Study of Antioxidants and Oxidants in Malnourished Children
It is believed that the organs of severely malnourished children malfunction because harmful compounds called oxidants injure the tissues in these organs. In a healthy person oxidants are made harmless because another compound called glutathione neutralizes them. Glutathione is made from three amino acids that we get from the protein we eat in our food. We found that malnourished children were not making enough glutathione because they lacked one of these amino acids called cysteine. In this study we determine why malnourished children do not have sufficient cysteine, and we will feed malnourished children a whey-based diet which is rich in cysteine during their treatment to determine whether they will make more glutathione. This in turn may make their organs recover faster. These findings will let us know whether malnourished children can recover faster if they are given more cysteine during the early phase of treatment.
Allocation: Randomized, Control: Placebo Control, Endpoint Classification: Efficacy Study, Intervention Model: Parallel Assignment, Masking: Double-Blind, Primary Purpose: Treatment
cysteine-rich whey based formula
Tropical Metabolism Research Unit, University of the West Indies
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Results (where available)
- Source: http://clinicaltrials.gov/show/NCT00069134
- Information obtained from ClinicalTrials.gov on July 15, 2010
Medical and Biotech [MESH] Definitions
The lack of sufficient energy or protein to meet the body's metabolic demands, as a result of either an inadequate dietary intake of protein, intake of poor quality dietary protein, increased demands due to disease, or increased nutrient losses.
Ring Finger Domains
A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.
Receptor-like Protein Tyrosine Phosphatases, Class 1
A subclass of receptor-like protein tryosine phosphatases that contain heavily glycosylated and cysteine-rich extracellular regions that include fibronectin type III-like domains.
Cysteine-rich Protein 61
A CCN protein family member that regulates a variety of extracellular functions including CELL ADHESION; CELL MIGRATION; and EXTRACELLULAR MATRIX synthesis. It may play an important role in the development of branched CAPILLARIES during EMBRYOGENESIS.
Ccn Intercellular Signaling Proteins
A family of secreted proteins found associated with the EXTRACELLULAR MATRIX and cell surface receptors. They are believed to play a role in modulating the effects of a variety of GROWTH FACTORS and PROTEASES at the cell membrane extracellular matrix. The CCN protein family is named after three protypical members; CYSTEINE-RICH PROTEIN 61; CONNECTIVE TISSUE GROWTH FACTOR; and NEPHROBLASTOMA OVEREXPRESSED PROTEIN.
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