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- Publisher Website: 10.1016/S0014-5793(97)00890-9
- Scopus: eid_2-s2.0-0030840667
- PMID: 9287127
- WOS: WOS:A1997XT08400022
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Article: Distinct type-2A protein phosphatases activate HMGCoA reductase and acetyl-CoA carboxylase in liver
Title | Distinct type-2A protein phosphatases activate HMGCoA reductase and acetyl-CoA carboxylase in liver |
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Authors | |
Keywords | Acetyl-CoA carboxylase AMP-activated protein kinase Glutamine HMGCoA reductase Protein phosphatase-2A |
Issue Date | 1997 |
Publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet |
Citation | Febs Letters, 1997, v. 413 n. 1, p. 115-118 How to Cite? |
Abstract | Acetyl-CoA carboxylase and HMGCoA reductase are inactivated by the same AMP-activated protein kinase and are activated by type-2A protein phosphatase. To determine whether the same species of protein phosphatase-2A were involved, we studied the interconversion of acetyl-CoA carboxylase and HMGCoA reductase in isolated rat hepatocytes. We show that (i) these enzymes are differently regulated in hepatocytes and (ii) the species of type-2A protein phosphatase involved in their activation are different and can be separated by anion-exchange chromatography. |
Persistent Identifier | http://hdl.handle.net/10722/149561 |
ISSN | 2023 Impact Factor: 3.0 2023 SCImago Journal Rankings: 1.208 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Gaussin, V | en_US |
dc.contributor.author | Skarlas, P | en_US |
dc.contributor.author | Ching, YP | en_US |
dc.contributor.author | Hardie, DG | en_US |
dc.contributor.author | Hue, L | en_US |
dc.date.accessioned | 2012-06-26T05:55:17Z | - |
dc.date.available | 2012-06-26T05:55:17Z | - |
dc.date.issued | 1997 | en_US |
dc.identifier.citation | Febs Letters, 1997, v. 413 n. 1, p. 115-118 | en_US |
dc.identifier.issn | 0014-5793 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/149561 | - |
dc.description.abstract | Acetyl-CoA carboxylase and HMGCoA reductase are inactivated by the same AMP-activated protein kinase and are activated by type-2A protein phosphatase. To determine whether the same species of protein phosphatase-2A were involved, we studied the interconversion of acetyl-CoA carboxylase and HMGCoA reductase in isolated rat hepatocytes. We show that (i) these enzymes are differently regulated in hepatocytes and (ii) the species of type-2A protein phosphatase involved in their activation are different and can be separated by anion-exchange chromatography. | en_US |
dc.language | eng | en_US |
dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet | en_US |
dc.relation.ispartof | FEBS Letters | en_US |
dc.subject | Acetyl-CoA carboxylase | - |
dc.subject | AMP-activated protein kinase | - |
dc.subject | Glutamine | - |
dc.subject | HMGCoA reductase | - |
dc.subject | Protein phosphatase-2A | - |
dc.subject.mesh | Amp-Activated Protein Kinases | en_US |
dc.subject.mesh | Acetyl-Coa Carboxylase - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cell Hypoxia | en_US |
dc.subject.mesh | Chromatography | en_US |
dc.subject.mesh | Enzyme Activation | en_US |
dc.subject.mesh | Glutamine - Pharmacology | en_US |
dc.subject.mesh | Hydroxymethylglutaryl Coa Reductases - Metabolism | en_US |
dc.subject.mesh | Liver - Drug Effects - Enzymology | en_US |
dc.subject.mesh | Male | en_US |
dc.subject.mesh | Multienzyme Complexes - Metabolism | en_US |
dc.subject.mesh | Phosphoprotein Phosphatases - Metabolism | en_US |
dc.subject.mesh | Protein Kinases - Metabolism | en_US |
dc.subject.mesh | Protein Phosphatase 2 | en_US |
dc.subject.mesh | Protein-Serine-Threonine Kinases | en_US |
dc.subject.mesh | Rats | en_US |
dc.subject.mesh | Rats, Wistar | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.title | Distinct type-2A protein phosphatases activate HMGCoA reductase and acetyl-CoA carboxylase in liver | en_US |
dc.type | Article | en_US |
dc.identifier.email | Ching, YP:ypching@hku.hk | en_US |
dc.identifier.authority | Ching, YP=rp00469 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/S0014-5793(97)00890-9 | en_US |
dc.identifier.pmid | 9287127 | - |
dc.identifier.scopus | eid_2-s2.0-0030840667 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0030840667&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 413 | en_US |
dc.identifier.issue | 1 | en_US |
dc.identifier.spage | 115 | en_US |
dc.identifier.epage | 118 | en_US |
dc.identifier.isi | WOS:A1997XT08400022 | - |
dc.publisher.place | Netherlands | en_US |
dc.identifier.scopusauthorid | Gaussin, V=6602467247 | en_US |
dc.identifier.scopusauthorid | Skarlas, P=6504513845 | en_US |
dc.identifier.scopusauthorid | Ching, YP=7005431277 | en_US |
dc.identifier.scopusauthorid | Hardie, DG=24373207900 | en_US |
dc.identifier.scopusauthorid | Hue, L=7006578984 | en_US |
dc.identifier.issnl | 0014-5793 | - |