메뉴 건너뛰기




Volumn 45, Issue 9, 1997, Pages 1197-1205

Crosslinked plasmalemmal cholesterol is sequestered to caveolae: Analysis with a new cytochemical probe

Author keywords

Caveolae; Cholesterol; Electron microscopy; Freeze fracture; Histochemistry; Plasma membrane; toxin

Indexed keywords

AVIDIN; CHOLESTEROL; COLLOIDAL GOLD; DIGITONIN; FILIPIN; FLUORESCEIN; LIPID BINDING PROTEIN; STREPTAVIDIN; TOXIN;

EID: 0030865913     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/002215549704500903     Document Type: Article
Times cited : (61)

References (39)
  • 1
    • 0018771894 scopus 로고
    • Freeze-fracture evidence for the presence of cholesterol in particle-free patches of basal disks and the plasma membrane of retinal rod outer segments of mice and frogs
    • Andrews LD, Cohen AI (1979) Freeze-fracture evidence for the presence of cholesterol in particle-free patches of basal disks and the plasma membrane of retinal rod outer segments of mice and frogs. J Cell Biol 81:215-228
    • (1979) J Cell Biol , vol.81 , pp. 215-228
    • Andrews, L.D.1    Cohen, A.I.2
  • 2
    • 0022862167 scopus 로고
    • How do the polyene macrolide antibiotics affect the cellular membrane properties?
    • Bolard J (1986) How do the polyene macrolide antibiotics affect the cellular membrane properties? Biochim Biophys Acta 864:257-304
    • (1986) Biochim Biophys Acta , vol.864 , pp. 257-304
    • Bolard, J.1
  • 3
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 4
    • 0023473534 scopus 로고
    • Influence of the membrane undercoat on filipin perturbation of the red blood cell membrane
    • Clark MR, Mel S, Lupu F, Friend DS (1987) Influence of the membrane undercoat on filipin perturbation of the red blood cell membrane. Exp Cell Res 171:321-330
    • (1987) Exp Cell Res , vol.171 , pp. 321-330
    • Clark, M.R.1    Mel, S.2    Lupu, F.3    Friend, D.S.4
  • 5
    • 0018713265 scopus 로고
    • Membrane sterol heterogeneity. Freeze-fracture detection with saponins and filipin
    • Elias PM, Friend DS, Goerke J (1979) Membrane sterol heterogeneity. Freeze-fracture detection with saponins and filipin. J Histochem Cytochem 27:1247-1260
    • (1979) J Histochem Cytochem , vol.27 , pp. 1247-1260
    • Elias, P.M.1    Friend, D.S.2    Goerke, J.3
  • 6
    • 0018096805 scopus 로고
    • Freeze-fracture identification of sterol-digitonin complexes in cell and liposome membranes
    • Elias PM, Goerke J, Friend DS (1978) Freeze-fracture identification of sterol-digitonin complexes in cell and liposome membranes. J Cell Biol 78:577-596
    • (1978) J Cell Biol , vol.78 , pp. 577-596
    • Elias, P.M.1    Goerke, J.2    Friend, D.S.3
  • 7
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra AM, Williamson E, Simons K, Parton RG (1994) Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J Biol Chem 269:30745-30748
    • (1994) J Biol Chem , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 8
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are distributed diffusely in untreated cells and sequestered to caveolae only after crosslinking
    • Fujimoto T (1996) GPI-anchored proteins, glycosphingolipids, and sphingomyelin are distributed diffusely in untreated cells and sequestered to caveolae only after crosslinking. J Histochem Cytochem 44:929-941
    • (1996) J Histochem Cytochem , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 9
    • 85036491792 scopus 로고    scopus 로고
    • Analysis of plasmalemmal organization by a new cholesterol probe. Histochemisty and Cytochemistry 1996
    • Saito T, ed. Japan Society of Histochemistry and Cytochemistry
