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Volumn 1793, Issue 3, 2009, Pages 584-591

PLTP is present in the nucleus, and its nuclear export is CRM1-dependent

Author keywords

Leptomycin B; Neuronal cell; Nuclear localization; Phospholipid transfer protein; PLTP

Indexed keywords

EXPORTIN 1; LEPTOMYCIN B; PHOSPHOLIPID TRANSFER PROTEIN;

EID: 60549116131     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.01.010     Document Type: Article
Times cited : (14)

References (52)
  • 2
    • 33744823777 scopus 로고    scopus 로고
    • Active plasma phospholipid transfer protein is associated with apoA-I but not apoE-containing lipoproteins
    • Cheung M.C., and Albers J.J. Active plasma phospholipid transfer protein is associated with apoA-I but not apoE-containing lipoproteins. J. Lipid Res. 47 (2006) 1315-1321
    • (2006) J. Lipid Res. , vol.47 , pp. 1315-1321
    • Cheung, M.C.1    Albers, J.J.2
  • 3
    • 20344381348 scopus 로고    scopus 로고
    • Reduced CSF PLTP activity in Alzheimer's disease and other neurologic diseases; PLTP induces ApoE secretion in primary human astrocytes in vitro
    • Vuletic S., Peskind E.R., Marcovina S.M., Quinn J.F., Cheung M.C., Kennedy H., Kaye J.A., Jin L.W., and Albers J.J. Reduced CSF PLTP activity in Alzheimer's disease and other neurologic diseases; PLTP induces ApoE secretion in primary human astrocytes in vitro. J. Neurosci. Res. 80 (2005) 406-413
    • (2005) J. Neurosci. Res. , vol.80 , pp. 406-413
    • Vuletic, S.1    Peskind, E.R.2    Marcovina, S.M.3    Quinn, J.F.4    Cheung, M.C.5    Kennedy, H.6    Kaye, J.A.7    Jin, L.W.8    Albers, J.J.9
  • 4
    • 2642554959 scopus 로고    scopus 로고
    • Emerging roles for phospholipid transfer protein in lipid and lipoprotein metabolism
    • Albers J.J., and Cheung M.C. Emerging roles for phospholipid transfer protein in lipid and lipoprotein metabolism. Curr. Opin. Lipidol. 15 (2004) 255-260
    • (2004) Curr. Opin. Lipidol. , vol.15 , pp. 255-260
    • Albers, J.J.1    Cheung, M.C.2
  • 5
    • 0029096429 scopus 로고
    • Functional expression of human and mouse plasma phospholipid transfer protein: effect of recombinant and plasma PLTP on HDL subspecies
    • Albers J.J., Wolfbauer G., Cheung M.C., Day J.R., Ching A.F., Lok S., and Tu A.Y. Functional expression of human and mouse plasma phospholipid transfer protein: effect of recombinant and plasma PLTP on HDL subspecies. Biochim. Biophys. Acta 1258 (1995) 27-34
    • (1995) Biochim. Biophys. Acta , vol.1258 , pp. 27-34
    • Albers, J.J.1    Wolfbauer, G.2    Cheung, M.C.3    Day, J.R.4    Ching, A.F.5    Lok, S.6    Tu, A.Y.7
  • 6
    • 0031003037 scopus 로고    scopus 로고
    • Phospholipid transfer protein mediates transfer of not only phosphatidylcholine but also cholesterol from phosphatidylcholine-cholesterol vesicles to high density lipoproteins
    • Nishida H.I., and Nishida T. Phospholipid transfer protein mediates transfer of not only phosphatidylcholine but also cholesterol from phosphatidylcholine-cholesterol vesicles to high density lipoproteins. J. Biol. Chem. 272 (1997) 6959-6964
    • (1997) J. Biol. Chem. , vol.272 , pp. 6959-6964
    • Nishida, H.I.1    Nishida, T.2
  • 7
    • 0030984536 scopus 로고    scopus 로고
    • Molecular and macromolecular specificity of human plasma phospholipid transfer protein
    • Rao R., Albers J.J., Wolfbauer G., and Pownall H.J. Molecular and macromolecular specificity of human plasma phospholipid transfer protein. Biochemistry 36 (1997) 3645-3653
    • (1997) Biochemistry , vol.36 , pp. 3645-3653
    • Rao, R.1    Albers, J.J.2    Wolfbauer, G.3    Pownall, H.J.4
  • 8
    • 0028795065 scopus 로고
    • Human plasma phospholipid transfer protein accelerates exchange/transfer of alpha-tocopherol between lipoproteins and cells
