Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals
The enzyme 11 βHSD2 protects the non-selective mineralocorticoid receptor from occupation by glucocorticoids in aldosterone target tissues. We studied the effect of stress elicited by intubation with a rubber catheter and administration of 10 ml of 0.45% NaCl (G3), of 10 ml of 200 mM HCl (G4) or int...
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paper:paper_00243205_v64_n24_p2285_Igarreta2023-06-08T14:52:03Z Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals Calvo, Juan Carlos 11 βHSD2 Acidosis Corticosteroids Kidney Stress 11beta hydroxysteroid dehydrogenase aldosterone corticosterone glucocorticoid mineralocorticoid 11beta hydroxysteroid dehydrogenase corticosterone glucocorticoid hydroxysteroid dehydrogenase isoenzyme mineralocorticoid receptor acidosis animal experiment article binding affinity data analysis enzyme activity kidney function mammal nonhuman rat receptor binding species difference stress animal enzymology kidney kinetics male metabolism microsome Sprague Dawley rat Animalia Mammalia 11-beta-Hydroxysteroid Dehydrogenases Acidosis Animals Corticosterone Glucocorticoids Hydroxysteroid Dehydrogenases Isoenzymes Kidney Kinetics Male Microsomes Rats Rats, Sprague-Dawley Receptors, Mineralocorticoid Stress The enzyme 11 βHSD2 protects the non-selective mineralocorticoid receptor from occupation by glucocorticoids in aldosterone target tissues. We studied the effect of stress elicited by intubation with a rubber catheter and administration of 10 ml of 0.45% NaCl (G3), of 10 ml of 200 mM HCl (G4) or intubation alone (G2) on the kinetics of the renal enzyme compared with untreated rats (G1). Microsomes were incubated with increasing masses of 3H corticosterone and 400 μM NAD at pH=7.4 during 5 minutes. Samples were extracted with ethyl acetate and analyzed by TLC. Results for n=4: Vmax for G1, 4.82 ± 0.67. G2, 10.04 ± 0.16. G3, 9.16 ± 0.74. G4, 10.19 ± 0.79 pmoles/min/mg prot. Km for G1, 22.37 ± 2.42. G2, 50.72 ± 7.05*. G3, 55.25 ± 8.37**. G4, 27.40 ± 3.20 nM. (***p<0.001, **p<0.01 and *p<0.05 vs G1). All treatments increased Vmax. Intubation alone and gavage with 0.45% NaCl, but not with 200 mM HCl, increased Km. Taking together, the results could reflect a way to prevent occupation of type I receptors by increased levels of circulating glucocorticoids due to stressful situations. This protection seems more efficient under acidotic conditions causing -in addition to an increased Vmax- a low Km for the enzyme. Fil:Calvo, J.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1999 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00243205_v64_n24_p2285_Igarreta http://hdl.handle.net/20.500.12110/paper_00243205_v64_n24_p2285_Igarreta |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
11 βHSD2 Acidosis Corticosteroids Kidney Stress 11beta hydroxysteroid dehydrogenase aldosterone corticosterone glucocorticoid mineralocorticoid 11beta hydroxysteroid dehydrogenase corticosterone glucocorticoid hydroxysteroid dehydrogenase isoenzyme mineralocorticoid receptor acidosis animal experiment article binding affinity data analysis enzyme activity kidney function mammal nonhuman rat receptor binding species difference stress animal enzymology kidney kinetics male metabolism microsome Sprague Dawley rat Animalia Mammalia 11-beta-Hydroxysteroid Dehydrogenases Acidosis Animals Corticosterone Glucocorticoids Hydroxysteroid Dehydrogenases Isoenzymes Kidney Kinetics Male Microsomes Rats Rats, Sprague-Dawley Receptors, Mineralocorticoid Stress |
spellingShingle |
11 βHSD2 Acidosis Corticosteroids Kidney Stress 11beta hydroxysteroid dehydrogenase aldosterone corticosterone glucocorticoid mineralocorticoid 11beta hydroxysteroid dehydrogenase corticosterone glucocorticoid hydroxysteroid dehydrogenase isoenzyme mineralocorticoid receptor acidosis animal experiment article binding affinity data analysis enzyme activity kidney function mammal nonhuman rat receptor binding species difference stress animal enzymology kidney kinetics male metabolism microsome Sprague Dawley rat Animalia Mammalia 11-beta-Hydroxysteroid Dehydrogenases Acidosis Animals Corticosterone Glucocorticoids Hydroxysteroid Dehydrogenases Isoenzymes Kidney Kinetics Male Microsomes Rats Rats, Sprague-Dawley Receptors, Mineralocorticoid Stress Calvo, Juan Carlos Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
topic_facet |
11 βHSD2 Acidosis Corticosteroids Kidney Stress 11beta hydroxysteroid dehydrogenase aldosterone corticosterone glucocorticoid mineralocorticoid 11beta hydroxysteroid dehydrogenase corticosterone glucocorticoid hydroxysteroid dehydrogenase isoenzyme mineralocorticoid receptor acidosis animal experiment article binding affinity data analysis enzyme activity kidney function mammal nonhuman rat receptor binding species difference stress animal enzymology kidney kinetics male metabolism microsome Sprague Dawley rat Animalia Mammalia 11-beta-Hydroxysteroid Dehydrogenases Acidosis Animals Corticosterone Glucocorticoids Hydroxysteroid Dehydrogenases Isoenzymes Kidney Kinetics Male Microsomes Rats Rats, Sprague-Dawley Receptors, Mineralocorticoid Stress |
description |
The enzyme 11 βHSD2 protects the non-selective mineralocorticoid receptor from occupation by glucocorticoids in aldosterone target tissues. We studied the effect of stress elicited by intubation with a rubber catheter and administration of 10 ml of 0.45% NaCl (G3), of 10 ml of 200 mM HCl (G4) or intubation alone (G2) on the kinetics of the renal enzyme compared with untreated rats (G1). Microsomes were incubated with increasing masses of 3H corticosterone and 400 μM NAD at pH=7.4 during 5 minutes. Samples were extracted with ethyl acetate and analyzed by TLC. Results for n=4: Vmax for G1, 4.82 ± 0.67. G2, 10.04 ± 0.16. G3, 9.16 ± 0.74. G4, 10.19 ± 0.79 pmoles/min/mg prot. Km for G1, 22.37 ± 2.42. G2, 50.72 ± 7.05*. G3, 55.25 ± 8.37**. G4, 27.40 ± 3.20 nM. (***p<0.001, **p<0.01 and *p<0.05 vs G1). All treatments increased Vmax. Intubation alone and gavage with 0.45% NaCl, but not with 200 mM HCl, increased Km. Taking together, the results could reflect a way to prevent occupation of type I receptors by increased levels of circulating glucocorticoids due to stressful situations. This protection seems more efficient under acidotic conditions causing -in addition to an increased Vmax- a low Km for the enzyme. |
author |
Calvo, Juan Carlos |
author_facet |
Calvo, Juan Carlos |
author_sort |
Calvo, Juan Carlos |
title |
Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
title_short |
Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
title_full |
Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
title_fullStr |
Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
title_full_unstemmed |
Activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
title_sort |
activity of renal 11 βhydroxysteroid dehydrogenase 2 (11 βhsd2) in stressed animals |
publishDate |
1999 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00243205_v64_n24_p2285_Igarreta http://hdl.handle.net/20.500.12110/paper_00243205_v64_n24_p2285_Igarreta |
work_keys_str_mv |
AT calvojuancarlos activityofrenal11bhydroxysteroiddehydrogenase211bhsd2instressedanimals |
_version_ |
1768542774626353152 |