메뉴 건너뛰기




Volumn 23, Issue 1, 2004, Pages 33-44

Identification of a family of animal sphingomyelin synthases

Author keywords

Apoptosis; Ceramide; Golgi; Lipid phosphate phosphatase; Sphingomyelin synthase

Indexed keywords

CERAMIDE; DIACYLGLYCEROL; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; PHOSPHORYLCHOLINE; SPHINGOLIPID; SPHINGOMYELIN; SPHINGOMYELIN SYNTHASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0842263750     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600034     Document Type: Article
Times cited : (518)

References (40)
  • 1
    • 0037203354 scopus 로고    scopus 로고
    • Sphingomyelin hydrolysis during apoptosis
    • Andrieu-Abadie N, Levade T (2002) Sphingomyelin hydrolysis during apoptosis. Biochim Biophys Acta 1585: 126-134
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 126-134
    • Andrieu-Abadie, N.1    Levade, T.2
  • 2
    • 0037059448 scopus 로고    scopus 로고
    • Cell biology Slick recruitment to the Golgi
    • Bankaitis VA (2002) Cell biology Slick recruitment to the Golgi. Science 295: 290-291
    • (2002) Science , vol.295 , pp. 290-291
    • Bankaitis, V.A.1
  • 3
    • 0032553310 scopus 로고    scopus 로고
    • Tumor necrosis factor induces ceramide oscillations and negatively controls sphingolipid synthases by caspases in apoptotic Kym-1 cells
    • Bourteele S, Hausser A, Doppler H, Horn-Muller J, Ropke C, Schwarzmann G, Pfizenmaier K, Muller G (1998) Tumor necrosis factor induces ceramide oscillations and negatively controls sphingolipid synthases by caspases in apoptotic Kym-1 cells. J Biol Chem 273: 31245-31251
    • (1998) J Biol Chem , vol.273 , pp. 31245-31251
    • Bourteele, S.1    Hausser, A.2    Doppler, H.3    Horn-Muller, J.4    Ropke, C.5    Schwarzmann, G.6    Pfizenmaier, K.7    Muller, G.8
  • 4
    • 0038359758 scopus 로고    scopus 로고
    • A new phospholipid phosphatase. PRG-1, is involved in axon growth and regenerative sprouting
    • Brauer AU, Savaskan NE, Kuhn H, Prehn S, Ninnemann O, Nitsch R (2003) A new phospholipid phosphatase, PRG-1, is involved in axon growth and regenerative sprouting. Nat Neurosci 6: 572-578
    • (2003) Nat Neurosci , vol.6 , pp. 572-578
    • Brauer, A.U.1    Savaskan, N.E.2    Kuhn, H.3    Prehn, S.4    Ninnemann, O.5    Nitsch, R.6
  • 5
    • 0036905264 scopus 로고    scopus 로고
    • Move over protein kinase C, you've got company
    • Brose N, Rosenmund C (2002) Move over protein kinase C, you've got company. J Cell Sci 115: 4399-4411
    • (2002) J Cell Sci , vol.115 , pp. 4399-4411
    • Brose, N.1    Rosenmund, C.2
  • 6
    • 0031936292 scopus 로고    scopus 로고
    • Quantitative analysis of phosphatidylcholine molecular species using HPLC and light scattering detection
    • Brouwers JF, Gadella BM, van Golde LM, Tielens AG (1998) Quantitative analysis of phosphatidylcholine molecular species using HPLC and light scattering detection. J Lipid Res 39: 344-353
    • (1998) J Lipid Res , vol.39 , pp. 344-353
    • Brouwers, J.F.1    Gadella, B.M.2    Van Golde, L.M.3    Tielens, A.G.4
  • 7
    • 0031662853 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals
    • Dickson RC (1998) Sphingolipid functions in Saccharomyces cerevisiae: comparison to mammals. Annu Rev Biochem 67: 27-48
    • (1998) Annu Rev Biochem , vol.67 , pp. 27-48
    • Dickson, R.C.1
  • 8
    • 0028008830 scopus 로고
    • Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes
    • Elmendorf HG, Haldar K (1994) Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes. J Cell Biol 124: 449-462
    • (1994) J Cell Biol , vol.124 , pp. 449-462
    • Elmendorf, H.G.1    Haldar, K.2
  • 9
    • 0033593788 scopus 로고    scopus 로고
    • Genetic evidence for ATP-dependent ER-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in CHO cells
    • Fukasawa M, Nishijima M, Hanada K (1999) Genetic evidence for ATP-dependent ER-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in CHO cells. J Cell Biol 144: 673-685
    • (1999) J Cell Biol , vol.144 , pp. 673-685
    • Fukasawa, M.1    Nishijima, M.2    Hanada, K.3
  • 10
    • 0025323167 scopus 로고
    • Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus
    • Futerman AH, Stieger B, Hubbard AL, Pagano RE (1990) Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus. J Biol Chem 265: 8650-8657
