메뉴 건너뛰기




Volumn 27, Issue 11, 2002, Pages 1269-1277

Myelin proteolipid protein-induced aggregation of lipid vesicles: Efficacy of the various molecular species

Author keywords

Adhesion; Lipid vesicle; Myelin; Proteolipid protein

Indexed keywords

CHOLESTEROL; ORGANIC SOLVENT; PHOSPHATIDYLCHOLINE; PROTEOLIPID PROTEIN; TRYPSIN;

EID: 0036866795     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021659313213     Document Type: Article
Times cited : (7)

References (37)
  • 1
    • 0029127508 scopus 로고
    • Adhesive properties of proteolipid protein are responsible for the compaction of CNS myelin sheaths
    • Boison, D., Bussow, H., D'Urso, D., Muller, H., and Stoffel, W. 1995. Adhesive properties of proteolipid protein are responsible for the compaction of CNS myelin sheaths. J. Neurosci. 15:5502-5513.
    • (1995) J. Neurosci. , vol.15 , pp. 5502-5513
    • Boison, D.1    Bussow, H.2    D'Urso, D.3    Muller, H.4    Stoffel, W.5
  • 2
    • 0029747137 scopus 로고    scopus 로고
    • Myelin structure in proteolipid protein (PLP)-null mouse spinal cord
    • Rosenbluth, J., Stoffel, W., and Schiff, R. 1996. Myelin structure in proteolipid protein (PLP)-null mouse spinal cord. J. Comp. Neurol. 371:336-344.
    • (1996) J. Comp. Neurol. , vol.371 , pp. 336-344
    • Rosenbluth, J.1    Stoffel, W.2    Schiff, R.3
  • 4
    • 0035118156 scopus 로고    scopus 로고
    • Chemical deacylation reduces the adhesive properties of proteolipid protein and leads to decompaction of the myelin sheath
    • Bizzozero, O. A., Bixler, H. A., Davis, J., Espinosa, A., and Messier, A. M. 2001. Chemical deacylation reduces the adhesive properties of proteolipid protein and leads to decompaction of the myelin sheath. J. Neurochem. 76:1129-1141.
    • (2001) J. Neurochem. , vol.76 , pp. 1129-1141
    • Bizzozero, O.A.1    Bixler, H.A.2    Davis, J.3    Espinosa, A.4    Messier, A.M.5
  • 5
    • 0023389399 scopus 로고
    • Splice site selection in the proteolipid protein (PLP) gene transcript and the primary structure of the DM-20 protein of CNS myelin
    • Nave, K., Lai, C., Bloom, F., and Milner, R. 1987. Splice site selection in the proteolipid protein (PLP) gene transcript and the primary structure of the DM-20 protein of CNS myelin. Proc. Natl. Acad. Sci. USA 84:5665-5669.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5665-5669
    • Nave, K.1    Lai, C.2    Bloom, F.3    Milner, R.4
  • 6
    • 0023549849 scopus 로고
    • Structure and expression of the mouse myelin proteolipid protein gene
    • Macklin, W., Campagnoni, C., Deiminger, P., and Gardinier, M. 1987. Structure and expression of the mouse myelin proteolipid protein gene. J. Neurosci. Res. 18:383-394.
    • (1987) J. Neurosci. Res. , vol.18 , pp. 383-394
    • Macklin, W.1    Campagnoni, C.2    Deiminger, P.3    Gardinier, M.4
  • 7
    • 0036313115 scopus 로고    scopus 로고
    • Mass spectrometric analysis of myelin proteolipids reveals new features of this family of palmitoylated membrane proteins
    • Bizzozero, O. A., Malkoski, S. P., Mobarak, C., Bixler, H. A., and Evans, J. E. 2002. Mass spectrometric analysis of myelin proteolipids reveals new features of this family of palmitoylated membrane proteins. J. Neurochem. 81:636-645.
    • (2002) J. Neurochem. , vol.81 , pp. 636-645
    • Bizzozero, O.A.1    Malkoski, S.P.2    Mobarak, C.3    Bixler, H.A.4    Evans, J.E.5
  • 8
    • 0017398012 scopus 로고
    • Protein-lipid interactions: Recombinants of the proteolipid apoprotein of myelin with dimyristoyllecithin
