1994
DOI: 10.1006/bbrc.1994.1612
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Sphingolipid Activator Protein D (sap-D) Stimulates the Lysosomal Degradation of Ceramide in Vivo

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Cited by 154 publications
(97 citation statements)
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“…Previous data obtained by computer analysis and comparison of the secondary structures of sphingolipid activator proteins and ASM suggest a high similarity between the ASM domain N-terminal to the hinge region and the activator proteins (Ponting, 1994). Since ASM, in contrast to most other lysosomal hydrolases degrading sphingolipids with short hydrophilic groups, does not need stimulation by known sphingolipid activator proteins in vivo (Klein et al, 1994), the mature enzyme of 70 kDa may already contain an intrinsic sphingomyelin activating domain loosely attached to the enzymatic domain (57 kDa) by a proline spacer.…”
Section: Phosphorylation Of the Asm Oligosaccharidesmentioning
confidence: 90%
“…Previous data obtained by computer analysis and comparison of the secondary structures of sphingolipid activator proteins and ASM suggest a high similarity between the ASM domain N-terminal to the hinge region and the activator proteins (Ponting, 1994). Since ASM, in contrast to most other lysosomal hydrolases degrading sphingolipids with short hydrophilic groups, does not need stimulation by known sphingolipid activator proteins in vivo (Klein et al, 1994), the mature enzyme of 70 kDa may already contain an intrinsic sphingomyelin activating domain loosely attached to the enzymatic domain (57 kDa) by a proline spacer.…”
Section: Phosphorylation Of the Asm Oligosaccharidesmentioning
confidence: 90%
“…Sap D has been proposed to have a role in ceramide degradation, since its addition to the culture medium of fibroblasts from a patient suffering from prosaposin deficiency resulted in the reduction of ceramide storage (22). Recently it has been .…”
Section: Discussionmentioning
confidence: 99%
“…Control radioactivity was measured by adding SAPs and enzyme only after termination of the incubation. SAPs, SAP-A to D, were purified from human tissues [7]. ct-Galactosidase activity was measured with 4-methylumbeUiferyl-eto-galactopyranoside as the artificial substrate [10].…”
Section: Enzyme Assaysmentioning
confidence: 99%
“…Four of the five known SAPs, SAP-A to D, also called saposin A-D, are derived from a common precursor [4][5][6]. Despite their homology, like the identical locations of cysteine residues and glycosylation sites, SAP-B, C and D have different functions, which comprise lipid binding and enzyme stimulating specificities [3,7]. On the other hand, the physiological function of SAP-A remains unclear because no SAP-A deficiency has been characterized so far [3].…”
Section: Introductionmentioning
confidence: 99%