    • Kostner G.M., Oettl M., Jauhiainen M., Ehnholm C., Esterbauer H., and Dieplinger H. Human plasma phospholipid transfer protein accelerates exchange/transfer of alpha-tocopherol between lipoproteins and cells. Biochem. J. 305 (1995) 659-667
    • (1995) Biochem. J. , vol.305 , pp. 659-667
    • Kostner, G.M.1    Oettl, M.2    Jauhiainen, M.3    Ehnholm, C.4    Esterbauer, H.5    Dieplinger, H.6
  • 10
    • 0033996833 scopus 로고    scopus 로고
    • Phospholipid transfer protein gene knockout mice have low high density lipoprotein levels, due to hypercatabolism, and accumulate apoA-IV-rich lamellar lipoproteins
    • Qin S., Kawano K., Bruce C., Lin M., Bisgaier C., Tall A.R., and Jiang X.C. Phospholipid transfer protein gene knockout mice have low high density lipoprotein levels, due to hypercatabolism, and accumulate apoA-IV-rich lamellar lipoproteins. J. Lipid Res. 41 (2000) 269-276
    • (2000) J. Lipid Res. , vol.41 , pp. 269-276
    • Qin, S.1    Kawano, K.2    Bruce, C.3    Lin, M.4    Bisgaier, C.5    Tall, A.R.6    Jiang, X.C.7
  • 12
    • 0142074257 scopus 로고    scopus 로고
    • Widespread distribution of PLTP in human CNS: evidence for PLTP synthesis by glia and neurons, and increased levels in Alzheimer's disease
    • Vuletic S., Jin L.W., Marcovina S.M., Peskind E.R., Moller T., and Albers J.J. Widespread distribution of PLTP in human CNS: evidence for PLTP synthesis by glia and neurons, and increased levels in Alzheimer's disease. J. Lipid Res. 44 (2003) 1113-1123
    • (2003) J. Lipid Res. , vol.44 , pp. 1113-1123
    • Vuletic, S.1    Jin, L.W.2    Marcovina, S.M.3    Peskind, E.R.4    Moller, T.5    Albers, J.J.6
  • 13
    • 0034742659 scopus 로고    scopus 로고
    • Phospholipase A2 mediates ischemic injury in the hippocampus: a regional difference of neuronal vulnerability
    • Arai K., Ikegaya Y., Nakatani Y., Kudo I., Nishiyama N., and Matsuki N. Phospholipase A2 mediates ischemic injury in the hippocampus: a regional difference of neuronal vulnerability. Eur. J. Neurosci. 13 (2001) 2319-2323
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 2319-2323
    • Arai, K.1    Ikegaya, Y.2    Nakatani, Y.3    Kudo, I.4    Nishiyama, N.5    Matsuki, N.6
  • 14
    • 33745400092 scopus 로고    scopus 로고
    • Plasma phospholipid transfer protein fused with green fluorescent protein is secreted by HepG2 cells and displays phosphatidylcholine transfer activity
    • Siggins S., Ehnholm C., Jauhiainen M., and Olkkonen V.M. Plasma phospholipid transfer protein fused with green fluorescent protein is secreted by HepG2 cells and displays phosphatidylcholine transfer activity. Biochem. Cell Biol. 84 (2006) 117-125
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 117-125
    • Siggins, S.1    Ehnholm, C.2    Jauhiainen, M.3    Olkkonen, V.M.4
  • 15
    • 0030604033 scopus 로고    scopus 로고
    • Plasma phospholipid mass transfer rate: relationship to plasma phospholipid and cholesteryl ester transfer activities and lipid parameters
    • Cheung M.C., Wolfbauer G., and Albers J.J. Plasma phospholipid mass transfer rate: relationship to plasma phospholipid and cholesteryl ester transfer activities and lipid parameters. Biochim. Biophys. Acta 1303 (1996) 103-110
    • (1996) Biochim. Biophys. Acta , vol.1303 , pp. 103-110
    • Cheung, M.C.1    Wolfbauer, G.2    Albers, J.J.3
  • 16
    • 60549106823 scopus 로고    scopus 로고
    • Human plasma transfer protein specific activity is correlated with HDL size; implications for lipoprotein physiology
    • In Pressdoi:10.1016/j.bbalip.2008.12.010
    • M.C. Cheung, G. Wolfbauer, H. Deguchi, J.A. Fernandez, J.H. Griffin, J.J. Albers, Human plasma transfer protein specific activity is correlated with HDL size; implications for lipoprotein physiology, Biochim. Biophys. Acta (In Press)doi:10.1016/j.bbalip.2008.12.010.
