The neutral sphingomyelinase family: Identifying biochemical connections
نویسندگان
چکیده
منابع مشابه
Nuclear localization of neutral sphingomyelinase 1: biochemical and immunocytochemical analyses.
To examine the intracellular localization of neutral sphingomyelinase 1 (nSMase 1), a rabbit polyclonal antibody was raised against a recombinant form of the enzyme expressed in E. coli. It has been reported that, in rat liver or in ascites hepatoma AH7974, high activity of neutral sphingomyelinase (SMase) is found at the plasma membrane, with a lesser but significant amount in nucleus and cyto...
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Our understanding of the functions of neutral sphingomyelinase (N-SMase) signaling has advanced over the past decade. In this review, we focus on the roles and regulation of N-SMase 1, N-SMase 2, N-SMase 3, an enzyme that generates the bioactive lipid ceramide through the hydrolysis of the membrane lipid sphingomyelin. A large body of work has now implicated N-SMase 2 in a diverse set of cellul...
متن کاملNeutral sphingomyelinase 2 (nSMase2) is the primary neutral sphingomyelinase isoform activated by tumour necrosis factor-α in MCF-7 cells.
Activation of N-SMase (neutral sphingomyelinase) is an established part of the response of cytokines such as TNF (tumour necrosis factor)-α. However, it remains unclear which of the currently cloned N-SMase isoforms (nSMase1, nSMase2 and nSMase3) are responsible for this activity. In MCF-7 cells, we found that TNF-α induces late, but not early, increases in N-SMase activity, and that nSMase2 is...
متن کاملInvolvement of neutral sphingomyelinase in the angiotensin II signaling pathway.
The possibility that angiotensin II (ANG II) exerts its effects through the activation of neutral sphingomyelinase (nSMase) has not been tested in kidneys. The results of the present study provide evidence for the activity and expression of nSMase in rat kidneys. In isolated perfused rat kidney, ANG II-induced renal vasoconstriction was inhibited by GW4869, an inhibitor of nSMase. We used nSMas...
متن کاملThe subcellular localization of neutral sphingomyelinase in rat liver.
The subcellular distribution of neutral sphingomyelinase activity has been determined in rat liver. Neutral sphingomyelinase is present in the plasma membrane. This enzyme requires either Mg2+ or Mn2+ for full activity; these cations cannot be replaced by Co2+ or Ca2+. The plasma membrane sphingomyelinase is strongly inhibited by Hg2+. A small amount of neutral spingomyelinase activity appears ...
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ژورنال
عنوان ژورنال: Advances in Enzyme Regulation
سال: 2011
ISSN: 0065-2571
DOI: 10.1016/j.advenzreg.2010.09.016