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Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes (Microarray Expression)

ABSTRACT: Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes (Microarray Expression)

PROVIDER: PRJNA481870 | ENA |

REPOSITORIES: ENA

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Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes

Project description:Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes

| PRJNA481868 | ENA

Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes (Microarray Expression)

Project description:Accumulation of subcutaneous white adipose tissue (WAT) is associated with increased insulin sensitivity, low levels of inflammation and a generally metabolically-healthy state, whereas accumulation of visceral adipose tissue is associated with insulin resistance, adipose tissue inflammation and metabolic syndrome. Membrane Metallo-Endopeptidase (MME/Neprislyin) is an extracellular, membrane-bound protease enriched in subcutaneous WAT that can target degradation of a variety of peptides, including insulin, IL6, and β-amyloids. Here, we show that MME in white preadipocytes is differently expressed in subcutaneous vs visceral WAT, and favors insulin signaling and a low inflammatory response. Thus, knockdown of MME in preadipocytes increases the inflammatory response to substance P and amyloidβ aggregates. This is associated with increased basal insulin signaling and decreased insulin-stimulated signaling. Moreover, MME differentially regulates the internalization and turnover of the α/β subunits of the insulin receptor. Thus, MME is a novel regulator of the insulin receptor in adipose tissue and may serve as a therapeutic target to increase insulin sensitivity and decrease inflammatory susceptibility.

2019-02-25 | GSE117352 | GEO

Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes (RNA-Seq)

2019-02-25 | GSE117270 | GEO

Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes

Project description:Accumulation of visceral white adipose tissue (WAT) associates with insulin resistance, adipose tissue inflammation, and metabolic syndrome, whereas accumulation of subcutaneous WAT may be protective. We aimed to identify molecular mechanisms that might provide mechanistic insights underlying the phenotypic differences in these tissues. Membrane Metallo-Endopeptidase (MME/Neprislyin) is an extracellular, membrane-bound protease enriched in subcutaneous WAT that can target degradation of a variety of peptides, including insulin, IL6, and β-amyloids. We hypothesized that MME contributes to adipose depot-specific metabolic properties.

2019-02-25 | GSE117353 | GEO

Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes (RNA-Seq)

Project description:Membrane Metallo-Endopeptidase (Neprilysin) Regulates Inflammatory Response and Insulin Signaling in White Preadipocytes (RNA-Seq)

| PRJNA481672 | ENA

Membrane metallo-endopeptidase (Neprilysin) regulates inflammatory response and insulin signaling in white preadipocytes.

Project description: Not available

| S-EPMC6437599 | biostudies-literature

Myxobacterial metallo-β-lactamases

Project description:Understanding the biology of B1 metallo-β-lactamases (MβLs) in their native hosts and the molecular bases of the adaptive mechanisms during the transfer process to human pathogens, may provide novel therapeutic insights against these important resistance factors. Through large scale phylogenomic analyses, we identified Bacteroidota and Myxococcota as the primary hosts of the enzymes in environmental habitats. The monophyletic lineage of MβL homologues from the predatory members of the latter phylum shared common ancestry with clinically relevant families found in γ-Proteobacteria, highlighting their evolutionary significance. Resistance phenotypes and biochemical properties of native MβLs from three myxobacterial genera expressed in the model γ-proteobacterium, Escherichia coli, and comparisons with the New Delhi Metallo-β-lactamase revealed that evolution of the enzymes concerned mainly adaptations enhancing their production in the new hosts rather than functional differentiation. Periplasmic localization is the main evolved trait, with E. coli not recognizing optimally the signal peptides of the environmental MβLs which were secreted as soluble proteins in the cell envelope despite predicted to be lipoproteins. The unique features of N-terminal secretory signals of myxobacterial MβLs likely reflected the enzymes integration into the physiology of their hosts and pointed to naturally occurring molecules potentially controlling their expression.

2026-05-20 | PXD077803 | Pride

Natriuretic peptide pharmacogenetics: membrane metallo-endopeptidase (MME): common gene sequence variation, functional characterization and degradation.

Project description: Not available

| S-EPMC3092155 | biostudies-literature

Human membrane metallo-endopeptidase-like protein degrades both beta-amyloid 42 and beta-amyloid 40.

Project description: Not available

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Menin and Daxx Interact to Suppress Neuroendocrine Tumors through Epigenetic Control of the Membrane Metallo-Endopeptidase.

Project description: Not available

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