    • Biochim. Biophys. Acta
    • Cheung, M.C.1    Wolfbauer, G.2    Deguchi, H.3    Fernandez, J.A.4    Griffin, J.H.5    Albers, J.J.6
  • 17
    • 0028834428 scopus 로고
    • Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M., and Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83 (1995) 683-692
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 19
    • 0037455715 scopus 로고    scopus 로고
    • An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity
    • Xiao Z., Latek R., and Lodish H.F. An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity. Oncogene 22 (2003) 1057-1069
    • (2003) Oncogene , vol.22 , pp. 1057-1069
    • Xiao, Z.1    Latek, R.2    Lodish, H.F.3
  • 20
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: definition, function and interaction with importin α
    • Lange A., Mills R.E., Lange C.J., Stewart M., Devine S.E., and Corbett A.H. Classical nuclear localization signals: definition, function and interaction with importin α. J. Biol. Chem. 282 (2005) 5101-5105
    • (2005) J. Biol. Chem. , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5    Corbett, A.H.6
  • 21
    • 33947726050 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export: to the pore and beyond
    • Hutten S., and Kehlenbach R.H. CRM1-mediated nuclear export: to the pore and beyond. Trends Cell Biol. 17 (2007) 193-201
    • (2007) Trends Cell Biol. , vol.17 , pp. 193-201
    • Hutten, S.1    Kehlenbach, R.H.2
  • 22
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M., and Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90 (1997) 1051-1060
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 23
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • Nishi K., Yoshida M., Fujiwara D., Nishikawa M., Horinouchi S., and Beppu T. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J. Biol. Chem. 269 (1994) 6320-6324
    • (1994) J. Biol. Chem. , vol.269 , pp. 6320-6324
    • Nishi, K.1    Yoshida, M.2    Fujiwara, D.3    Nishikawa, M.4    Horinouchi, S.5    Beppu, T.6
  • 24
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B., Bachelerie F., and Dargemont C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278 (1997) 141-144
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 25
    • 52049108218 scopus 로고    scopus 로고
    • Identification and characterization of a general nuclear translocation signal in signaling proteins
    • Chuderland D., Konson A., and Seger R. Identification and characterization of a general nuclear translocation signal in signaling proteins. Mol. Cell 31 (2008) 850-861
    • (2008) Mol. Cell , vol.31 , pp. 850-861
    • Chuderland, D.1    Konson, A.2    Seger, R.3
  • 26
    • 38949088891 scopus 로고    scopus 로고
    • Analysis of apolipoprotein E nuclear localization using green fluorescent protein and biotinylation approaches
    • Kim W.S., Elliot D.A., Kockx M., Kritharides L., Rye K.A., Jans D.A., and Garner B. Analysis of apolipoprotein E nuclear localization using green fluorescent protein and biotinylation approaches. Biochem. J. 409 (2008) 701-709
    • (2008) Biochem. J. , vol.409 , pp. 701-709
    • Kim, W.S.1    Elliot, D.A.2    Kockx, M.3    Kritharides, L.4    Rye, K.A.5    Jans, D.A.6    Garner, B.7
  • 27
    • 34249668383 scopus 로고    scopus 로고
    • Modulation of apolipoprotein D expression and translocation under specific stress conditions
    • Do Carmo S., Levros L.-C., and Rassart E. Modulation of apolipoprotein D expression and translocation under specific stress conditions. Biochim. Biophys. Acta, Mol. Cell Res. 1773 (2007) 954-969
    • (2007) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1773 , pp. 954-969
