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Article: Immunocytochemical studies on the localization of 5-aminolevulinate synthase in rat liver

TitleImmunocytochemical studies on the localization of 5-aminolevulinate synthase in rat liver
Authors
Issue Date1990
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabbi
Citation
Archives Of Biochemistry And Biophysics, 1990, v. 280 n. 2, p. 331-335 How to Cite?
AbstractThe localization of 5-aminolevulinate synthase (ALAS) in hepatocytes of untreated and porphyrinogenic drug-treated animals has been examined by an immunocytochemical approach using a monoclonal antibody and protein A-gold labeling. Gold particles representing antigenic sites for ALAS were observed in the mitochondria and cytoplasm of untreated and drug-treated cells. Quantitative analysis of the labeling density showed that levels of ALAS increased significantly in both of these cellular compartments following drug treatment. Evidence that the detected cytoplasmic form of ALAS represents the precursor of the enzyme was obtained from immunoblotting experiments. The direct detection of cytosolic ALAS in vivo rules out the possibility that enzyme activity previously detected in the cytosol fraction resulted from mitochondrial leakage during cell fractionation. The results indicate that the cytosolic accumulation of ALAS is not a consequence of the inability of mitochondria to accommodate more enzyme. However, the molecular basis for this cytosolic accumulation is not known. The studies also established that the mitochondrial enzyme is predominantly, if not exclusively, associated with the matrix side of the inner mitochondrial membrane.
Persistent Identifierhttp://hdl.handle.net/10722/147871
ISSN
2015 Impact Factor: 2.807
2015 SCImago Journal Rankings: 1.478
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorRohde, Men_US
dc.contributor.authorSrivastava, Gen_US
dc.contributor.authorRylatt, DBen_US
dc.contributor.authorBundesen, Pen_US
dc.contributor.authorZamattia, Jen_US
dc.contributor.authorCrane, DIen_US
dc.contributor.authorMay, BKen_US
dc.date.accessioned2012-05-29T06:09:40Z-
dc.date.available2012-05-29T06:09:40Z-
dc.date.issued1990en_US
dc.identifier.citationArchives Of Biochemistry And Biophysics, 1990, v. 280 n. 2, p. 331-335en_US
dc.identifier.issn0003-9861en_US
dc.identifier.urihttp://hdl.handle.net/10722/147871-
dc.description.abstractThe localization of 5-aminolevulinate synthase (ALAS) in hepatocytes of untreated and porphyrinogenic drug-treated animals has been examined by an immunocytochemical approach using a monoclonal antibody and protein A-gold labeling. Gold particles representing antigenic sites for ALAS were observed in the mitochondria and cytoplasm of untreated and drug-treated cells. Quantitative analysis of the labeling density showed that levels of ALAS increased significantly in both of these cellular compartments following drug treatment. Evidence that the detected cytoplasmic form of ALAS represents the precursor of the enzyme was obtained from immunoblotting experiments. The direct detection of cytosolic ALAS in vivo rules out the possibility that enzyme activity previously detected in the cytosol fraction resulted from mitochondrial leakage during cell fractionation. The results indicate that the cytosolic accumulation of ALAS is not a consequence of the inability of mitochondria to accommodate more enzyme. However, the molecular basis for this cytosolic accumulation is not known. The studies also established that the mitochondrial enzyme is predominantly, if not exclusively, associated with the matrix side of the inner mitochondrial membrane.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabbien_US
dc.relation.ispartofArchives of Biochemistry and Biophysicsen_US
dc.subject.mesh5-Aminolevulinate Synthetase - Metabolismen_US
dc.subject.meshAllylisopropylacetamide - Pharmacologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCytosol - Enzymologyen_US
dc.subject.meshImmunohistochemistryen_US
dc.subject.meshLiver - Cytology - Drug Effects - Enzymologyen_US
dc.subject.meshMaleen_US
dc.subject.meshMitochondria, Liver - Enzymologyen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.titleImmunocytochemical studies on the localization of 5-aminolevulinate synthase in rat liveren_US
dc.typeArticleen_US
dc.identifier.emailSrivastava, G:gopesh@pathology.hku.hken_US
dc.identifier.authoritySrivastava, G=rp00365en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0003-9861(90)90338-Yen_US
dc.identifier.pmid2369125-
dc.identifier.scopuseid_2-s2.0-0025352051en_US
dc.identifier.volume280en_US
dc.identifier.issue2en_US
dc.identifier.spage331en_US
dc.identifier.epage335en_US
dc.identifier.isiWOS:A1990DN57800014-
dc.publisher.placeUnited Statesen_US

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