A Novel Peptide Prevents Enterotoxin- and Inflammation-Induced Intestinal Fluid Secretion by Stimulating Sodium-Hydrogen Exchanger 3 Activity.


Journal

Gastroenterology
ISSN: 1528-0012
Titre abrégé: Gastroenterology
Pays: United States
ID NLM: 0374630

Informations de publication

Date de publication:
10 2023
Historique:
received: 12 04 2022
revised: 05 06 2023
accepted: 09 06 2023
medline: 25 9 2023
pubmed: 11 7 2023
entrez: 10 7 2023
Statut: ppublish

Résumé

Acute diarrheal diseases are the second most common cause of infant mortality in developing countries. This is contributed to by lack of effective drug therapy that shortens the duration or lessens the volume of diarrhea. The epithelial brush border sodium (Na+)/hydrogen (H A peptide (sodium-hydrogen exchanger 3 stimulatory peptide [N3SP]) was synthesized to mimic the part of the NHE3 C-terminus that forms a multiprotein complex that inhibits NHE3 activity. The effect of N3SP on NHE3 activity was evaluated in NHE3-transfected fibroblasts null for other plasma membrane NHEs, a human colon cancer cell line that models intestinal absorptive enterocytes (Caco-2/BBe), human enteroids, and mouse intestine in vitro and in vivo. N3SP was delivered into cells via a hydrophobic fluorescent maleimide or nanoparticles. N3SP uptake stimulated NHE3 activity at nmol/L concentrations under basal conditions and partially reversed the reduced NHE3 activity caused by elevated adenosine 3',5'-cyclic monophosphate, guanosine 3',5'-cyclic monophosphate, and Ca These findings suggest pharmacologic stimulation of NHE3 activity as an efficacious approach for the treatment of moderate/severe diarrheal diseases.

Sections du résumé

BACKGROUND & AIMS
Acute diarrheal diseases are the second most common cause of infant mortality in developing countries. This is contributed to by lack of effective drug therapy that shortens the duration or lessens the volume of diarrhea. The epithelial brush border sodium (Na+)/hydrogen (H
METHODS
A peptide (sodium-hydrogen exchanger 3 stimulatory peptide [N3SP]) was synthesized to mimic the part of the NHE3 C-terminus that forms a multiprotein complex that inhibits NHE3 activity. The effect of N3SP on NHE3 activity was evaluated in NHE3-transfected fibroblasts null for other plasma membrane NHEs, a human colon cancer cell line that models intestinal absorptive enterocytes (Caco-2/BBe), human enteroids, and mouse intestine in vitro and in vivo. N3SP was delivered into cells via a hydrophobic fluorescent maleimide or nanoparticles.
RESULTS
N3SP uptake stimulated NHE3 activity at nmol/L concentrations under basal conditions and partially reversed the reduced NHE3 activity caused by elevated adenosine 3',5'-cyclic monophosphate, guanosine 3',5'-cyclic monophosphate, and Ca
CONCLUSIONS
These findings suggest pharmacologic stimulation of NHE3 activity as an efficacious approach for the treatment of moderate/severe diarrheal diseases.

Identifiants

pubmed: 37429363
pii: S0016-5085(23)04766-2
doi: 10.1053/j.gastro.2023.06.028
pii:
doi:

Substances chimiques

Sodium-Hydrogen Exchanger 3 0
Enterotoxins 0
Sodium-Hydrogen Exchangers 0
Sodium 9NEZ333N27
Peptides 0

Types de publication

Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

986-998.e11

Subventions

Organisme : NIBIB NIH HHS
ID : P41 EB028239
Pays : United States
Organisme : NIDDK NIH HHS
ID : R24 DK099803
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK089502
Pays : United States

Commentaires et corrections

Type : ErratumIn

Informations de copyright

Copyright © 2023 AGA Institute. Published by Elsevier Inc. All rights reserved.

Auteurs

Nicholas C Zachos (NC)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland. Electronic address: n.zachos@vumc.org.

Hannah Vaughan (H)

Translational Tissue Engineering Center, Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Rafiquel Sarker (R)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Savannah Est-Witte (S)

Translational Tissue Engineering Center, Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Molee Chakraborty (M)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Nicholas W Baetz (NW)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Hongzhe Yu (H)

Translational Tissue Engineering Center, Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Vladimir Yarov-Yarovoy (V)

Department of Physiology and Membrane Biology, University of California Davis, Davis, California; Department of Anesthesiology and Pain Medicine, University of California Davis, Davis, California.

George McNamara (G)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Jordan J Green (JJ)

Translational Tissue Engineering Center, Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Chung-Ming Tse (CM)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland.

Mark Donowitz (M)

Division of Gastroenterology and Hepatology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland; Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland. Electronic address: mdonowit@jhmi.edu.

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Classifications MeSH