induced by peroxisome proliferators

Peroxisomal proliferation induced by treatment with clofibrate in a patient with a peroxisomal disease

Disruption of a yeast very-long-chain acyl-CoA synthetase gene simulates the cellular phenotype of X-linked adrenoleukodystrophy

Cell Biochemistry and Biophysics : Volume 31

Cell Biochemistry and Biophysics : Volume 30

Cell Biochemistry and Biophysics : Volume 29

Cell Biochemistry and Biophysics : Volume 28

Cell Biochemistry and Biophysics : Volume 27

Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism

Content Provider	Springer Nature Link
Author	Hunt, Mary C. Lindquist, Per J. G. usiainen, Sari Huttunen, Merja Orii, Kenji Svensson, Thomas L. T. Aoyama, T. Hashimoto, Takashi Diczfalusy, Uulf Alexson, Stefan E. H.
Copyright Year	2000
Abstract	Acyl-CoA thioesterases hydrolyze acyl-CoAs to the corresponding free fatty acid plus coenzyme A. The activity is strongly induced in rat and mouse liver after feeding the animals peroxisome proliferators (PPs). To elucidate the role of these enzymes in lipid metabolism, the authors have cloned the cDNAs corresponding to the inducible cytosolic and mitochondrial type I enzymes (CTE-I and MTE-I), and studied tissue expression and nutritional regulation of expression of the mRNAs in mice. The constitutive expression of both mRNAs was low in liver, with CTE-I expressed mainly in kidney and brown adipose tissue, and MTE-I expressed in brown adipose tissue and heart. As expected, the expression in liver of both the CTE-I and MTE-I mRNAs were strongly induced (>50-fold) by treatment with clofibrate. A similar level of induction was observed by fasting and a time-course study showed that the CTE-I and MTE-I mRNAs were increased already at 6 h after removal of the diet. Refeeding normal chow diet to mice fasted for 24h normalized the mRNA levels with a T $_{1/2}$ of about 3–4 h. Feeding mice a fat-free diet further decreased the expression, possibly indicating repression of expression. The strong expression of MTE-I and CTE-I in the heart was increased about 10-fold by fasting. To further characterize these highly regulated enzymes, the authors have cloned the corresponding genes and promoter regions. The structures of the two genes were found to be very similar, consisting of three exons and two introns. Exon-intron borders conform to general consensus sequences, and, especially, the first exon appears to be highly conserved. The promoter regions of both the CTE-I and MTE-I genes contain putative PP response elements, suggesting an involvement of PP-activated receptors in the regulation of these genes.
Starting Page	317
Ending Page	324
Page Count	8
File Format	PDF
ISSN	10859195
Journal	Cell Biochemistry and Biophysics
Volume Number	32
Issue Number	1-3
e-ISSN	15590283
Language	English
Publisher	Humana Press
Publisher Date	2000-01-01
Publisher Place	Totowa
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Biochemistry Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Involvement of the peroxisome proliferator-activated receptor α in regulating long-chain acyl-CoA thioesterases

Involvement of the peroxisome proliferator-activated receptor a.

Peroxisome Proliferator-induced Long Chain Acyl-CoA Thioesterases Comprise a Highly Conserved Novel Multi-gene Family Involved in Lipid Metabolism

Involvement of the peroxisome proliferator-activated receptor alpha in regulating long-chain acylCoA thioesterases (2000)

Peroxisome proliferator-activated receptors, coactivators, and downstream targets

Molecular Cloning and Characterization of Two Mouse Peroxisome Proliferator-activated Receptor α (PPARα)-regulated Peroxisomal Acyl-CoA Thioesterases

Acyl-CoA thioesterases - auxiliary enzymes in peroxisomal lipid metabolism

Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases.

The acyl-CoA thioesterase I is regulated by PPARα and HNF4α via a distal response element in the promoter

Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism

Similar Documents

Involvement of the peroxisome proliferator-activated receptor α in regulating long-chain acyl-CoA thioesterases

Involvement of the peroxisome proliferator-activated receptor a.

Peroxisome Proliferator-induced Long Chain Acyl-CoA Thioesterases Comprise a Highly Conserved Novel Multi-gene Family Involved in Lipid Metabolism

Involvement of the peroxisome proliferator-activated receptor alpha in regulating long-chain acylCoA thioesterases (2000)

Peroxisome proliferator-activated receptors, coactivators, and downstream targets

Molecular Cloning and Characterization of Two Mouse Peroxisome Proliferator-activated Receptor α (PPARα)-regulated Peroxisomal Acyl-CoA Thioesterases

Acyl-CoA thioesterases - auxiliary enzymes in peroxisomal lipid metabolism

Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases.

The acyl-CoA thioesterase I is regulated by PPARα and HNF4α via a distal response element in the promoter

Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism