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Human Milk Oligosaccharides and Childhood Diarrhoea

2016-09-12 18:38:22 | BioPortfolio

Summary

Assessment of the impact of oral Human Milk Oligosaccharides (HMO) application on acute diarrhoea and the development of prolonged and persistent diarrhoea in paediatric patients hospitalized with acute diarrhoea.

Description

The trial is single site, double blind, randomized of HMO addition (1.5 g /day) to standard of care in paediatric diarrhoea patients. HMO application and follow-up of the children at home will be done for 2 weeks. Control patients receive only the standard of care (ORS plus zinc). A breastfed group of diarrhoea patients will serve as reference group.

The total sample size is 495 patients. Patients will be females and males aged 6 months to 2 years old with acute diarrhoea.

Study Design

Allocation: Randomized, Endpoint Classification: Efficacy Study, Intervention Model: Parallel Assignment, Masking: Double Blind (Subject, Caregiver, Investigator, Outcomes Assessor)

Conditions

Acute Diarrhea

Intervention

ORS+ZINC, ORS+ZINC+HMO, ORS+ZINC+Breastfeeding

Location

Centre for Nutrition and Food Security icddr,b
Dhaka
Mohakhali
Bangladesh
1212

Status

Not yet recruiting

Source

Nestlé

Results (where available)

View Results

Links

Published on BioPortfolio: 2016-09-12T18:38:22-0400

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Medical and Biotech [MESH] Definitions

A ZINC metalloenzyme that catalyzes the transfer of a methyl group from BETAINE to HOMOCYSTEINE to produce dimethylglycine and METHIONINE, respectively. This enzyme is a member of a family of ZINC-dependent METHYLTRANSFERASES that use THIOLS or selenols as methyl acceptors.

EXOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.

ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.

Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.

A tripartite motif protein that contains three ZINC FINGERS, including a RING FINGER DOMAIN, at its N-terminal. Several nuclear and one cytoplasmic isoforms result from alternative splicing of the PML gene; most nuclear isoforms localize to subnuclear structures (PML nuclear bodies) that are disrupted in ACUTE PROMYELOCYTIC LEUKEMIA cells.

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