    • Do Carmo, S.1    Levros, L.-C.2    Rassart, E.3
  • 28
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B., Ye Y., and Rapoport T.A. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev., Mol. Cell Biol. 3 (2002) 246-255
    • (2002) Nat. Rev., Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 29
    • 0038029881 scopus 로고    scopus 로고
    • ER quality control can lead to retrograte transport from the ER lumen to the cytosol and the nucleoplasm in plants
    • Brandizzi F., Hanton S., DaSilva L.L., Boevink P., Evans D., Oparka K., Denecke J., and Hawes C. ER quality control can lead to retrograte transport from the ER lumen to the cytosol and the nucleoplasm in plants. Plant J. 34 (2003) 269-281
    • (2003) Plant J. , vol.34 , pp. 269-281
    • Brandizzi, F.1    Hanton, S.2    DaSilva, L.L.3    Boevink, P.4    Evans, D.5    Oparka, K.6    Denecke, J.7    Hawes, C.8
  • 30
    • 0037377217 scopus 로고    scopus 로고
    • Nuclear localization and possible functions of receptor tyrosine kinases
    • Carpenter G. Nuclear localization and possible functions of receptor tyrosine kinases. Curr. Opin. Cell Biol. 15 (2003) 143-148
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 143-148
    • Carpenter, G.1
  • 31
    • 4644247974 scopus 로고    scopus 로고
    • Trafficking and signaling pathways of nuclear localizing protein ligands and their receptors
    • Johnson H.M., Subramaniam P.S., Olsnes S., and Jans D.A. Trafficking and signaling pathways of nuclear localizing protein ligands and their receptors. BioEssays 26 (2004) 993-1004
    • (2004) BioEssays , vol.26 , pp. 993-1004
    • Johnson, H.M.1    Subramaniam, P.S.2    Olsnes, S.3    Jans, D.A.4
  • 32
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • Wang Q., Lianyun L., and Yihong Y. Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J. Cell Biol. 174 (2006) 963-971
    • (2006) J. Cell Biol. , vol.174 , pp. 963-971
    • Wang, Q.1    Lianyun, L.2    Yihong, Y.3
  • 33
    • 33947118714 scopus 로고    scopus 로고
    • Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression
    • Liao H.-J., and Carpenter G. Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression. Mol. Biol. Cell 18 (2007) 1064-1072
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1064-1072
    • Liao, H.-J.1    Carpenter, G.2
  • 34
    • 33947240257 scopus 로고    scopus 로고
    • Dual localization: proteins in extracellular and intracellular compartments
    • Arnoys E.J., and Wang J.L. Dual localization: proteins in extracellular and intracellular compartments. Acta Histochem. 109 (2007) 89-110
    • (2007) Acta Histochem. , vol.109 , pp. 89-110
    • Arnoys, E.J.1    Wang, J.L.2
  • 35
  • 36
    • 9444223350 scopus 로고    scopus 로고
    • The role of intranuclear lipids
    • Albi E., and Viola Magni M.P. The role of intranuclear lipids. Biol. Cell 96 (2004) 657-667
    • (2004) Biol. Cell , vol.96 , pp. 657-667
    • Albi, E.1    Viola Magni, M.P.2
  • 37
    • 31544437436 scopus 로고    scopus 로고
    • Dynamic lipidomics of the nucleus
    • Hunt A.N. Dynamic lipidomics of the nucleus. J. Cell. Biochem. 97 (2006) 244-251
    • (2006) J. Cell. Biochem. , vol.97 , pp. 244-251
    • Hunt, A.N.1
  • 38
    • 0000587295 scopus 로고
    • Evidence for lipid material in chromosomes
    • La Cour L.F., Chayen J., and Gahan P.B. Evidence for lipid material in chromosomes. Exp. Cell Res. 14 (1958) 469-485
    • (1958) Exp. Cell Res. , vol.14 , pp. 469-485
    • La Cour, L.F.1    Chayen, J.2    Gahan, P.B.3
  • 39
    • 0001473476 scopus 로고
