Gene/Protein
Disease
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Drug
Enzyme
Compound
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Target Concepts:
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Query: UMLS:C0029089 (
ophthalmoplegia
)
3,338
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We examined the degradation of a labeled phosphatidylglycerol (PG) by fibroblasts from a normal control and a patient with Niemann-Pick (NP) disease. The control homogenate had both phospholipase A and
phospholipase C
activities toward PG, but NP cells had only phospholipase A. The PG
phospholipase C
of control fibroblasts was solubilized by sonication and freezing and thawing, was most active at pH 5.0, and was inhibited by Ca2-, detergents, sphingomyelin, and 5' AMP. Assay of PG
phospholipase C
in fibroblast cultures from NP patients with sphingomyelinase deficiency (three designated type A and four type B) confirmed absence of activity, whereas cultures from NP patients without sphingomyelinase deficiency (three designated type C and one with neurovisceral lipidoses and vertical supranuclear
ophthalmoplegia
) had activities close to those of normal controls. These findings substantiate previous observations of low phosphodiesterase activities in NP disease and suggest that the enzymatic function affected by the NP genes includes specificity toward PG and sphingomyelin. Deficiency of PG
phospholipase C
may explain the accumulation of bis(monoacylglycero)phosphate in NP disease.
...
PMID:Deficiency of phospholipase C acting on phosphatidylglycerol in Niemann-Pick disease. 668 61
Examination of release of labeled glyceride from 2-[1-14C]oleoyl phosphatidylcholine by a soluble extract of human fibroblasts confirmed the presence of phosphodiesterase which is stimulated strongly by sodium taurocholate. This activity was maximal at pH 4.5 and was inhibited by sphingomyelin and 5' AMP. Assay of the phosphatidylcholine phosphodiesterase activity in fibroblast cultures from patients with Niemann-Pick disease revealed a severe deficiency in those cultures also deficient in sphingomyelinase (3 type A and 4 type B) whereas assay of cultures from Niemann-Pick patients without sphingomyelinase deficiency (3 type C and 1 with neurovisceral lipidosis and vertical supranuclear
ophthalmoplegia
) gave activities similar to controls. The distribution of label in the products of the reactions catalyzed by both control and Niemann-Pick extracts indicates that the phosphodiesterase activity observed was
phospholipase C
and that phospholipase D was not involved. The close correlation of phosphatidylcholine
phospholipase C
and sphingomyelinase activities in the control and mutant fibroblasts strongly suggests that both activities are catalyzed by one enzyme. Various alterations in the regulation of the specificity of a multifunctional
phospholipase C
may underlie phenotypic variation in Niemann-Pick disease.
...
PMID:Deficiency of taurocholate-dependent phospholipase C acting on phosphatidylcholine in Niemann-Pick disease. 685 19
