메뉴 건너뛰기




Volumn 112, Issue 4, 2010, Pages 1088-1097

Purification of neutral sphingomyelinase 2 from bovine brain and its calcium-dependent activation

Author keywords

Calcium; Ceramide; Characterization; Neutral sphingomyelinase 2; Purification

Indexed keywords

BRAIN EXTRACT; CALCIMYCIN; CALCIUM ION; CERAMIDE; FUMONISIN B1; GW 4869; MAGNESIUM ION; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOMYELIN PHOSPHODIESTERASE INHIBITOR; SPHINGOMYELINASE 2; TRITON X 100; UNCLASSIFIED DRUG;

EID: 75149116783     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06527.x     Document Type: Article
Times cited : (11)

References (30)
  • 1
    • 0026399923 scopus 로고
    • The calcium signal for transmitter secretion from presynaptic nerve terminals
    • Augustine G. J., Adler E. M. Charlton M. P. (1991) The calcium signal for transmitter secretion from presynaptic nerve terminals. Ann. N Y Acad. Sci. 635, 365 381.
    • (1991) Ann. N y Acad. Sci. , vol.635 , pp. 365-381
    • Augustine, G.J.1    Adler, E.M.2    Charlton, M.P.3
  • 2
    • 0034677881 scopus 로고    scopus 로고
    • Purification and characterization of a magnesium-dependent neutral sphingomyelinase from bovine brain
    • Bernardo K., Krut O., Wiegmann K. et al. (2000) Purification and characterization of a magnesium-dependent neutral sphingomyelinase from bovine brain. J. Biol. Chem. 275, 7641 7647.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7641-7647
    • Bernardo, K.1    Krut, O.2    Wiegmann, K.3
  • 3
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E. G. Dyer W. J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911 917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 6
    • 0037605881 scopus 로고    scopus 로고
    • 2) enzymes in membrane trafficking: Mediators of membrane shape and function
    • 2) enzymes in membrane trafficking: mediators of membrane shape and function. Traffic 4, 214 221.
    • (2003) Traffic , vol.4 , pp. 214-221
    • Brown, W.J.1    Chambers, K.2    Doody, A.3
  • 8
    • 0032406354 scopus 로고    scopus 로고
    • Calcium sensors in regulated exocytosis
    • Burgoyne R. D. Morgan A. (1998) Calcium sensors in regulated exocytosis. Cell Calcium 24, 367 376.
    • (1998) Cell Calcium , vol.24 , pp. 367-376
    • Burgoyne, R.D.1    Morgan, A.2
  • 9
    • 0032868933 scopus 로고    scopus 로고
    • Neutral sphingomyelinase: Past, present and future
    • Chatterjee S. (1999) Neutral sphingomyelinase: past, present and future. Chem. Phys. Lipids 102, 79 96.
    • (1999) Chem. Phys. Lipids , vol.102 , pp. 79-96
    • Chatterjee, S.1
  • 10
    • 47749095383 scopus 로고    scopus 로고
    • Linking calcium to Abeta and Alzheimer's disease
    • Green K. N. LaFerla F. M. (2008) Linking calcium to Abeta and Alzheimer's disease. Neuron 59 (2 190 194.
    • (2008) Neuron , vol.59 , Issue.2 , pp. 190-194
    • Green, K.N.1    Laferla, F.M.2
  • 11
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • Hannun Y. A. Obeid L. M. (2008) Principles of bioactive lipid signalling: lessons from sphingolipids. Nat. Rev. Mol. Cell Biol. 9 (2 139 150.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , Issue.2 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 14
    • 27644576503 scopus 로고    scopus 로고
    • Dopamine release in PC12 cells is mediated by Ca (2+)-dependent production of ceramide via sphingomyelin pathway
    • Jeon H. J., Lee D. H., Kang M. S., Lee M. O., Jung K. M., Jung S. Y. Kim D. K. (2005) Dopamine release in PC12 cells is mediated by Ca (2+)-dependent production of ceramide via sphingomyelin pathway. J. Neurochem. 95, 811 820.
    • (2005) J. Neurochem. , vol.95 , pp. 811-820
    • Jeon, H.J.1    Lee, D.H.2    Kang, M.S.3    Lee, M.O.4    Jung, K.M.5    Jung, S.Y.6    Kim, D.K.7
  • 15
    • 0033840568 scopus 로고    scopus 로고
    • Identification of multiple forms of membrane-associated neutral sphingomyelinase in bovine brain
    • Jung S. Y., Suh J. H., Park H. J., Jung K. M., Kim M. Y., Na D. S. Kim D. K. (2000) Identification of multiple forms of membrane-associated neutral sphingomyelinase in bovine brain. J. Neurochem. 75, 1004 1014.
    • (2000) J. Neurochem. , vol.75 , pp. 1004-1014
    • Jung, S.Y.1    Suh, J.H.2    Park, H.J.3    Jung, K.M.4    Kim, M.Y.5    Na, D.S.6    Kim, D.K.7
  • 16
    • 33744953581 scopus 로고    scopus 로고
    • Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein
    • Krut O., Wiegmann K., Kashkar H., Yazdanpanah B. Krönke M. (2006) Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein. J. Biol. Chem. 281 (19 13784.
    • (2006) J. Biol. Chem. , vol.281 , Issue.19 , pp. 13784
    • Krut, O.1    Wiegmann, K.2    Kashkar, H.3    Yazdanpanah, B.4    Krönke, M.5
  • 18
    • 2342570273 scopus 로고    scopus 로고