    • Curatolo, W., Sakura, J. D., Small, D. M., and Shipley, G. G. 1977. Protein-lipid interactions: Recombinants of the proteolipid apoprotein of myelin with dimyristoyllecithin. Biochemistry 16:2313-2319.
    • (1977) Biochemistry , vol.16 , pp. 2313-2319
    • Curatolo, W.1    Sakura, J.D.2    Small, D.M.3    Shipley, G.G.4
  • 9
    • 0021772134 scopus 로고
    • Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance
    • Brophy, P. J., Horvath, L. I., and Marsh, D. 1984. Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance. Biochemistry 23:860-865.
    • (1984) Biochemistry , vol.23 , pp. 860-865
    • Brophy, P.J.1    Horvath, L.I.2    Marsh, D.3
  • 10
    • 0017840420 scopus 로고
    • Structural effects of myelin proteolipid apoprotein on phospholipids: A Raman spectroscopic study
    • Curatolo, W., Verma, S. P., Sakura, J. D., Small, D. M., Shipley, G. G., and Wallach, D. F. 1978. Structural effects of myelin proteolipid apoprotein on phospholipids: A Raman spectroscopic study. Biochemistry. 17:1802-1807.
    • (1978) Biochemistry , vol.17 , pp. 1802-1807
    • Curatolo, W.1    Verma, S.P.2    Sakura, J.D.3    Small, D.M.4    Shipley, G.G.5    Wallach, D.F.6
  • 12
    • 0017799875 scopus 로고
    • Intrinsic fluorescence of a myelin protein and some complexes with phospholipids
    • Cockle, S. A., Epand, R. M., and Moscarello, M. A. 1978. Intrinsic fluorescence of a myelin protein and some complexes with phospholipids. Biochemistry 17:630-637.
    • (1978) Biochemistry , vol.17 , pp. 630-637
    • Cockle, S.A.1    Epand, R.M.2    Moscarello, M.A.3
  • 13
    • 0028338896 scopus 로고
    • Reconstitution of proteolipid protein: Some properties and its role in interlamellar attachment
    • ter Beest, M., Hoekstra, K., Sein, A., and Hoekstra, D. 1994. Reconstitution of proteolipid protein: Some properties and its role in interlamellar attachment. Biochem. J. 300:545-552.
    • (1994) Biochem. J. , vol.300 , pp. 545-552
    • Ter Beest, M.1    Hoekstra, K.2    Sein, A.3    Hoekstra, D.4
  • 14
    • 0032466305 scopus 로고    scopus 로고
    • Human proteolipid protein (PLP) mediates winding and adhesion of phospholipid membranes but prevents their fusion
    • Palaniyar, N., Semotok, J. L., Wood, D. D., Moscarello, M. A., and Harauz, G. 1998. Human proteolipid protein (PLP) mediates winding and adhesion of phospholipid membranes but prevents their fusion. Biochim. Biophys. Acta 1415:85-100.
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 85-100
    • Palaniyar, N.1    Semotok, J.L.2    Wood, D.D.3    Moscarello, M.A.4    Harauz, G.5
  • 16
    • 0000599260 scopus 로고
    • Simple device for preparing ethereal diazomethane without resorting to codistillation
    • Fales, H. M., Jaouni, T. M., and Babashak, J. F. 1973. Simple device for preparing ethereal diazomethane without resorting to codistillation. Anal. Chem. 45:2302-2303.
    • (1973) Anal. Chem. , vol.45 , pp. 2302-2303
    • Fales, H.M.1    Jaouni, T.M.2    Babashak, J.F.3
  • 17
    • 0023028343 scopus 로고
    • Spectroscopic analysis of acylated and deacylated myelin proteolipid protein
    • Bizzozero, O. A. and Less, M. B. 1986. Spectroscopic analysis of acylated and deacylated myelin proteolipid protein. Biochemistry 25:6762-6768.
    • (1986) Biochemistry , vol.25 , pp. 6762-6768
    • Bizzozero, O.A.1    Less, M.B.2
  • 19
    • 0014526593 scopus 로고
    • Carboxymethylation of sulfhydryl groups in proteolipids
    • Lees, M. B., Leston, J. A., and Marfey, P. 1969. Carboxymethylation of sulfhydryl groups in proteolipids. J. Neurochem. 16:1025-1032.
    • (1969) J. Neurochem. , vol.16 , pp. 1025-1032
    • Lees, M.B.1    Leston, J.A.2    Marfey, P.3
  • 20
