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Murine glucocorticoid receptors and the H-2 locus--A reappraisal

dc.contributor.authorLiu, Sharon L.en_US
dc.contributor.authorGrippo, Joseph F.en_US
dc.contributor.authorErickson, Robert P.en_US
dc.contributor.authorPratt, William B.en_US
dc.date.accessioned2006-04-07T18:16:57Z
dc.date.available2006-04-07T18:16:57Z
dc.date.issued1984-12en_US
dc.identifier.citationLiu, Sharon L., Grippo, Joseph F., Erickson, Robert P., Pratt, William B. (1984/12)."Murine glucocorticoid receptors and the H-2 locus--A reappraisal." Journal of Steroid Biochemistry 21(6): 633-637. <http://hdl.handle.net/2027.42/24623>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73GT-47KPMBW-58/2/3a71ce23cb656c29b9b9b7e8eab5ee4ben_US
dc.identifier.urihttps://hdl.handle.net/2027.42/24623
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6527531&dopt=citationen_US
dc.description.abstractIt has been demonstrated that susceptibility to glucocorticoid-induced formation of cleft palate is regulated by the mouse histocompatibility complex (H-2). This has encouraged us to examine H-2 effects on glucocorticoid binding in tissues of adult animals which would provide sufficient material with which to study the biochemical mechanism of the H-2 effect. Although it has been reported that cytosol prepared from lungs of adult mice with a high susceptibility to steroid-induced cleft palate formation have a higher level of glucocorticoid binding than lung cytosol prepared from a low-susceptibility strain, we are unable to demonstrate any influence of H-2 on binding capacity in this tissue from adult animals when glucocorticoid receptors are assayed in the presence of receptor reducing and stabilizing agents that maximize binding capacity.Cytosol prepared from rat liver contains an endogenous receptor-reducing system composed of NADPH and thioredoxin. It has also been reported that the murine H-2 complex contains a gene(s) that regulates the level of a modifier(s) in fetal hepatic cytosol that affects the binding of glucocorticoids to the receptor. Of two known low molecular weight modifiers that could account for this effect, we have previously established that the heat-stable, steroid receptor "modulator" is not regulated by the H-2 complex. In the present work we have assayed thioredoxin, a second potential modifier, in liver cytosols prepared from adults of two pairs of two H-2 congenic mouse strains. Our results show that the amount of thioredoxin is the same in all four mouse strains and that it is not regulated by the H-2 locus.At this time, we are unable to identify a system in adult mice in which the widely reported regulation of glucocorticoid binding by the mouse histocompatibility locus can be submitted to definitive biochemical study.en_US
dc.format.extent705473 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleMurine glucocorticoid receptors and the H-2 locus--A reappraisalen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartments of Human Genetics, University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.: Departments of Pharmacology, university of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationotherDepartments of Pharmacology, university of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationotherDepartments of Pharmacology, university of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationotherDepartments of Pharmacology, university of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.identifier.pmid6527531en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/24623/1/0000033.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0022-4731(84)90023-2en_US
dc.identifier.sourceJournal of Steroid Biochemistryen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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