Sex-dimorphic neuroestradiol regulation of ventromedial hypothalamic nucleus glucoregulatory transmitter and glycogen metabolism enzyme protein expression in the rat.


Journal

BMC neuroscience
ISSN: 1471-2202
Titre abrégé: BMC Neurosci
Pays: England
ID NLM: 100966986

Informations de publication

Date de publication:
25 11 2020
Historique:
received: 18 06 2020
accepted: 30 10 2020
entrez: 26 11 2020
pubmed: 27 11 2020
medline: 3 9 2021
Statut: epublish

Résumé

Ventromedial hypothalamic nucleus (VMN) gluco-regulatory transmission is subject to sex-specific control by estradiol. The VMN is characterized by high levels of aromatase expression. The aromatase inhibitor letrozole (LZ) was used with high-resolution microdissection/Western blot techniques to address the hypothesis that neuroestradiol exerts sex-dimorphic control of VMN neuronal nitric oxide synthase (nNOS) and glutamate decarboxylase VMN aromatase protein content was similar between sexes. Intracerebroventricular LZ infusion of testes-intact male and ovariectomized, estradiol-replaced female rats blocked insulin-induced hypoglycemic (IIH) up-regulation of this profile. LZ exerted sex-contingent effects on basal VMN nNOS and GAD expression, but blocked IIH-induced NO stimulation and GAD suppression in each sex. Sex-contingent LZ effects on basal and hypoglycemic patterns of GPbb and GPmm expression occurred at distinctive levels of the VMN. LZ correspondingly down- or up-regulated baseline pyruvate recycling pathway marker protein expression in males (glutaminase) and females (malic enzyme-1), and altered INS effects on those proteins. Results infer that neuroestradiol is required in each sex for optimal VMN metabolic transmitter signaling of hypoglycemic energy deficiency. Sex differences in VMN GP variant protein levels and sensitivity to aromatase may correlate with sex-dimorphic glycogen mobilization during this metabolic stress. Neuroestradiol may also exert sex-specific effects on glucogenic amino acid energy yield by actions on distinctive enzyme targets in each sex.

Sections du résumé

BACKGROUND
Ventromedial hypothalamic nucleus (VMN) gluco-regulatory transmission is subject to sex-specific control by estradiol. The VMN is characterized by high levels of aromatase expression.
METHODS
The aromatase inhibitor letrozole (LZ) was used with high-resolution microdissection/Western blot techniques to address the hypothesis that neuroestradiol exerts sex-dimorphic control of VMN neuronal nitric oxide synthase (nNOS) and glutamate decarboxylase
RESULTS
VMN aromatase protein content was similar between sexes. Intracerebroventricular LZ infusion of testes-intact male and ovariectomized, estradiol-replaced female rats blocked insulin-induced hypoglycemic (IIH) up-regulation of this profile. LZ exerted sex-contingent effects on basal VMN nNOS and GAD expression, but blocked IIH-induced NO stimulation and GAD suppression in each sex. Sex-contingent LZ effects on basal and hypoglycemic patterns of GPbb and GPmm expression occurred at distinctive levels of the VMN. LZ correspondingly down- or up-regulated baseline pyruvate recycling pathway marker protein expression in males (glutaminase) and females (malic enzyme-1), and altered INS effects on those proteins.
CONCLUSIONS
Results infer that neuroestradiol is required in each sex for optimal VMN metabolic transmitter signaling of hypoglycemic energy deficiency. Sex differences in VMN GP variant protein levels and sensitivity to aromatase may correlate with sex-dimorphic glycogen mobilization during this metabolic stress. Neuroestradiol may also exert sex-specific effects on glucogenic amino acid energy yield by actions on distinctive enzyme targets in each sex.

Identifiants

pubmed: 33238883
doi: 10.1186/s12868-020-00598-w
pii: 10.1186/s12868-020-00598-w
pmc: PMC7687823
doi:

Substances chimiques

Aromatase Inhibitors 0
Estradiol 4TI98Z838E
Letrozole 7LKK855W8I
Glycogen 9005-79-2
Malate Dehydrogenase EC 1.1.1.37
malate dehydrogenase (decarboxylating) EC 1.1.1.39
Nitric Oxide Synthase EC 1.14.13.39
Glycogen Synthase EC 2.4.1.11
Glutaminase EC 3.5.1.2
Glutamate Decarboxylase EC 4.1.1.15
Glucose IY9XDZ35W2

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

51

Subventions

Organisme : NIDDK NIH HHS
ID : R01 DK109382
Pays : United States

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Auteurs

Md Main Uddin (MM)

Willis-Knighton Endowed Professor of Pharmacy and Director, School of Basic Pharmaceutical and Toxicological Sciences, College of Pharmacy, University of Louisiana Monroe, 356 Bienville Building, 1800 Bienville Drive, Monroe, LA, 71201, USA.

Mostafa M H Ibrahim (MMH)

Willis-Knighton Endowed Professor of Pharmacy and Director, School of Basic Pharmaceutical and Toxicological Sciences, College of Pharmacy, University of Louisiana Monroe, 356 Bienville Building, 1800 Bienville Drive, Monroe, LA, 71201, USA.

Karen P Briski (KP)

Willis-Knighton Endowed Professor of Pharmacy and Director, School of Basic Pharmaceutical and Toxicological Sciences, College of Pharmacy, University of Louisiana Monroe, 356 Bienville Building, 1800 Bienville Drive, Monroe, LA, 71201, USA. briski@ulm.edu.

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Classifications MeSH