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Biomedical subjects

E Mussini

Publications and source records attributed to E Mussini.

At least 37 records · Page 2Linked to original sources
PubMed1984

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↗
PubMed1984

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↗
PubMed1983

Experimental pharmacological Parkinsonism (preliminary report).

The purpose of our project was to analyse membrane-bound proteins in Haloperidol-treated rats with clear Parkinson type motor inhibitions. Membrane-bound protein was chosen because the main sites of functional changes in the Parkinson syndrome may be the plasma membrane and postsynaptic membranes of nerve cells. Twenty male Sprague-Dawley rats were treated with Haloperidol for 67 days. The areas analyzed were the hippocampus and the caudate nucleus. The electrophoretic analyses were done by the method of Ballou (1974) as further elaborated by Booth (1977). Double-labeling analysis of 7 protein fractions after gel electrophoresis showed the presence of a 50 000-dalton protein in fraction 3 of the caudate nucleus (see block diagrams) in the haloperidol-treated animals but not in the hippocampus material.

Animals↗
PubMed1983

Small-bowel involvement in dermatitis herpetiformis and in linear-IgA bullous dermatosis.

In 23 patients with dermatitis herpetiformis (DH) and five patients with linear-IgA bullous dermatosis (BD), we evaluated the occurrence of histologic jejunal changes and small-bowel function abnormalities. None of the patients showed clinical signs or symptoms of malabsorption. Morphological jejunal changes consistent with gluten-sensitive enteropathy were found in 82% of DH patients and in 60% of BD patients. However, BD patients showed only mild jejunal histologic abnormalities, whereas more severe jejunal lesions were found in most patients with DH. Functional tests showed a rough correlation with the severity of the jejunal lesions, being almost completely normal in BD patients and DH patients with mild intestinal damage, whereas most of DH patients with subtotal or total villous atrophy showed abnormal d-xylose tests and folic acid assays. Lactose tolerance tests (H2 breath test and blood glucose after oral lactose load) showed no correlation with the degree of jejunal damage.

Adult↗
PubMed1983

Respiratory excretion of hydrogen and methane in Italian subjects after ingestion of lactose and milk.

Lactose malabsorption, by the breath hydrogen test, and lactose intolerance (presence of symptoms) were studied in twenty healthy Italian subjects after intake of 12.5, 25 and 50 g lactose, whole milk and low-lactose milk. A rise in respiratory concentration of hydrogen (greater than 20 ppm) (malabsorption) was found in fifteen subjects after 50 g lactose, in thirteen after 25 g and in seven after 12.5 g. Symptoms generally occurred in subjects presenting a rise in respiratory hydrogen excretion, but such a rise was often observed without symptoms. Thirteen subjects presented symptoms after 50 g lactose, but only three after 25 g and one after 12.5 g. Whole milk (500 ml) gave a lower incidence of lactose malabsorption than 25 g lactose (7/20 versus 13/20, P less than 0.05) and more subjects developed symptoms (7/20 versus 3/20, NS). Low-lactose milk produced no malabsorbers and one intolerant. Breath methane was detected constantly in seven subjects and in three on some of the days of observation. Respiratory methane excretion generally appeared to be unrelated to lactose ingestion.

Adult↗
PubMed1981

Metabolism of pinazepam by rat liver microsomes.

The pathways by which pinazepam and diazepam are metabolized by rat microsomes in vitro were studied in detail. Using a gas chromatographic technique to measure either the two parent compounds or their metabolites, it was demonstrated that pinazepam and diazepam were metabolized through the same pathways, but at different rates. Pinazepam was mainly N-dealkylated, while the C3-hydroxylation was a minor metabolic pathway. Diazepam was mostly C3-hydroxylated, with very little being N-demethylated. The different rats for the two metabolic pathways could be of importance in differentiating the action of the two drugs in vivo.

Animals↗
PubMed1981

Pharmacokinetic studies of ethylediaminetetraacetic acid (EDTA) in rats.

A gas chromatographic assay of ethylenediaminetetraacetic acid (EDTA) in rat serum and urine has been developed. The procedure involves benzene extraction of the sample, and uses the internal standard technique for determining EDTA concentrations in biological samples. The pharmacokinetics of EDTA was investigated in rats after i.v. injection of 5 and 50 mg/kg or oral administration of 50 and 250 mg/kg. No significant dose-related differences were between the mean biological half-lives (ranging between 21.6 and 22.9 min). EDTA was extracted in rat urine within 24 h of either i.v. dose, and within 80 min of the 50 mg/kg and 3 h of the 250 mg/kg or oral doses. In the applications described the analytical limit of sensitivity is 0.5 microgram/ml of rat serum of urine.

Administration, Oral↗
PubMed1981

Phosphodiesterase activity in muscles of control and dystrophic mice.

Cyclic AMP and cyclic GMP phosphodiesterase activity was determined in the heart and in nine skeletal muscles of control and dystrophic Re 129/J male and female mice. Phosphodiesterase activity in the presence of 0.5 mM cyclic AMP of cyclic GMP was increased in all the muscle but the heart of dystrophic mice.

Animals↗