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Biomedical subjects

G De Ponte

Publications and source records attributed to G De Ponte.

7 recordsLinked to original sources

Effect of swimming on protein degradation: 3-methylhistidine and creatinine excretion.

The effect of 5-km noncompetitive swimming (moderate exercise) and 2-km competitive speed swimming (intensive exercise) on protein breakdown was studied in a group of young male volunteers (16-20 years old) who followed a 3-MH-free diet throughout the study. Urinary 3-MH and creatinine were determined over a period of 24 and 48 hr as an index of protein degradation. Basal 3-MH levels in the two groups of swimmers were 2.85 and 3.07 mumole X kg-1 X day-1. Mean rates of 3-MH excretion were, respectively, 1.54 and 1.94 mumole X kg-1 X day-1 for the 48 hr after moderate exercise and the 24 hr after intensive exercise. The decrease in 3-MH urinary excretion was still evident when calculated as the urinary 3-MH-to-creatinine ratio.

Adolescent

Increased myofibrillar protein catabolism in duchenne muscular dystrophy measured by 3-methylhistidine excretion in the urine.

Myofibrillar protein catabolic rate was calculated in 50 young patients with Duchenne muscular dystrophy from the amount of 3-methylhistidine excreted in the urine, and was found to be about seven times that of a control series, expressed as the percentage of myofibrillar protein catabolized per day. This wastage of myofibrillar protein is a consequence of Duchenne muscular dystrophy and inhibition of protein degradation appears to be one possible approach in the treatment of this disease.

Child

Decrease in N-acetyl-L-aspartic acid in brain of myodystrophic mice.

Brain tissue from myodystrophic mice (male 129/ReJ-dy and female 129 B6F1/J-dy) was examined to determine whether CNS abnormalities accompany the known muscular defects. Brain N-acetyl-L-aspartate, aspartate, and glutamate were significantly lower than in brain from control mice. These amino acids are only slightly reduced in brains of female dystrophic mice.

Animals

Content of methylhistidines in normal and pathological human skeletal muscles.

The content of 3-methylhistidine (3-MH) and 1-methylhistidine (1-MH) was measured in muscle biopsy specimens from 13 normal controls, 19 patients with Duchenne muscular dystrophy, 8 limb-girdle disease patients, and 23 disease controls with different forms of muscular pathology. 3-MH and 1-MH concentrations in normal human muscle did not appear to be influenced by sex, body weight, and age, at least for subjects in the 10--60 year age group examined. Skeletal muscle 1-MH levels did not significantly differ from mean control values in any of the pathologies investigated. In the patient population examined, the mean 3-MH level per unit of noncollagen protein (NCP) was significantly lower than normal in Duchenne dystrophy only, the reduction being related to disease severity. The significantly lower concentrations of 3-MH in muscle of Duchenne patients indicate the importance of measuring 3-MH in diseased muscle to obtain reliable estimates of the myofibrillar protein catabolic rate.

Adolescent