    • (1990) J Biol Chem , vol.265 , pp. 8650-8657
    • Futerman, A.H.1    Stieger, B.2    Hubbard, A.L.3    Pagano, R.E.4
  • 11
    • 0032971476 scopus 로고    scopus 로고
    • p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway
    • Gommel D, Orci L, Emig EM, Hannah MJ, Ravazzola M, Nickel W, Helms JB, Wieland FT, Sohn K (1999) p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway. FEBS Lett 447: 179-185
    • (1999) FEBS Lett , vol.447 , pp. 179-185
    • Gommel, D.1    Orci, L.2    Emig, E.M.3    Hannah, M.J.4    Ravazzola, M.5    Nickel, W.6    Helms, J.B.7    Wieland, F.T.8    Sohn, K.9
  • 12
  • 13
    • 0033991515 scopus 로고    scopus 로고
    • Inositol phosphoryl transferases from human pathogenic fungi
    • Heidler SA, Radding JA (2000) Inositol phosphoryl transferases from human pathogenic fungi. Biochim Biophys Acta 1500: 147-152
    • (2000) Biochim Biophys Acta , vol.1500 , pp. 147-152
    • Heidler, S.A.1    Radding, J.A.2
  • 15
  • 17
    • 0028210170 scopus 로고
    • Synthesis of surface sphingomyelin in the plasma membrane recycling pathway of BHK Cells
    • Kallen K-J, Allan D, Whatmore J, Quinn P (1994) Synthesis of surface sphingomyelin in the plasma membrane recycling pathway of BHK Cells. Biochim Biophys Acta 1191: 52-58
    • (1994) Biochim Biophys Acta , vol.1191 , pp. 52-58
    • Kallen, K.-J.1    Allan, D.2    Whatmore, J.3    Quinn, P.4
  • 19
    • 0029022032 scopus 로고
    • Sphingolipid synthesis as a target for chemotherapy against malaria parasites
    • Lauer SA, Ghori N, Haldar K (1995) Sphingolipid synthesis as a target for chemotherapy against malaria parasites. Proc Natl Acad Sci USA 92: 9181-9185
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9181-9185
    • Lauer, S.A.1    Ghori, N.2    Haldar, K.3
  • 20
    • 0033944545 scopus 로고    scopus 로고
    • Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae
    • Levine TP, Wiggins CA, Munro S (2000) Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol Biol Cell 11: 2267-2281
    • (2000) Mol Biol Cell , vol.11 , pp. 2267-2281
    • Levine, T.P.1    Wiggins, C.A.2    Munro, S.3
  • 21
    • 0021958898 scopus 로고
    • Intracellular translocation of fluorescent sphingolipids in cultured fibroblasts
    • Lipsky NG, Pagano RE (1985) Intracellular translocation of fluorescent sphingolipids in cultured fibroblasts. J Cell Biol 100: 27-34
    • (1985) J Cell Biol , vol.100 , pp. 27-34
    • Lipsky, N.G.1    Pagano, R.E.2
  • 22
    • 0032486257 scopus 로고    scopus 로고
    • Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation
    • Luberto C, Hannun YA (1998) Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. J Biol Chem 273: 14550-14559
    • (1998) J Biol Chem , vol.273 , pp. 14550-14559
    • Luberto, C.1    Hannun, Y.A.2
  • 24
    • 0022627769 scopus 로고
    • Sphingomyelin and ceramide-phosphoethanolamine synthesis by microsomes and plasma membranes from rat liver and brain
    • Malgat M, Maurice A, Baraud J (1986) Sphingomyelin and ceramide-phosphoethanolamine synthesis by microsomes and plasma membranes from rat liver and brain. J Lipid Res 27: 251-260
    • (1986) J Lipid Res , vol.27 , pp. 251-260
    • Malgat, M.1    Maurice, A.2    Baraud, J.3
  • 25
    • 0019409170 scopus 로고
    • The formation of sphingomyelin from phosphatidylcholine in plasma membrane preparations from mouse fibroblasts
    • Marggraf WD, Anderer FA, Kanfer JN (1981) The formation of sphingomyelin from phosphatidylcholine in plasma membrane preparations from mouse fibroblasts. Biochim Biophys Acta 664: 61-73
    • (1981) Biochim Biophys Acta , vol.664 , pp. 61-73
    • Marggraf, W.D.1    Anderer, F.A.2    Kanfer, J.N.3
  • 26
    • 0021760351 scopus 로고
    • The phosphorylcholine receptor in the phosphatidylcholine:ceramide cholinephosphotransferase reaction
    • Marggraf W-D, Kanfer JN (1984) The phosphorylcholine receptor in the phosphatidylcholine:ceramide cholinephosphotransferase reaction. Biochim Biophys Acta 793: 346-353
    • (1984) Biochim Biophys Acta , vol.793 , pp. 346-353
    • Marggraf, W.-D.1    Kanfer, J.N.2
  • 28
    • 0030753213 scopus 로고    scopus 로고
    • An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