    • Acid and neutral sphingomyelinases: Roles and mechanisms of regulation
    • Marchesini N. Hannun Y. A. (2004) Acid and neutral sphingomyelinases: roles and mechanisms of regulation. Biochem. Cell Biol. 82, 27 44.
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 27-44
    • Marchesini, N.1    Hannun, Y.A.2
  • 19
    • 0038529730 scopus 로고    scopus 로고
    • Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
    • Marchesini N., Luberto C. Hannun Y. A. (2003) Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism. J. Biol. Chem. 278 (16 13775 13783.
    • (2003) J. Biol. Chem. , vol.278 , Issue.16 , pp. 13775-13783
    • Marchesini, N.1    Luberto, C.2    Hannun, Y.A.3
  • 20
    • 0024543412 scopus 로고
    • Purification and characterization of neutral and acid sphingomyelinases from rat brain
    • Maruyama E. N. Arima M. (1989) Purification and characterization of neutral and acid sphingomyelinases from rat brain. J. Neurochem. 52, 611 618.
    • (1989) J. Neurochem. , vol.52 , pp. 611-618
    • Maruyama, E.N.1    Arima, M.2
  • 22
    • 2342418547 scopus 로고    scopus 로고
    • Ceramide kinase is a mediator of calcium-dependent degranulation in mast cells
    • Mitsutake S., Kim T. J., Inagaki Y., Kato M., Yamashita T. Igarashi Y. (2004) Ceramide kinase is a mediator of calcium-dependent degranulation in mast cells. J. Biol. Chem. 279, 17570 17577.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17570-17577
    • Mitsutake, S.1    Kim, T.J.2    Inagaki, Y.3    Kato, M.4    Yamashita, T.5    Igarashi, Y.6
  • 23
    • 0033214059 scopus 로고    scopus 로고
    • Polarity in intracellular calcium signaling
    • Petersen O. H., Burdakov D. Tepikin A. V. (1999) Polarity in intracellular calcium signaling. Bioessays 21, 851 860.
    • (1999) Bioessays , vol.21 , pp. 851-860
    • Petersen, O.H.1    Burdakov, D.2    Tepikin, A.V.3
  • 24
    • 0034623715 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • Siskind L. J. Colombini M. (2000) Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins. J. Biol. Chem. 275, 38640 38644.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38640-38644
    • Siskind, L.J.1    Colombini, M.2
  • 25
    • 0037178790 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • Siskind L. J., Kolesnick R. N. Colombini M. (2002) Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins. J. Biol. Chem. 277, 26796 26803.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26796-26803
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 26
    • 2942632787 scopus 로고    scopus 로고
    • Activation of NF-kappaB and inhibition of p53-mediated apoptosis by API2/mucosa-associated lymphoid tissue 1 fusions promote oncogenesis
    • Stoffel A., Chaurushiya M., Singh B. Levine A. J. (2004) Activation of NF-kappaB and inhibition of p53-mediated apoptosis by API2/mucosa-associated lymphoid tissue 1 fusions promote oncogenesis. Proc. Natl Acad. Sci. USA 101, 9079 9084.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9079-9084
    • Stoffel, A.1    Chaurushiya, M.2    Singh, B.3    Levine, A.J.4
  • 27
    • 0030473287 scopus 로고    scopus 로고
    • Sphingomyelin break down and cell fate
    • Testi R. (1996) Sphingomyelin break down and cell fate. Trends Biochem. Sci. 21, 468 471.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 468-471
    • Testi, R.1
  • 28
    • 0032584153 scopus 로고    scopus 로고
    • Cloned mammalian neutral sphingomyelinase: Functions in sphingolipid signaling?
    • Tomiuk S., Hofmann K., Nix M., Zumbansen M. Stoffel W. (1998) Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling? Proc. Natl Acad. Sci. USA 95, 3638 3643.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3638-3643
    • Tomiuk, S.1    Hofmann, K.2    Nix, M.3    Zumbansen, M.4    Stoffel, W.5
  • 29
    • 0030614827 scopus 로고    scopus 로고
    • 2+ release from internal stores control exocytosis in pituitary gonadotrophs
    • 2+ release from internal stores control exocytosis in pituitary gonadotrophs. Neuron 18, 121 132.
    • (1997) Neuron , vol.18 , pp. 121-132
    • Tse, F.W.1    Tse, A.2    Hille, B.3    Horstmann, H.4    Almers, W.5
  • 30
    • 0026317132 scopus 로고
    • Inhibition of sphingolipid biosynthesis by fumonisins. Implications for diseases associated with Fusarium moniliforme
    • Wang E., Norred W. P., Bacon C. W., Riley R. T. Merrill A. H. Jr. (1991) Inhibition of sphingolipid biosynthesis by fumonisins. Implications for diseases associated with Fusarium moniliforme. J. Biol. Chem. 266, 14486 14490.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14486-14490
    • Wang, E.1    Norred, W.P.2    Bacon, C.W.3    Riley, R.T.4    Merrill, Jr.A.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.