ArticleJournal of bioenergetics and biomembranes2001
Neutral magnesium-dependent sphingomyelinase from liver plasma membrane: purification and inhibition by ubiquinol.
Article in Journal of bioenergetics and biomembranes, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 32 citations in OpenAlex.
- Diverse Roles of Ceramide in the Progression and Pathogenesis of Alzheimer's Disease.Biomedicines · 2022Review
- Small Molecule Inhibitors Targeting Biosynthesis of Ceramide, the Central Hub of the Sphingolipid Network.Journal of medicinal chemistry · 2021Review
- Dietary fat modifies mitochondrial and plasma membrane apoptotic signaling in skeletal muscle of calorie-restricted mice.Age (Dordrecht, Netherlands) · 2013Article
- Vitamin E prevents the age-dependent and palmitate-induced disturbances of sphingolipid turnover in liver cells.Age (Dordrecht, Netherlands) · 2012Article
- Drug targeting of sphingolipid metabolism: sphingomyelinases and ceramidases.British journal of pharmacology · 2011Review
- 4-Nitrobenzoate inhibits coenzyme Q biosynthesis in mammalian cell cultures.Nature chemical biology · 2010Article
- Coenzyme Q-dependent functions of plasma membrane in the aging process.Age (Dordrecht, Netherlands) · 2005Article
- Preimplantation diagnosis of a lysosomal storage disorder by in situ enzymatic activity: 'proof of principle' in acid sphingomyelinase-deficient mice.Journal of inherited metabolic disease · 2005Article
- A novel plasma membrane quinone reductase and NAD(P)H:quinone oxidoreductase 1 are upregulated by serum withdrawal in human promyelocytic HL-60 cells.Journal of bioenergetics and biomembranes · 2002Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasma membranes isolated from pig liver contained almost no acid sphingomyelinase but significant neutral magnesium-dependent sphingomyelinase that was activated by phosphatidylserine. We report here the purification to apparent homogeneity of neutral sphingomyelinase of about 87 kDa from liver plasma membranes. The purified enzyme strictly required magnesium and had a neutral optimal pH. In contrast with neutral sphingomyelinase purified from other sources (such as brain), the enzyme purified from from liver plasma membrane was not inhibited by GSH and, strikingly, it was not activated by phosphatidylserine. Liver sphingomyelinase was inhibited by several lipophilic antioxidants in a dose-dependent way. Ubiquinol-10 was more effective than alpha-tocopherol, alpha-tocopherylquinone, alpha-tocopherylquinone, and ubiquinone-10, and inhibition was noncompetitive. Differential inhibition of neutral sphingomyelinase by antioxidants did not correlate with different levels of protection against lipid peroxidation. The purified sphingomyelinase was not inhibited significantly by ubiquinone-10 and ubiquinol- 10, but ubiquinol-0 and ubiquinone-0 inhibited by 30 and 60% respectively. Our results demonstrate a direct inhibitory effect of ubiquinol on the plasma membrane n-SMase and support the participation of this molecule in the regulation of ceramide-mediated signaling.
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