    • Fujimoto T, Aoki T, Hagiwara H, Hayashi M, Ohno-Iwashita Y (1996) Analysis of plasmalemmal organization by a new cholesterol probe. Histochemisty and Cytochemistry 1996. Proc Xth Int Congr Histochem Cytochem. Saito T, ed. Japan Society of Histochemistry and Cytochemistry, 170-171
    • (1996) Proc Xth Int Congr Histochem Cytochem , pp. 170-171
    • Fujimoto, T.1    Aoki, T.2    Hagiwara, H.3    Hayashi, M.4    Ohno-Iwashita, Y.5
  • 10
    • 0028877917 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments
    • Fujimoto T, Miyawaki A, Mikoshiba K (1995) Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments. J Cell Sci 108:7-15
    • (1995) J Cell Sci , vol.108 , pp. 7-15
    • Fujimoto, T.1    Miyawaki, A.2    Mikoshiba, K.3
  • 11
    • 85007786586 scopus 로고
    • Uneven formation of filipin-sterol complexes in frog urinary bladder epithelium
    • Fujimoto T, Ogawa K (1983) Uneven formation of filipin-sterol complexes in frog urinary bladder epithelium. Acta Histochem Cytochem 16:513-521
    • (1983) Acta Histochem Cytochem , vol.16 , pp. 513-521
    • Fujimoto, T.1    Ogawa, K.2
  • 12
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky A, Harris DA (1995) Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J Cell Biol 129:619-627
    • (1995) J Cell Biol , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 13
    • 0019719917 scopus 로고
    • Ultrastructural localization of cholesterol by enzyme histochemistry
    • Jones HM, Miyai K (1981) Ultrastructural localization of cholesterol by enzyme histochemistry. Histochem J 13:1017-1028
    • (1981) Histochem J , vol.13 , pp. 1017-1028
    • Jones, H.M.1    Miyai, K.2
  • 14
    • 0028933450 scopus 로고
    • Guilt by insolubility - Does a protein's detergent insolubility reflect a caveolar location?
    • Kurzchalia TV, Harmann E, Dupree P (1995) Guilt by insolubility - does a protein's detergent insolubility reflect a caveolar location? Trends Cell Biol 5:187-189
    • (1995) Trends Cell Biol , vol.5 , pp. 187-189
    • Kurzchalia, T.V.1    Harmann, E.2    Dupree, P.3
  • 15
    • 0021341798 scopus 로고
    • Cholesterol oxidase susceptibility of the red cell membrane
    • Lange YH, Matthies H, Steck TL (1984) Cholesterol oxidase susceptibility of the red cell membrane. Biochim Biophys Acta 769:551-562
    • (1984) Biochim Biophys Acta , vol.769 , pp. 551-562
    • Lange, Y.H.1    Matthies, H.2    Steck, T.L.3
  • 16
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by crosslinking
    • Mayor S, Rothberg K, Maxfield FR (1994) Sequestration of GPI-anchored proteins in caveolae triggered by crosslinking. Science 264:1948-1951
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.2    Maxfield, F.R.3
  • 17
    • 0020956251 scopus 로고
    • Filipin-cholesterol complexes form in uncoated vesicle membrane derived from coated vesicles during receptor-mediated endocytosis of low density lipoprotein
    • McGookey R, Vassalli R, Anderson RGW (1983) Filipin-cholesterol complexes form in uncoated vesicle membrane derived from coated vesicles during receptor-mediated endocytosis of low density lipoprotein. J Cell Biol 96:1273-1278
    • (1983) J Cell Biol , vol.96 , pp. 1273-1278
    • McGookey, R.1    Vassalli, R.2    Anderson, R.G.W.3
  • 19
    • 0025355631 scopus 로고
    • A modified θ-toxin produced by limited proteolysis and methylation: A probe for the functional study of membrane cholesterol
    • Ohno-Iwashita Y, Iwamoto M, Ando S, Mitsui K, Iwashita S (1990) A modified θ-toxin produced by limited proteolysis and methylation: a probe for the functional study of membrane cholesterol. Biochim Biophys Acta 1023:441-448
