INT72870
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
However, more recent studies showed that both mutations reduce the normal serine palmitoyltransferase activity in various mammalian cell types, including cultured lymphoblasts from HSN1 patients indicating that SPTLC1 mutations are dominant inactivating [23,24]. | |||||||||||||||
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Carnitine palmitoyltransferase-II deficiency was suspected based on the determination of serum acylcarnitines by tandem mass spectrometry which showed a characteristic elevation of long-chain C16 and C18:1 acylcarnitines. | |||||||||||||||
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CONCLUSION: Carnitine palmitoyltransferase-II deficiency should be included in the differential diagnosis of isolated muscular weakness even when manifesting in early childhood. | |||||||||||||||
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Moreover, both chemical depalmitoylation by hydroxylamine and inhibition of palmitoyl-CoA transferase in vivo by tunicamycin treatment incresed the reconstitutive activity of detergent extracts and eliminated the differences between native and opioid-dependent cells, indicating that the increase in stimulatory activity is due to depalmitoylation of Gs alpha. | |||||||||||||||
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These mutations are dominant and decrease serine palmitoyltransferase activity by 50% when the wild-type and mutant LCB1 alleles are coexpressed. | |||||||||||||||
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Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. | |||||||||||||||
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We found that the corresponding mutations in the LCB1 gene of Saccharomyces cerevisiae reduce serine palmitoyltransferase activity. | |||||||||||||||
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