Search PubMed⌕ Search

Biomedical subjects

M Rimoldi

Publications and source records attributed to M Rimoldi.

68 records · Page 4Linked to original sources
PubMed1980

Ketogenic response to fasting in human carnitine deficiencies.

Carnitine and its short-chain and long-chain esters have been determined in muscle and liver of two patients with carnitine-deficient myopathy. Plasma carnitines and ketone bodies were monitored in the two patients during a 38-h fast. The two patients showed different ketogenic responses to the fast. One patient, with carnitine deficiency restricted to skeletal muscle, had exaggerated ketone production on fasting. The other patient, with carnitine deficiency in skeletal muscle and liver, had poor ketone body production on fasting. It is assumed that the presence of adequate levels of carnitine in the liver are crucial for the activation of ketogenic machinery in liver.

Adult↗
PubMed1980

"Carnitine deficient" myopathy and cardiomyopathy with fatal outcome.

A 13-year-old boy with a mild limb girdle muscular weakness had a massive rhabdomyolysis and cardiac arrest after general anesthesia. A congestive cardiomyopathy then developed. Muscle biopsy revealed an unspecific "myopathic" degeneration of muscle fibers and a slight accumulation of lipid droplets. Carnitine content was markedly reduced in muscle and moderately in plasma. Both prednisone and carnitine therapies were unable to improve the heart insufficiency, and the patient died 1 year after the acute episode of rhabdomyolysis.

Adolescent↗
PubMed1979

Fatal ataxic encephalopathy and carnitine acetyltransferase deficiency: a functional defect of pyruvate oxidation?

A 3-year 8-month-old girl died after 14 months of illness characterized by episodes of intermittent ataxia associated with oculomotor palsy, hypotonia, mental confusion, and disturbances of consciousness. In the last 4 months of life, there were signs of liver dysfunction. Pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase activities were normal in autopsy brain specimens and in cultured fibroblasts from the patient. Carnitine acetyltransferase was deficient in liver, brain, kidney, and cultured fibroblasts. Medium- and long-chain carnitine acyltransferase activities were normal. It is proposed that a functional defect of acetyl-coenzyme A (acetyl-CoA) utilization in brain mitochondria accompanies the carnitine acetyltransferase deficiency.

Acetyltransferases↗
PubMed1979

Hepatic ketogenesis and muscle carnitine deficiency.

The levels of plasma free carnitine and ketone bodies have been found to fluctuate inversely in fasting individuals without muscle disease. Circulating short-chain acyl-carnitines paralleled beta-hydroxybutyrate levels. A patient with lipid storage myopathy and muscle carnitine deficiency, and his two daughters, developed exaggerated ketogenesis on fasting. The content of total carnitines in the patient's liver was normal, but free carnitine was reduced to 50 percent, and total esterified carnitines were four times greater than the mean value for the controls. The decreased muscle carnitine content in this case may have resulted from chronic hepatic ketogenesis, draining muscle carnitine. Alternatively, decreased muscle carnitine content may have initiated hepatic ketogenesis.

Acetoacetates↗
PubMed1978

Acid maltase deficiency in adults. Clinical, morphological and biochemical study of three patients.

3 adult women with distinct clinical pictures of progressive myopathy were studied. The morphological findings of biopsied skeletal muscle suggested the diagnosis of type II glycogenosis. Biochemical analysis confirmed a profound deficiency of alpha-1,4-glucosidase activity. Electrophoresis of muscle acid maltase showed the presence of one band in normal individuals. A very faint band with normal electrophoretic mobility was present in the patients' muscles. Muscle neutral maltase is composed of four bands in normal adult individuals: two of the four bands were clearly reduced in the muscles of the patients. The acid and neutral maltases were not significantly reduced in the patients' leukocytes. Acid maltase determination in urine made it possible to identify the homozygous, but not to completely segregate the heterozygous, from unaffected adult subjects.

Female↗
PubMedDate not supplied

Analysis of heat shock transcription factor for suppression of polyglutamine toxicity.

Individually over-expressed chaperones can interfere with cytotoxicity and aggregation of polyglutamine proteins in disease models. As chaperones cooperate, the analysis of suppression or reversal of polyglutamine pathology may require ways to up-regulate multiple chaperone coding genes. This condition might be achieved by exogenous expression of de-repressed forms of heat shock transcription factor 1 (HSF1), which mediates induction of several genes coding cytosolic and nuclear chaperones. Here we present the rationale behind this possible approach and the caveats, and employ a non-neuronal cell system to test whether Ataxin-1 aggregation can be modulated by de-repressed HSF1 mutants through augmented expression of chaperone coding genes. In our experiments, HSF1 mutants have induced heat shock protein 70 and Human DnaJ (HDJ)-1 to intermediate levels. Cells expressing such mutants also showed partial reduction of Ataxin-1 [31Q] aggregation. A consolidated positive outcome of these tests in cellular models would encourage experiments in transgenic mice and prospects for pharmacological modulation of HSF1 activity or delivery.

Animals↗