    • (1990) Biochim Biophys Acta , vol.1023 , pp. 441-448
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Ando, S.3    Mitsui, K.4    Iwashita, S.5
  • 20
    • 0025880182 scopus 로고
    • A cytolysin, θ-toxin, preferentially binds to membrane cholesterol surrounded by phospholipids with 18-carbon hydrocarbon chains in cholesterol-rich region
    • Ohno-Iwashita Y, Iwamoto M, Mitsui K, Ando S, Iwashita S (1991) A cytolysin, θ-toxin, preferentially binds to membrane cholesterol surrounded by phospholipids with 18-carbon hydrocarbon chains in cholesterol-rich region. J Biochem 110: 369-375
    • (1991) J Biochem , vol.110 , pp. 369-375
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Mitsui, K.3    Ando, S.4    Iwashita, S.5
  • 21
    • 0023783454 scopus 로고
    • Protease-nicked θ-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes
    • Ohno-Iwashita Y, Iwamoto M, Mitsui K, Ando S, Nagai Y (1988) Protease-nicked θ-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes. Eur J Biochem 176:95-101
    • (1988) Eur J Biochem , vol.176 , pp. 95-101
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Mitsui, K.3    Ando, S.4    Nagai, Y.5
  • 22
    • 0023008127 scopus 로고
    • Cold-labile hemolysin produced by limited proteolysis of θ-toxin from Clostridium perfringens
    • Ohno-Iwashita Y, Iwamoto M, Mitsui K, Kawasaki H, Ando S (1986) Cold-labile hemolysin produced by limited proteolysis of θ-toxin from Clostridium perfringens. Biochemistry 25: 6048-6053
    • (1986) Biochemistry , vol.25 , pp. 6048-6053
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Mitsui, K.3    Kawasaki, H.4    Ando, S.5
  • 24
    • 0028138908 scopus 로고
    • Filipin vs enzymatic localization of cholesterol in guinea pig, mink, and mallard duck testicular cells
    • Pelletier R-M, Vitale ML (1994) Filipin vs enzymatic localization of cholesterol in guinea pig, mink, and mallard duck testicular cells. J Histochem Cytochem 42:1539-1554
    • (1994) J Histochem Cytochem , vol.42 , pp. 1539-1554
    • Pelletier, R.-M.1    Vitale, M.L.2
  • 25
    • 0021200252 scopus 로고
    • Label-fracture: A method for high resolution labeling of cell surfaces
    • Pinto da Silva P, Kan FWK (1984) Label-fracture: a method for high resolution labeling of cell surfaces. J Cell Biol 99:1156-1161
    • (1984) J Cell Biol , vol.99 , pp. 1156-1161
    • Pinto Da Silva, P.1    Kan, F.W.K.2
  • 27
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-metyltetrahydrofolate
    • Rothberg K, Ying Y, Kamen BA, Anderson RGW (1990) Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-metyltetrahydrofolate. J Cell Biol 111:2931-2938
    • (1990) J Cell Biol , vol.111 , pp. 2931-2938
    • Rothberg, K.1    Ying, Y.2    Kamen, B.A.3    Anderson, R.G.W.4
  • 28
    • 0022288865 scopus 로고
    • Preparation of apical plasma membranes from cells grown on coverslips. Electron microscopic investigations of the protoplasmic surface
    • Rutter G, Bohn W, Hohenberg H, Mannweiler K (1985) Preparation of apical plasma membranes from cells grown on coverslips. Electron microscopic investigations of the protoplasmic surface. Eur J Cell Biol 39:443-448
    • (1985) Eur J Cell Biol , vol.39 , pp. 443-448
    • Rutter, G.1    Bohn, W.2    Hohenberg, H.3    Mannweiler, K.4
  • 29
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP (1993) Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 122:789-807
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 30
