Effects of Macronutrients on the In Vitro Production of ClpB, a Bacterial Mimetic Protein of α-MSH and Its Possible Role in Satiety Signaling

Gut microbiota can influence the feeding behavior of the host, but the underlying mechanisms are unknown. Recently, caseinolytic protease B (ClpB), a disaggregation chaperon protein of , was identified as a conformational mimetic of α-melanocyte-stimulating hormone (α-MSH), an anorexigenic neuropept...

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Veröffentlicht in:Nutrients 2019-09, Vol.11 (9), p.2115
Hauptverfasser: Dominique, Manon, Breton, Jonathan, Guérin, Charlène, Bole-Feysot, Christine, Lambert, Grégory, Déchelotte, Pierre, Fetissov, Sergueï
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container_issue 9
container_start_page 2115
container_title Nutrients
container_volume 11
creator Dominique, Manon
Breton, Jonathan
Guérin, Charlène
Bole-Feysot, Christine
Lambert, Grégory
Déchelotte, Pierre
Fetissov, Sergueï
description Gut microbiota can influence the feeding behavior of the host, but the underlying mechanisms are unknown. Recently, caseinolytic protease B (ClpB), a disaggregation chaperon protein of , was identified as a conformational mimetic of α-melanocyte-stimulating hormone (α-MSH), an anorexigenic neuropeptide. Importantly, ClpB was necessary for to have an anorexigenic effect in mice, suggesting that it may participate in satiety signaling. To explore this further, we determined the short-term (2 h) effects of three macronutrients: protein (bovine serum albumin), carbohydrate (D-fructose) and fat (oleic acid), on the production of ClpB by and analyzed whether ClpB can stimulate the secretion of the intestinal satiety hormone, peptide YY (PYY). Isocaloric amounts of all three macronutrients added to a continuous culture of increased ClpB immunoreactivity. However, to increase the levels of ClpB mRNA and ClpB protein in bacteria and supernatants, supplementation with protein was required. A nanomolar concentration of recombinant ClpB dose-dependently stimulated PYY secretion from the primary cell cultures of rat intestinal mucosa. Total proteins extracted from but not from ClpB-deficient strains also tended to increase PYY secretion. These data support a possible link between ClpB and protein-induced satiety signaling in the gut.
doi_str_mv 10.3390/nu11092115
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Recently, caseinolytic protease B (ClpB), a disaggregation chaperon protein of , was identified as a conformational mimetic of α-melanocyte-stimulating hormone (α-MSH), an anorexigenic neuropeptide. Importantly, ClpB was necessary for to have an anorexigenic effect in mice, suggesting that it may participate in satiety signaling. To explore this further, we determined the short-term (2 h) effects of three macronutrients: protein (bovine serum albumin), carbohydrate (D-fructose) and fat (oleic acid), on the production of ClpB by and analyzed whether ClpB can stimulate the secretion of the intestinal satiety hormone, peptide YY (PYY). Isocaloric amounts of all three macronutrients added to a continuous culture of increased ClpB immunoreactivity. However, to increase the levels of ClpB mRNA and ClpB protein in bacteria and supernatants, supplementation with protein was required. A nanomolar concentration of recombinant ClpB dose-dependently stimulated PYY secretion from the primary cell cultures of rat intestinal mucosa. Total proteins extracted from but not from ClpB-deficient strains also tended to increase PYY secretion. 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subjects Activation
alpha-melanocyte-stimulating hormone
Anaerobic conditions
Animals
Appetite
Bacteria
bovine serum albumin
Carbohydrates
cell culture
Cells, Cultured
ClpB protein
Diet
E coli
Eating disorders
Electrolytes
Electrolytic cells
Endopeptidase Clp - genetics
Endopeptidase Clp - metabolism
Escherichia coli
Escherichia coli K12 - drug effects
Escherichia coli K12 - enzymology
Escherichia coli K12 - genetics
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fatty acids
Feeding Behavior
Food and Nutrition
fructose
Fructose - pharmacology
Gastrointestinal Microbiome
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic
Heat-Shock Proteins - genetics
Heat-Shock Proteins - metabolism
Hormones
Host-Pathogen Interactions
Ingestion
intestinal microorganisms
intestinal mucosa
Intestinal Mucosa - metabolism
Intestinal Mucosa - microbiology
Life Sciences
Male
Meals
messenger RNA
Metabolism
Metabolites
mice
Microbiota
Nutrients
Obesity
oleic acid
Oleic Acid - pharmacology
peptide YY
Peptide YY - metabolism
Peptides
Physiological effects
Physiology
proteinases
Proteins
Psychopathology
rats
Rats, Sprague-Dawley
Satiety
Satiety Response
Secretion
Secretions
Serum Albumin, Bovine - pharmacology
Signal Transduction
Stationary phase
Weight control
title Effects of Macronutrients on the In Vitro Production of ClpB, a Bacterial Mimetic Protein of α-MSH and Its Possible Role in Satiety Signaling
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