Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives
The following in vitro glucocorticoid (GC) parameters of progesterone (P), 1-ene progesterone (ΔP), 11β-hydroxyprogesterone (HOP), 11β-1-ene progesterone (ΔHOP) and dexamethasone (Dexa) were assayed in the presence or absence of bovine calf serum (BCS): binding to thymus cytosol, dissociation of the...
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todo:paper_09600760_v66_n4_p211_Vicent2023-10-03T15:53:31Z Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives Vicent, G.P. Burton, G. Ghini, A. Lantos, C.P. Galigniana, M.D. 11beta hydroxyprogesterone dexamethasone glucocorticoid receptor heat shock protein progesterone tyrosine aminotransferase amino acid transport animal cell article controlled study enzyme induction glycogen synthesis hormone action hormone binding hormone receptor interaction mouse nonhuman structure activity relation thymocyte Adrenalectomy Animals Blood Cattle Cells, Cultured Corticosterone Cytosol Dexamethasone Enzyme Induction HSP90 Heat-Shock Proteins Liver Liver Glycogen Male Methionine Mice Mice, Inbred BALB C Progesterone Rats Rats, Sprague-Dawley Receptors, Glucocorticoid Structure-Activity Relationship Thymus Gland Transcortin Tyrosine Transaminase Uridine Animalia Bovinae Humulus The following in vitro glucocorticoid (GC) parameters of progesterone (P), 1-ene progesterone (ΔP), 11β-hydroxyprogesterone (HOP), 11β-1-ene progesterone (ΔHOP) and dexamethasone (Dexa) were assayed in the presence or absence of bovine calf serum (BCS): binding to thymus cytosol, dissociation of the glucocorticoid receptor (GR)-heat shock protein 90 (hsp90) complex (diss.), tyrosine aminotransferase (TAT) induction in hepatocytes and the inhibition of 3H-uridine and 35S-methionine uptake by thymocytes. Without BCS, steroids were in most cases active in this general order: Dex>ΔHOP>HOP>ΔP>P. BCS abolished all activities in P and ΔP, but left them unaltered in all other steroids, except diss. in HOP, which diminished intermediately. Binding of P, ΔP, HOP and ΔHOP to GR and CBG paralleled their in vivo activating effects on glycogen deposition. Conclusions: in this steroid series, BCS, but not CBG, inhibits GC responses of P and ΔP. 11-β hydroxylation frees those molecules from the inhibitory effects of BCS. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09600760_v66_n4_p211_Vicent |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
11beta hydroxyprogesterone dexamethasone glucocorticoid receptor heat shock protein progesterone tyrosine aminotransferase amino acid transport animal cell article controlled study enzyme induction glycogen synthesis hormone action hormone binding hormone receptor interaction mouse nonhuman structure activity relation thymocyte Adrenalectomy Animals Blood Cattle Cells, Cultured Corticosterone Cytosol Dexamethasone Enzyme Induction HSP90 Heat-Shock Proteins Liver Liver Glycogen Male Methionine Mice Mice, Inbred BALB C Progesterone Rats Rats, Sprague-Dawley Receptors, Glucocorticoid Structure-Activity Relationship Thymus Gland Transcortin Tyrosine Transaminase Uridine Animalia Bovinae Humulus |
| spellingShingle |
11beta hydroxyprogesterone dexamethasone glucocorticoid receptor heat shock protein progesterone tyrosine aminotransferase amino acid transport animal cell article controlled study enzyme induction glycogen synthesis hormone action hormone binding hormone receptor interaction mouse nonhuman structure activity relation thymocyte Adrenalectomy Animals Blood Cattle Cells, Cultured Corticosterone Cytosol Dexamethasone Enzyme Induction HSP90 Heat-Shock Proteins Liver Liver Glycogen Male Methionine Mice Mice, Inbred BALB C Progesterone Rats Rats, Sprague-Dawley Receptors, Glucocorticoid Structure-Activity Relationship Thymus Gland Transcortin Tyrosine Transaminase Uridine Animalia Bovinae Humulus Vicent, G.P. Burton, G. Ghini, A. Lantos, C.P. Galigniana, M.D. Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| topic_facet |
11beta hydroxyprogesterone dexamethasone glucocorticoid receptor heat shock protein progesterone tyrosine aminotransferase amino acid transport animal cell article controlled study enzyme induction glycogen synthesis hormone action hormone binding hormone receptor interaction mouse nonhuman structure activity relation thymocyte Adrenalectomy Animals Blood Cattle Cells, Cultured Corticosterone Cytosol Dexamethasone Enzyme Induction HSP90 Heat-Shock Proteins Liver Liver Glycogen Male Methionine Mice Mice, Inbred BALB C Progesterone Rats Rats, Sprague-Dawley Receptors, Glucocorticoid Structure-Activity Relationship Thymus Gland Transcortin Tyrosine Transaminase Uridine Animalia Bovinae Humulus |
| description |
The following in vitro glucocorticoid (GC) parameters of progesterone (P), 1-ene progesterone (ΔP), 11β-hydroxyprogesterone (HOP), 11β-1-ene progesterone (ΔHOP) and dexamethasone (Dexa) were assayed in the presence or absence of bovine calf serum (BCS): binding to thymus cytosol, dissociation of the glucocorticoid receptor (GR)-heat shock protein 90 (hsp90) complex (diss.), tyrosine aminotransferase (TAT) induction in hepatocytes and the inhibition of 3H-uridine and 35S-methionine uptake by thymocytes. Without BCS, steroids were in most cases active in this general order: Dex>ΔHOP>HOP>ΔP>P. BCS abolished all activities in P and ΔP, but left them unaltered in all other steroids, except diss. in HOP, which diminished intermediately. Binding of P, ΔP, HOP and ΔHOP to GR and CBG paralleled their in vivo activating effects on glycogen deposition. Conclusions: in this steroid series, BCS, but not CBG, inhibits GC responses of P and ΔP. 11-β hydroxylation frees those molecules from the inhibitory effects of BCS. |
| format |
JOUR |
| author |
Vicent, G.P. Burton, G. Ghini, A. Lantos, C.P. Galigniana, M.D. |
| author_facet |
Vicent, G.P. Burton, G. Ghini, A. Lantos, C.P. Galigniana, M.D. |
| author_sort |
Vicent, G.P. |
| title |
Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| title_short |
Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| title_full |
Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| title_fullStr |
Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| title_full_unstemmed |
Influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| title_sort |
influence of calf serum on glucocorticoid-responses of certain progesterone derivatives |
| url |
http://hdl.handle.net/20.500.12110/paper_09600760_v66_n4_p211_Vicent |
| work_keys_str_mv |
AT vicentgp influenceofcalfserumonglucocorticoidresponsesofcertainprogesteronederivatives AT burtong influenceofcalfserumonglucocorticoidresponsesofcertainprogesteronederivatives AT ghinia influenceofcalfserumonglucocorticoidresponsesofcertainprogesteronederivatives AT lantoscp influenceofcalfserumonglucocorticoidresponsesofcertainprogesteronederivatives AT galignianamd influenceofcalfserumonglucocorticoidresponsesofcertainprogesteronederivatives |
| _version_ |
1782025172178436096 |