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer JE, Oh P, Pinney E, Allard J (1994) Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J Cell Biol 127:1217-1232
    • (1994) J Cell Biol , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 31
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer JE, McIntosh DP, Dvorak AM, Liu J, Oh P (1995) Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 269:1435-1439
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 32
    • 0013539210 scopus 로고
    • Lipid localization by membrane perturbation: A cautionary tale
    • Severs NJ, Shotton DM, eds. New York, Wiley-Liss
    • Severs NJ (1995) Lipid localization by membrane perturbation: a cautionary tale. In Severs NJ, Shotton DM, eds. Rapid Freezing, Freeze-Fracture, and Deep Etching. New York, Wiley-Liss, 225-234
    • (1995) Rapid Freezing, Freeze-Fracture, and Deep Etching , pp. 225-234
    • Severs, N.J.1
  • 33
    • 0021106131 scopus 로고
    • Failure of filipin to detect cholesterol-rich domains in smooth muscle plasma membrane
    • Severs NJ, Simons HL (1983) Failure of filipin to detect cholesterol-rich domains in smooth muscle plasma membrane. Nature 303:637-638
    • (1983) Nature , vol.303 , pp. 637-638
    • Severs, N.J.1    Simons, H.L.2
  • 34
    • 0019849864 scopus 로고
    • Analysis of membrane structure in the transitional epithelium of the rat urinary bladder. 3. Localization of cholesterol using filipin and digitonin
    • Severs NJ, Warren RC, Barnes SH (1981) Analysis of membrane structure in the transitional epithelium of the rat urinary bladder. 3. Localization of cholesterol using filipin and digitonin. J Ultrastruct Res 77:160-188
    • (1981) J Ultrastruct Res , vol.77 , pp. 160-188
    • Severs, N.J.1    Warren, R.C.2    Barnes, S.H.3
  • 35
    • 0021063738 scopus 로고
    • Rings of membrane sterols surround the openings of vesicles and fenestrae in capillary endothelium
    • Simionescu N, Lupu F, Simionescu M (1983) Rings of membrane sterols surround the openings of vesicles and fenestrae in capillary endothelium. J Cell Biol 97:1592-1600
    • (1983) J Cell Biol , vol.97 , pp. 1592-1600
    • Simionescu, N.1    Lupu, F.2    Simionescu, M.3
  • 36
    • 0022755770 scopus 로고
    • Plasmalemmal vesicles and the effects of sterol-binding agents in rabbit aortic endothelium
    • Simons HL, Severs NJ (1986) Plasmalemmal vesicles and the effects of sterol-binding agents in rabbit aortic endothelium. J Cell Sci 83:141-153
    • (1986) J Cell Sci , vol.83 , pp. 141-153
    • Simons, H.L.1    Severs, N.J.2
  • 37
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart EJ, Ying Y-S, Conrad PA, Anderson RGW (1994) Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J Cell Biol 127:1185-1197
    • (1994) J Cell Biol , vol.127 , pp. 1185-1197
    • Smart, E.J.1    Ying, Y.-S.2    Conrad, P.A.3    Anderson, R.G.W.4
  • 38
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle PL (1985) Cholesterol and the cell membrane. Biochim Biophys Acta 822:267-287
    • (1985) Biochim Biophys Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 39
    • 0019158157 scopus 로고
    • A survey of transformation markers in differentiating epidermal cell lines in culture
    • Yuspa SH, Hawley-Nelson P, Koehler B, Stanley JR (1980) A survey of transformation markers in differentiating epidermal cell lines in culture. Cancer Res 40:4694-4703
    • (1980) Cancer Res , vol.40 , pp. 4694-4703
    • Yuspa, S.H.1    Hawley-Nelson, P.2    Koehler, B.3    Stanley, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.