Enzymatic Hydrolysis of Sphingolipids

Barnholz, Yehezkel; Roitman, A.; Gátt, Shimon

doi:10.1016/s0021-9258(18)99833-9

Cited by 140 publications

(8 citation statements)

References 11 publications

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“…Sphingomyelin was prepared from bovine brain as described previously (Barenholz et al, 1966). Tritium-labeled sphingomyelin of spinal cord was prepared by catalytic hydrogenation with tritium gas in the presence of palladium on charcoal ) and was diluted with nonradioactive SM of bovine brain.…”

Section: Methodsmentioning

confidence: 99%

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Studies on the molecular packing of mixed dispersions of Triton X-100 and sphingomyelin and its dependence on temperature and cloud point

Lichtenberg¹,

Yedgar²,

Cooper³

et al. 1979

Biochemistry

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Section: Methodsmentioning

confidence: 99%

“…The rate of enzymatic hydrolysis of sphingomyelin was determined by the method of Barenholz et al (1966) as modified for assaying the hydrolysis of lecithin (Gatt, 1968). The assay mixtures were prepared by method B of Yedgar et al (1974b).…”

Section: Methodsmentioning

confidence: 99%

Studies on the molecular packing of mixed dispersions of Triton X-100 and sphingomyelin and its dependence on temperature and cloud point

Lichtenberg¹,

Yedgar²,

Cooper³

et al. 1979

Biochemistry

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“…A SM-cleaving hydrolase, the SM phosphodiesterase also called acid sphingomyelinase (ASM, E.C. 3.1.4.12) was discovered by Shimon Gatt in 1966 [8] and its deficiency identified by R. O. Brady as the cause of the progressive SM accumulation in Niemann-Pick disease [9]. Autosomal recessive Niemann-Pick disease caused by ASM deficiency is a rare lysosomal storage disorder with a broad disease spectrum that includes chronic visceral (type B) and neurovisceral forms (intermediate type A/B) as well as the infantile, rapidly progressive fatal neurovisceral disease (type A) with type B being the most prevalent [10] More recently, Niemann-Pick disease type A and B was renamed as ASM deficiency or ASMD to clearly differentiate the underlying pathology from Niemann-Pick disease type C which is caused by an intracellular cholesterol transport defect leading to the accumulation of cholesterol and SM but not by ASM deficiency [11].…”

Section: Introductionmentioning

confidence: 99%

Acid Sphingomyelinase, a Lysosomal and Secretory Phospholipase C, Is Key for Cellular Phospholipid Catabolism

Breiden¹,

Sandhoff

2021

IJMS

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Here, we present the main features of human acid sphingomyelinase (ASM), its biosynthesis, processing and intracellular trafficking, its structure, its broad substrate specificity, and the proposed mode of action at the surface of the phospholipid substrate carrying intraendolysosomal luminal vesicles. In addition, we discuss the complex regulation of its phospholipid cleaving activity by membrane lipids and lipid-binding proteins. The majority of the literature implies that ASM hydrolyses solely sphingomyelin to generate ceramide and ignores its ability to degrade further substrates. Indeed, more than twenty different phospholipids are cleaved by ASM in vitro, including some minor but functionally important phospholipids such as the growth factor ceramide-1-phosphate and the unique lysosomal lysolipid bis(monoacylglycero)phosphate. The inherited ASM deficiency, Niemann-Pick disease type A and B, impairs mainly, but not only, cellular sphingomyelin catabolism, causing a progressive sphingomyelin accumulation, which furthermore triggers a secondary accumulation of lipids (cholesterol, glucosylceramide, GM2) by inhibiting their turnover in late endosomes and lysosomes. However, ASM appears to be involved in a variety of major cellular functions with a regulatory significance for an increasing number of metabolic disorders. The biochemical characteristics of ASM, their potential effect on cellular lipid turnover, as well as a potential impact on physiological processes will be discussed.

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“…These bases occur in nature in the phospho-and glycosphingolipids, which can be regarded as derivatives of ceramide, the N-acylated sphingosine base (reviewed in Hanahan and Brockerhofif, 1965). Enzymes which hydrolyze the sphingolipids of animal origin have been isolated (Gatt, 1963(Gatt, ,b, 1967Barenholz and Gatt, 1966;Rapport, 1965, 1966a,b;Gatt, 1966, 1967a,b, Leibovitz and Gatt, 1968;Heller and Shapiro, 1966;Brady et al, 1965aBrady et al, ,b, 1967Hajra et al, 1966;Sandhoff and Jatzkewitz, 1967;Schneider and Kennedy, 1967). These enzymes can account for the complete, stepwise hydrolysis of the sphingolipids to a long-chain base, fatty acid, and the individual carbohydrate residues, or phosphorylchloline (summarized in ).…”

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confidence: 99%