Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.3.1.8 (acyl-CoA dehydrogenase)
 785 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Earlier research on ten horses suffering from the frequently fatal disorder atypical myopathy showed that MADD (multiple acyl-CoA dehydrogenase deficiency) is the biochemical derangement behind atypical myopathy. From five horses that died as a result of this disease and seven healthy control horses, urine and plasma were collected ante mortem and muscle biopsies were obtained immediately post-mortem (2 patients and 7 control horses), to analyse creatine, purine and carbohydrate metabolism as well as oxidative phosphorylation. In patients, the mean creatine concentration in urine was increased 17-fold and the concentration of uric acid approximately 4-fold, compared to controls. The highest degree of depletion of glycogen was observed in the patient with the most severe myopathy clinically. In this patient, glycolysis was more active than in the other patients and controls, which may explain this depletion. One patient demonstrated very low phosphoglycerate mutase (PGAM) activity, less than 10% of reference values. Most respiratory chain complex activity in patients was 20-30% lower than in control horses, complex II activity was 42% lower than normal, and one patient had severely decrease ATP-synthase activity, more than 60% lower than in control horses. General markers for myopathic damage are creatine kinase (CK) and lactic acid in plasma, and creatine and uric acid in urine. To obtain more information about the cause of the myopathy analysis of carbohydrate, lipid and protein metabolism as well as oxidative phosphorylation is advised. This study expands the diagnostic possibilities of equine myopathies.
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PMID:Decreased oxidative phosphorylation and PGAM deficiency in horses suffering from atypical myopathy associated with acquired MADD. 2184 62

In the experiments reported here, we used the female ladybird Coccinella septempunctata L. as a model to identify diapause-associated proteins using proteomics technology. Our results indicated that protein expression patterns of diapausing and nondiapausing individuals were highly differentiated. A total of 58 spots showed significant differences in abundance (Ratio > 2 and P < 0.05) according to two-dimensional electrophoresis and GE Image Scanner III analysis. Sixteen protein spots were further investigated using mass spectrometry. Eight proteins were characterized, including chaperones and proteins involved in glucose metabolism, lipid metabolism, and the tricarboxylic acid cycle. Among these proteins, five proteins were upregulated in diapausing female adults, including a chaperone (Symbionin symL), malate dehydrogenase (putative), two proteins linked to lipid metabolism (unknown and conserved hypothetical protein) and phosphoglyceromutase (partial). By contrast, isocitrate dehydrogenase (RH49423p), fumarylacetoacetate hydrolase (AGAP001942-PA), and a putative medium chain acyl-CoA dehydrogenase were downregulated. These results contribute to the understanding of diapause mechanisms of the ladybird C. septempunctata and may suggest methods for improving the application of this natural enemy insect.
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PMID:Proteomic research on diapause-related proteins in the female ladybird, Coccinella septempunctata L. 2660 22