A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation.
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Glucocerebrosidase is shaking up the synucleinopathiesThe role of saposin C in Gaucher diseaseThe protective role of prosaposin and its receptors in the nervous systemCathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid effluxNeurological deficits and glycosphingolipid accumulation in saposin B deficient mice.Severe vestibular dysfunction and altered vestibular innervation in mice lacking prosaposinProsaposin down-modulation decreases metastatic prostate cancer cell adhesion, migration, and invasionTemporal gene expression profiling reveals CEBPD as a candidate regulator of brain disease in prosaposin deficient mice.The birth prevalence of lysosomal storage disorders in the Czech Republic: comparison with data in different populations.Specific saposin C deficiency: CNS impairment and acid beta-glucosidase effects in the mouseThe exon 8-containing prosaposin gene splice variant is dispensable for mouse development, lysosomal function, and secretion.Multi-system disorders of glycosphingolipid and ganglioside metabolismBiosynthesis and degradation of mammalian glycosphingolipids.Secondary lipid accumulation in lysosomal disease.Serum prosaposin levels are increased in patients with advanced prostate cancer.Regional expression of prosaposin in the wild-type and saposin D-deficient mouse brain detected by an anti-mouse prosaposin-specific antibody.The function of sphingolipids in the nervous system: lessons learnt from mouse models of specific sphingolipid activator protein deficiencies.Tissue-specific effects of saposin A and saposin B on glycosphingolipid degradation in mutant mice.Direct tandem mass spectrometric profiling of sulfatides in dry urinary samples for screening of metachromatic leukodystrophy.Lysosomal storage disorders in the newborn.A saposin deficiency model in Drosophila: Lysosomal storage, progressive neurodegeneration and sensory physiological declineThe immunological functions of saposins.Saposin B mobilizes lipids from cholesterol-poor and bis(monoacylglycero)phosphate-rich membranes at acidic pH. Unglycosylated patient variant saposin B lacks lipid-extraction capacity.Progranulin, lysosomal regulation and neurodegenerative disease.Saposins (sap) A and C activate the degradation of galactosylsphingosine.Neurolysosomal pathology in human prosaposin deficiency suggests essential neurotrophic function of prosaposinSaposin C mutations in Gaucher disease patients resulting in lysosomal lipid accumulation, saposin C deficiency, but normal prosaposin processing and sorting.Concurrent increase of cholesterol, sphingomyelin and glucosylceramide in the spleen from non-neurologic Niemann-Pick type C patients but also patients possibly affected with other lipid trafficking disorders.Saposin C is required for normal resistance of acid beta-glucosidase to proteolytic degradation.Distribution of prosaposin mRNA in the central nervous system of the pigeon (Columba livia).Role of saposin C and D in auditory and vestibular function.The lipoprotein receptor-related protein-1 (LRP) adapter protein GULP mediates trafficking of the LRP ligand prosaposin, leading to sphingolipid and free cholesterol accumulation in late endosomes and impaired efflux.Conditional expression of human acid beta-glucosidase improves the visceral phenotype in a Gaucher disease mouse model.Clinical, biochemical and molecular characterization of prosaposin deficiency.Non-neuronopathic Gaucher disease due to saposin C deficiency.Prosaposin deficiency and saposin B deficiency (activator-deficient metachromatic leukodystrophy): report on two patients detected by analysis of urinary sphingolipids and carrying novel PSAP gene mutations.
P2860
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P2860
A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
A novel mutation in the coding ...... lactosylceramide accumulation.
@en
A novel mutation in the coding ...... lactosylceramide accumulation.
@nl
type
label
A novel mutation in the coding ...... lactosylceramide accumulation.
@en
A novel mutation in the coding ...... lactosylceramide accumulation.
@nl
prefLabel
A novel mutation in the coding ...... lactosylceramide accumulation.
@en
A novel mutation in the coding ...... lactosylceramide accumulation.
@nl
P2093
P356
P1476
A novel mutation in the coding ...... lactosylceramide accumulation.
@en
P2093
Befekadu A
Cervenková M
Hrebícek M
Poupetová H
P304
P356
10.1093/HMG/10.9.927
P577
2001-04-01T00:00:00Z