Linked Life Data

7657624

Source:http://linkedlifedata.com/resource/pubmed/id/7657624

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1995-10-4
pubmed:abstractText
We have recently shown that hsp56, the FK506-binding immunophilin component of both the heat shock protein (hsp90.hsp70.hsp56) heterocomplex and the untransformed glucocorticoid receptor heterocomplex, is bound directly to hsp90 (Czar, M. J., Owens-Grillo, J. K., Dittmar, K. D., Hutchison, K. A., Zacharek, A. M., Leach, K. L., Deibel, M. R., and Pratt, W. B. (1994) J. Biol. Chem. 269, 11155-11161). In this work, we show that both untransformed glucocorticoid receptor and hsp90 heterocomplexes contain CyP-40, a 40-kDa immunophilin of the cyclosporin A-binding class. CyP-40 is present in both native glucocorticoid receptor heterocomplexes and receptor heterocomplexes reconstituted with rabbit reticulocyte lysate, and the presence of CyP-40 in the receptor heterocomplex is stabilized by molybdate. Immunoadsorption of hsp90 from cell lysate yields coimmunoadsorption of both hsp56 and CyP-40, showing that both immunophilins are in native heterocomplex with hsp90. However, immunoadsorption of hsp56 does not yield coimmunoadsorption of CyP-40; thus, the two immunophilins do not exist in the same heterocomplex with hsp90. Both purified CyP-40 and hsp56 bind directly to purified hsp90, and excess CyP-40 blocks the binding of hsp56, consistent with the presence of a common immunophilin binding site on hsp90. Our data also suggest that there are at least two types of untransformed glucocorticoid receptor-hsp90 heterocomplexes, one that contains hsp56 and another that contains CyP-40. The role played by the immunophilins in steroid receptor action is unknown, but it is clear that the peptidylprolyl isomerase activity of immunophilins is not required for glucocorticoid receptor-hsp90 heterocomplex assembly and proper folding of the hormone binding domain by the hsp90-associated protein folding system of reticulocyte lysate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20479-84
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7657624-Animals, pubmed-meshheading:7657624-Binding Sites, pubmed-meshheading:7657624-Blotting, Western, pubmed-meshheading:7657624-CHO Cells, pubmed-meshheading:7657624-Carrier Proteins, pubmed-meshheading:7657624-Cattle, pubmed-meshheading:7657624-Cell-Free System, pubmed-meshheading:7657624-Cricetinae, pubmed-meshheading:7657624-Cyclosporine, pubmed-meshheading:7657624-Cytosol, pubmed-meshheading:7657624-DNA-Binding Proteins, pubmed-meshheading:7657624-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7657624-HSP90 Heat-Shock Proteins, pubmed-meshheading:7657624-Heat-Shock Proteins, pubmed-meshheading:7657624-Mice, pubmed-meshheading:7657624-Molecular Weight, pubmed-meshheading:7657624-Rabbits, pubmed-meshheading:7657624-Receptors, Glucocorticoid, pubmed-meshheading:7657624-Recombinant Proteins, pubmed-meshheading:7657624-Reticulocytes, pubmed-meshheading:7657624-Tacrolimus Binding Proteins, pubmed-meshheading:7657624-Transfection
pubmed:year
1995
pubmed:articleTitle
The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor.
pubmed:affiliation
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't