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5′-Dithiobis(2-nitrobenzoic acid) - A reexamination
    • Riddles, P. W., Blakely, R. L., and Zemer, B. 1979. Ellman's reagent: 5,5′-Dithiobis(2-nitrobenzoic acid) - A reexamination. Anal. Biochem. 94:75-81.
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakely, R.L.2    Zemer, B.3
  • 21
    • 0025218376 scopus 로고
    • Gel-staining techniques
    • Merril, C. R. 1990. Gel-staining techniques. Methods Enzymol. 182:477-488.
    • (1990) Methods Enzymol. , vol.182 , pp. 477-488
    • Merril, C.R.1
  • 22
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D., and Pagano, R. E. 1981. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20:4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 23
    • 0019546646 scopus 로고
    • Aggregation of colloidal particles modeled as a dynamical process
    • Bentz, J. and Nir, S. 1981. Aggregation of colloidal particles modeled as a dynamical process. Proc. Natl. Acad. Sci. USA 78:1634-1637.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1634-1637
    • Bentz, J.1    Nir, S.2
  • 24
    • 0026132370 scopus 로고
    • Major myelin proteolipid: The 4-alpha-helix topology
    • Popot, J. L., Phan-Dinh, D., and Dautigny, A. 1991. Major myelin proteolipid: The 4-alpha-helix topology. J. Membr. Biol. 120:233-246.
    • (1991) J. Membr. Biol. , vol.120 , pp. 233-246
    • Popot, J.L.1    Phan-Dinh, D.2    Dautigny, A.3
  • 25
    • 0000678622 scopus 로고
    • Structure and acylation of proteolipid protein
    • (Martenson R., ed.) CRC Press. Boca Raton, FL
    • Lees, M. B. and Bizzozero, O. A. 1992. Structure and acylation of proteolipid protein. In: Myelin: Biology and Chemistry (Martenson R., ed.) CRC Press. Boca Raton, FL. pp. 237-255.
    • (1992) Myelin: Biology and Chemistry , pp. 237-255
    • Lees, M.B.1    Bizzozero, O.A.2
  • 26
    • 0026980191 scopus 로고
    • Proteolipid protein (PLP) of CNS myelin: Positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP
    • Weimbs, T. and Stoffel, W. 1992. Proteolipid protein (PLP) of CNS myelin: Positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Biochemistry 31:12289-12296.
    • (1992) Biochemistry , vol.31 , pp. 12289-12296
    • Weimbs, T.1    Stoffel, W.2
  • 27
    • 0029861152 scopus 로고    scopus 로고
    • Myelin proteolipid protein (PLP), but not DM-20, is an inositol hexakisphosphate-binding protein
    • Yamaguchi, Y., Ikenaka, K., Niinobe, M., Yamada, H., and Mikoshiba, K. 1996. Myelin proteolipid protein (PLP), but not DM-20, is an inositol hexakisphosphate-binding protein. J. Biol Chem. 271:27838-27846.
    • (1996) J. Biol Chem. , vol.271 , pp. 27838-27846
    • Yamaguchi, Y.1    Ikenaka, K.2    Niinobe, M.3    Yamada, H.4    Mikoshiba, K.5
  • 28
    • 0024426172 scopus 로고
    • X-ray diffraction analysis of myelin lipid/proteolipid protein multilayers
    • Brown, F. R., Karthigasan, J., Singh, I., and Kirschner, D. A. 1989. X-ray diffraction analysis of myelin lipid/proteolipid protein multilayers. J. Neurosci. Res. 24:192-200.
    • (1989) J. Neurosci. Res. , vol.24 , pp. 192-200
    • Brown, F.R.1    Karthigasan, J.2    Singh, I.3    Kirschner, D.A.4
  • 29
    • 0018452480 scopus 로고
    • Liquid diffraction analysis of the model membrane system. Egg lecithin plus myelin protein (N-2)
    • Brady, G. W., Birnbaum, P., Moscarello, M. A., and Papahadjopoulos, D. 1979. Liquid diffraction analysis of the model membrane system. Egg lecithin plus myelin protein (N-2). Biophys. J. 26:23-42.
    • (1979) Biophys. J. , vol.26 , pp. 23-42
    • Brady, G.W.1    Birnbaum, P.2    Moscarello, M.A.3    Papahadjopoulos, D.4