    • Histochemical evidence for the presence of lipids on the chromosomes of animal cells
    • Gahan P.B. Histochemical evidence for the presence of lipids on the chromosomes of animal cells. Exp. Cell Res. 39 (1965) 136-144
    • (1965) Exp. Cell Res. , vol.39 , pp. 136-144
    • Gahan, P.B.1
  • 40
    • 0016712109 scopus 로고
    • Some biochemical characteristics of rat liver and Morris hepatoma nuclei and nuclear membranes
    • Spangler M., Coetzee M.L., Katlyl S.L., Morris H.P., and Ove P. Some biochemical characteristics of rat liver and Morris hepatoma nuclei and nuclear membranes. Cancer Res. 35 (1975) 3145
    • (1975) Cancer Res. , vol.35 , pp. 3145
    • Spangler, M.1    Coetzee, M.L.2    Katlyl, S.L.3    Morris, H.P.4    Ove, P.5
  • 41
    • 0020565971 scopus 로고
    • Membrane lipids of hepatic tissue II. Phospholipids from subcellular fractions of liver and hepatoma 7288CTC
    • Upreti G.C., De Autmno R.J., and Wood R. Membrane lipids of hepatic tissue II. Phospholipids from subcellular fractions of liver and hepatoma 7288CTC. J. Natl. Cancer Inst. 70 (1983) 567-573
    • (1983) J. Natl. Cancer Inst. , vol.70 , pp. 567-573
    • Upreti, G.C.1    De Autmno, R.J.2    Wood, R.3
  • 42
    • 0023494366 scopus 로고
    • Rat liver nuclear lipids. Composition and biosynthesis
    • Song M., and Rebel G. Rat liver nuclear lipids. Composition and biosynthesis. Basic Appl. Histochem. 31 (1987) 377-387
    • (1987) Basic Appl. Histochem. , vol.31 , pp. 377-387
    • Song, M.1    Rebel, G.2
  • 43
    • 0036189969 scopus 로고    scopus 로고
    • The presence and the role of chromatin cholesterol in rat liver regeneration
    • Albi E., and Viola Magni M.P. The presence and the role of chromatin cholesterol in rat liver regeneration. J. Hepatol. 36 (2002) 395-400
    • (2002) J. Hepatol. , vol.36 , pp. 395-400
    • Albi, E.1    Viola Magni, M.P.2
  • 44
    • 0013842227 scopus 로고
    • Composition and metabolism of lipids within repressed and active chromatin in interphase lymphocytes
    • Rose H.G., and Frenster J.H. Composition and metabolism of lipids within repressed and active chromatin in interphase lymphocytes. Biochim. Biophys. Acta 106 (1965) 577-591
    • (1965) Biochim. Biophys. Acta , vol.106 , pp. 577-591
    • Rose, H.G.1    Frenster, J.H.2
  • 47
    • 0019157337 scopus 로고
    • Subcellular localization of alpha-tocopherol and its effect on RNA synthesis in perfused rabbit heart
    • Guarnieri C., Flamigni F., and Caldarera C.R. Subcellular localization of alpha-tocopherol and its effect on RNA synthesis in perfused rabbit heart. Ital. J. Biochem. 29 (1980) 176-184
    • (1980) Ital. J. Biochem. , vol.29 , pp. 176-184
    • Guarnieri, C.1    Flamigni, F.2    Caldarera, C.R.3
  • 49
    • 45549094777 scopus 로고    scopus 로고
    • Indirect genomic effects on survival from gene expression data
    • Ferkingstad E., Frigessi A., and Lyng H. Indirect genomic effects on survival from gene expression data. Genome Biol. 9 (2008) R58-R72
    • (2008) Genome Biol. , vol.9
    • Ferkingstad, E.1    Frigessi, A.2    Lyng, H.3
  • 52
    • 1642279609 scopus 로고    scopus 로고
    • Genome-wide analysis of molecular changes in IL-12-induced control of mammary carcinoma via IFN-γ-independent mechanisms
    • Shi X., Cao S., Kitsuhashi M., Xiang Z., and Ma X. Genome-wide analysis of molecular changes in IL-12-induced control of mammary carcinoma via IFN-γ-independent mechanisms. J. Immunol. 172 (2004) 4111-4122
    • (2004) J. Immunol. , vol.172 , pp. 4111-4122
    • Shi, X.1    Cao, S.2    Kitsuhashi, M.3    Xiang, Z.4    Ma, X.5


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