Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP511

Reynolds, P. D.; Ruan, Y.; Smith, D. F.; Scammell, J. G.

doi:10.1210/jcem.84.2.5429

Cited by 184Estrogen and related hormone effectsStress Responses and CortisolSignaling Pathways in Disease

Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP511

Reynolds, P. D., Ruan, Y., Smith, D. F., Scammell, J. G.·1999·The Journal of Clinical Endocrinology & Metabolism

DOI 10.1210/jcem.84.2.5429

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Abstract

Squirrel monkeys are neotropical primates that have high circulating cortisol to compensate for expression of glucocorticoid receptors (GRs) with reduced affinity. The low binding affinity of squirrel monkey GR does not result from substitutions in the receptor, because squirrel monkey GR expressed in vitro exhibits high affinity. Rather, squirrel monkeys express a soluble factor that, in mixing studies of cytosol from squirrel monkey lymphocytes (SML) and mouse L929 cells, reduced GR binding affinity by 11-fold. In an effort to identify this factor, the cellular levels of components of the GR heterocomplex in SML and human lymphocytes (HL) were compared. The immunophilin FKBP51 was 13-fold higher in SML than in HL cytosol; FKBP52 in SML was 42% of that in HL cytosol. A role for changes in immunophilins, causing glucocorticoid resistance in neotropical primates, is supported by the following: the changes in FKBP51 and FKBP52 were observed in cells from other neotropical primates with glucocorticoid resistance; the elevated level of FKBP51 was reflected in an abundance of FKBP51 in heat shock protein 90 complexes in SML; when cytosols of SML and L929 cells were mixed, the decrease in GR binding was associated with incorporation of FKBP51 into GR heterocomplexes; the effect of SML cytosol on GR binding was reproduced with cytosol from COS cells expressing squirrel monkey FKBP51; and both the effect of SML cytosol on GR binding and the incorporation of FKBP51 into GR heterocomplexes were blocked by FK506. Regulation of GR binding by FKBP51 represents a previously unrecognized mechanism for regulating glucocorticoid sensitivity.

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The relative concentrations of FKBP51 and FKBP52 in the cell dictate the level of GR activity in vivo.
“Thus, the relative concentrations of FKBP51 and FKBP52 in the cell dictate the level of GR activity in vivo23,28,55.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [55]

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Squirrel Monkey Immunophilin FKBP51 Is a Potent Inhibitor of Glucocorticoid Receptor Binding<sup>1</sup>
Denny, W. B., Valentine, D. L., Reynolds, P. D., Smith, D. F., & Scammell, J. G. (2000) · Endocrinology · doi:10.1210/en.141.11.4107 · Cited by 66 · see citing works
Self-citation
Printed in U.S.A. Copyright © 2000 by The Endocrine Society Squirrel Monkey Immunophilin FKBP51 Is a Potent Inhibitor of Glucocorticoid Receptor Binding*
Denny, W. B., Valentine, D. L., Reynolds, P. D., Smith, D. F., Jonathan, & Scammell, G. (2000)
Self-citation
Overexpression of the FK506-Binding Immunophilin FKBP51 Is the Common Cause of Glucocorticoid Resistance in Three New World Primates
Scammell, J. G., Denny, W. B., Valentine, D. L., & Smith, D. F. (2001) · General and Comparative Endocrinology · doi:10.1006/gcen.2001.7696 · Cited by 238 · see citing works
Self-citation
Glucocorticoid resistance in squirrel monkeys results from a combination of a transcriptionally incompetent glucocorticoid receptor and overexpression of the glucocorticoid receptor co-chaperone FKBP51
Westberry, J. M., Sadosky, P. W., Hubler, T. R., Gross, K. L., & Scammell, J. G. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.03.004 · Cited by 91 · see citing works
Self-citation
Glucocorticoid resistance in squirrel monkeys results from a combination of overexpression of the glucocorticoid receptor cochaperone FKBP51 and mutations in the receptor
Westberry, J. M., Sadosky, P. W., Hubler, T. R., & Scammell, J. G. (2006) · The FASEB Journal · doi:10.1096/fasebj.20.4.a258-b
Self-citation

Authors: Reynolds, P. D., Ruan, Y., Smith, D. F., & Scammell, J. G.
Affiliations: University of South Alabama (US)
University of Nebraska Medical Center (US)
Corresponding author: Scammell, J. G.
ORCID: Smith, D. F.
Scammell, J. G.
Venue: The Journal of Clinical Endocrinology & Metabolism
Publisher: The Endocrine Society
Published: 1999-02
Volume: 84
Issue: 2
Pages: 663-669
ISSN: 0021-972X (ISSN-L)
1945-7197
DOI: 10.1210/jcem.84.2.5429
OpenAlex: W1978913374
Cited by: 184
References: 43
Citations by year: 2026: 1 · 2023: 5 · 2022: 2 · 2021: 2 · 2020: 8 · 2019: 5 · 2018: 2 · 2017: 7 · 2016: 7 · 2015: 6 · 2014: 6 · 2013: 7 · 2012: 11
FWCI: 4.95
Type: journal article
Language: en
Open access: closed
Locations: The Journal of Clinical Endocrinology & Metabolism (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Public Health Service (01254, 13200)
National Institute of Diabetes and Digestive and Kidney Diseases (DK-48218, R01DK048218)
National Center for Research Resources (P40RR001254, R24RR013200)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Life Sciences › Neuroscience › Behavioral Neuroscience › Stress Responses and Cortisol
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: glucocorticoid resistance, squirrel monkey, FKBP51, FKBP52, immunophilins, glucocorticoid receptor, receptor binding affinity, HSP90, lymphocytes, Neotropical primates, cortisol, FK506
MeSH terms: Animals, Cytosol, Drug Resistance, Glucocorticoids, Humans, Immunosuppressive Agents, Lymphocytes, Receptors, Glucocorticoid, Saimiri, Gene Expression, Tacrolimus, HSP90 Heat-Shock Proteins, Immunophilins, Sirolimus, Tacrolimus Binding Proteins

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Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP511

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