  • 30
    • 0023043540 scopus 로고
    • The intramembranous domains of lipophilin in phosphatidylcholine vesicles are similar to those in the myelin membrane
    • Kahan, I. and Moscarello, M. A. 1986. The intramembranous domains of lipophilin in phosphatidylcholine vesicles are similar to those in the myelin membrane. Biochim. Biophys. Acta 892:223-226.
    • (1986) Biochim. Biophys. Acta , vol.892 , pp. 223-226
    • Kahan, I.1    Moscarello, M.A.2
  • 31
    • 0025800503 scopus 로고
    • Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol
    • Sankaram, M. B., Brophy, P. J., and Marsh, D. 1991. Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol. Biochemistry 30:5866-5873.
    • (1991) Biochemistry , vol.30 , pp. 5866-5873
    • Sankaram, M.B.1    Brophy, P.J.2    Marsh, D.3
  • 32
    • 0021359687 scopus 로고
    • Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents
    • Smith, R., Cook, J., and Dickens, P. A. 1984. Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents. J. Neurochem. 42:306-313.
    • (1984) J. Neurochem. , vol.42 , pp. 306-313
    • Smith, R.1    Cook, J.2    Dickens, P.A.3
  • 33
    • 0014789914 scopus 로고
    • Rotatory dispersion and circular dichroism of brain proteolipid protein
    • Sherman, G. and Folch-Pi, J. 1970. Rotatory dispersion and circular dichroism of brain proteolipid protein. J. Neurochem. 17:597-605.
    • (1970) J. Neurochem. , vol.17 , pp. 597-605
    • Sherman, G.1    Folch-Pi, J.2
  • 34
    • 0030743093 scopus 로고    scopus 로고
    • Myelin proteolipid DM-20: Evidence for function independent of myelination
    • Nadon, N. L., Miller, S., Draeger, K., and Salvaggio, M. 1997. Myelin proteolipid DM-20: Evidence for function independent of myelination. Int. J. Dev. Neurosci. 15:285-293.
    • (1997) Int. J. Dev. Neurosci. , vol.15 , pp. 285-293
    • Nadon, N.L.1    Miller, S.2    Draeger, K.3    Salvaggio, M.4
  • 35
    • 0034212602 scopus 로고    scopus 로고
    • The evolution of lipophilin genes from invertebrates to tetrapods: DM-20 cannot replace proteolipid protein in CNS myelin
    • Stecca, B., Southwood, C. M., Gragerov, A., Kelley, K. A., Friedrich, V. L., and Gow, A. 2000. The evolution of lipophilin genes from invertebrates to tetrapods: DM-20 cannot replace proteolipid protein in CNS myelin. J. Neurosci. 20:4002-4010.
    • (2000) J. Neurosci. , vol.20 , pp. 4002-4010
    • Stecca, B.1    Southwood, C.M.2    Gragerov, A.3    Kelley, K.A.4    Friedrich, V.L.5    Gow, A.6
  • 36
    • 0025269607 scopus 로고
    • Influence of polar residue deletions on lipid-protein interactions with the myelin proteolipid protein. Spin-label ESR studies with DM-20/lipid recombinants
    • Horvath, L. I., Brophy, P. J., and Marsh, D. 1990. Influence of polar residue deletions on lipid-protein interactions with the myelin proteolipid protein. Spin-label ESR studies with DM-20/lipid recombinants. Biochemistry 29:2635-2638.
    • (1990) Biochemistry , vol.29 , pp. 2635-2638
    • Horvath, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 37
    • 0025123830 scopus 로고
    • Selectivity of lipid-protein interaction with myelin proteolipids PLP and DM-20. A fluorescence anisotropy study
    • Houbre, D., Schindler, P., Trifilieff, E., Luu, B., and Duportail, G. 1990. Selectivity of lipid-protein interaction with myelin proteolipids PLP and DM-20. A fluorescence anisotropy study. Biochim. Biophys. Acta 1029:136-142.
    • (1990) Biochim. Biophys. Acta , vol.1029 , pp. 136-142
    • Houbre, D.1    Schindler, P.2    Trifilieff, E.3    Luu, B.4    Duportail, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.