    • Neuwald AF (1997) An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases. Protein Sci 6: 1764-1767
    • (1997) Protein Sci , vol.6 , pp. 1764-1767
    • Neuwald, A.F.1
  • 29
    • 0037203342 scopus 로고    scopus 로고
    • Ceramide in apoptosis: An overview and current perspectives
    • Pettus BJ, Chalfant CE, Hannun YA (2002) Ceramide in apoptosis: an overview and current perspectives. Biochim Biophys Acta 1585:114-125
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 114-125
    • Pettus, B.J.1    Chalfant, C.E.2    Hannun, Y.A.3
  • 30
    • 0035918285 scopus 로고    scopus 로고
    • Basic fibroblast growth factor-induced proliferation of primary astrocytes
    • Riboni L, Viani P, Bassi R, Giussani P, Tettamanti G (2001) Basic fibroblast growth factor-induced proliferation of primary astrocytes. J Biol Chem 276: 12797-12804
    • (2001) J Biol Chem , vol.276 , pp. 12797-12804
    • Riboni, L.1    Viani, P.2    Bassi, R.3    Giussani, P.4    Tettamanti, G.5
  • 31
    • 0033597141 scopus 로고    scopus 로고
    • Association of sterol-and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains
    • Rietveld A, Neutz S, Simons K, Eaton S (1999) Association of sterol-and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains. J Biol Chem 274: 12049-12054
    • (1999) J Biol Chem , vol.274 , pp. 12049-12054
    • Rietveld, A.1    Neutz, S.2    Simons, K.3    Eaton, S.4
  • 32
    • 0027227621 scopus 로고
    • Phospholipids from the free-living nematode Caenorhabditis elegans
    • Satouchi K, Hirano K, Sakaguchi M, Takehara H, Matsuura F (1993) Phospholipids from the free-living nematode Caenorhabditis elegans. Lipids 28: 837-840
    • (1993) Lipids , vol.28 , pp. 837-840
    • Satouchi, K.1    Hirano, K.2    Sakaguchi, M.3    Takehara, H.4    Matsuura, F.5
  • 33
    • 0031022602 scopus 로고    scopus 로고
    • SAM as a protein interaction domain involved in developmental regulation
    • Schultz J, Ponting CP, Hofmann K, Bork P (1997) SAM as a protein interaction domain involved in developmental regulation. Protein Sci 6: 249-253
    • (1997) Protein Sci , vol.6 , pp. 249-253
    • Schultz, J.1    Ponting, C.P.2    Hofmann, K.3    Bork, P.4
  • 34
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 35
    • 0034189787 scopus 로고    scopus 로고
    • A novel pathway for transport and metabolism of a fluorescent phosphatidic acid analog in yeast
    • Trotter PJ (2000) A novel pathway for transport and metabolism of a fluorescent phosphatidic acid analog in yeast. Traffic 1: 425-434
    • (2000) Traffic , vol.1 , pp. 425-434
    • Trotter, P.J.1
  • 36
    • 0015987808 scopus 로고
    • The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver
    • Ullman MD, Radin NS (1974) The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver. J Biol Chem 249: 1506-1512
    • (1974) J Biol Chem , vol.249 , pp. 1506-1512
    • Ullman, M.D.1    Radin, N.S.2
  • 38
    • 0028055154 scopus 로고
    • Conversion of diacylglycerol to phosphatidylcholine on the basolateral surface of epithelial MDCK cells
    • van Helvoort A, van't Hof W, Ritsema T, Sandra A, van Meer G (1994) Conversion of diacylglycerol to phosphatidylcholine on the basolateral surface of epithelial MDCK cells. J Biol Chem 269: 1763-1769
    • (1994) J Biol Chem , vol.269 , pp. 1763-1769
    • Van Helvoort, A.1    Van't Hof, W.2    Ritsema, T.3    Sandra, A.4    Van Meer, G.5
  • 39
    • 0020287371 scopus 로고
    • Cellular and enzymic synthesis of sphingomyelin
    • Voelker DR, Kennedy EP (1982) Cellular and enzymic synthesis of sphingomyelin. Biochemistry 21: 2753-2759
    • (1982) Biochemistry , vol.21 , pp. 2753-2759
    • Voelker, D.R.1    Kennedy, E.P.2
  • 40
    • 0032775582 scopus 로고    scopus 로고
    • Structural organization of mammalian lipid phosphate phosphatases: Implications for signal transduction
    • Waggoner DW, Xu J, Singh I, Jasinska R, Zhang QX, Brindley DN (1999) Structural organization of mammalian lipid phosphate phosphatases: implications for signal transduction. Biochim Biophys Acta 1439: 299-316
    • (1999) Biochim Biophys Acta , vol.1439 , pp. 299-316
    • Waggoner, D.W.1    Xu, J.2    Singh, I.3    Jasinska, R.4    Zhang, Q.X.5    Brindley, D.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.