Evidence that removal of an endogenous metal that stabilizes the untransformed glucocorticoid receptor in cytosol allows ligand-independent receptor transformation
dc.contributor.author | Meshinchi, Soheil | en_US |
dc.contributor.author | Pratt, William B. | en_US |
dc.date.accessioned | 2006-04-07T20:58:15Z | |
dc.date.available | 2006-04-07T20:58:15Z | |
dc.date.issued | 1989 | en_US |
dc.identifier.citation | Meshinchi, Soheil, Pratt, William B. (1989)."Evidence that removal of an endogenous metal that stabilizes the untransformed glucocorticoid receptor in cytosol allows ligand-independent receptor transformation." Journal of Steroid Biochemistry 34(1-6): 315-317. <http://hdl.handle.net/2027.42/28177> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GT-47PGX5M-36/2/3cd2081e91b0c7e673c34d3158c1b517 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28177 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2626024&dopt=citation | en_US |
dc.description.abstract | Cytosol preparations contain an endogenous heat-stable factor which stabilizes the glucocorticoid receptor in its untransformed, non DNA-binding form. Elution of a partially purified preparation of this stabilizing factor through a metal chelating resin (Chelex-100) leads to the loss of its ability to inhibit temperature-mediated transformation of the receptor. Sodium molybdate mimicks the ability of this endogenous metal to stabilize the untransformed receptor, and it too is adsorbed by Chelex resin. When an L-cell cytosol preparation containing the glucocorticoid receptor is passed through a column of Chelex-100 resin and then incubated at 15[deg]C, the receptor is rapidly transformed to the DNA-binding state, regardless of whether it is steroid-bound or not. In contrast, whole cytosol containing endogenous metals is transformed to the DNA-binding state only when the receptor is both steroid-bound and exposed to elevated temperature, these data suggest that a metal (or metals) may be involved in conferring the property of ligand-dependency to the transformation process. | en_US |
dc.format.extent | 312593 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Evidence that removal of an endogenous metal that stabilizes the untransformed glucocorticoid receptor in cytosol allows ligand-independent receptor transformation | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 2626024 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28177/1/0000629.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0022-4731(89)90100-3 | en_US |
dc.identifier.source | Journal of Steroid Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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