Development Of An In-vitro Model System To Investigate The Mechanism Of Muscle Protein Catabolism Induced By Proteolysis-inducing Factor.

dc.creatorGomes-Marcondes, M C C
dc.creatorSmith, H J
dc.creatorCooper, J C
dc.creatorTisdale, M J
dc.date2002-May
dc.date2015-11-27T12:49:07Z
dc.date2015-11-27T12:49:07Z
dc.date.accessioned2018-03-29T00:56:14Z
dc.date.available2018-03-29T00:56:14Z
dc.identifierBritish Journal Of Cancer. v. 86, n. 10, p. 1628-33, 2002-May.
dc.identifier0007-0920
dc.identifier10.1038/sj.bjc.6600236
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/12085214
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195074
dc.identifier12085214
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295307
dc.descriptionThe mechanism of muscle protein catabolism induced by proteolysis-inducing factor, produced by cachexia-inducing murine and human tumours has been studied in vitro using C(2)C(12) myoblasts and myotubes. In both myoblasts and myotubes protein degradation was enhanced by proteolysis-inducing factor after 24 h incubation. In myoblasts this followed a bell-shaped dose-response curve with maximal effects at a proteolysis-inducing factor concentration between 2 and 4 nM, while in myotubes increased protein degradation was seen at all concentrations of proteolysis-inducing factor up to 10 nM, again with a maximum of 4 nM proteolysis-inducing factor. Protein degradation induced by proteolysis-inducing factor was completely attenuated in the presence of cycloheximide (1 microM), suggesting a requirement for new protein synthesis. In both myoblasts and myotubes protein degradation was accompanied by an increased expression of the alpha-type subunits of the 20S proteasome as well as functional activity of the proteasome, as determined by the 'chymotrypsin-like' enzyme activity. There was also an increased expression of the 19S regulatory complex as well as the ubiquitin-conjugating enzyme (E2(14k)), and in myotubes a decrease in myosin expression was seen with increasing concentrations of proteolysis-inducing factor. These results show that proteolysis-inducing factor co-ordinately upregulates both ubiquitin conjugation and proteasome activity in both myoblasts and myotubes and may play an important role in the muscle wasting seen in cancer cachexia.
dc.description86
dc.description1628-33
dc.languageeng
dc.relationBritish Journal Of Cancer
dc.relationBr. J. Cancer
dc.rightsfechado
dc.rightscomCopyright 2002 Cancer Research UK
dc.sourcePubMed
dc.subjectAdenosine Triphosphatases
dc.subjectAnimals
dc.subjectAntibodies, Monoclonal
dc.subjectBlood Proteins
dc.subjectCachexia
dc.subjectCells, Cultured
dc.subjectCysteine Endopeptidases
dc.subjectDose-response Relationship, Drug
dc.subjectEndopeptidases
dc.subjectGene Expression Regulation
dc.subjectMacromolecular Substances
dc.subjectMice
dc.subjectMultienzyme Complexes
dc.subjectMuscle Proteins
dc.subjectMuscle, Skeletal
dc.subjectMyosin Heavy Chains
dc.subjectProteasome Endopeptidase Complex
dc.subjectProtein Subunits
dc.subjectProteoglycans
dc.subjectUbiquitin
dc.titleDevelopment Of An In-vitro Model System To Investigate The Mechanism Of Muscle Protein Catabolism Induced By Proteolysis-inducing Factor.
dc.typeArtículos de revistas


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