메뉴 건너뛰기




Volumn 25, Issue 11, 2000, Pages 530-534

Multidrug resistance: A role for cholesterol efflux pathways?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARRIER PROTEIN; CAVEOLIN; CELL SURFACE PROTEIN; CHOLESTEROL; CYTOTOXIC AGENT;

EID: 0034327486     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01668-6     Document Type: Review
Times cited : (65)

References (57)
  • 1
    • 0027474456 scopus 로고
    • How cancer cells evade chemotherapy: Sixteenth Richard and Hinda Rosenthal Foundation Award Lecture
    • (1993) Cancer Res. , vol.53 , pp. 747-754
    • Gottesman, M.M.1
  • 4
    • 0025913555 scopus 로고
    • Transfection with protein kinase C alpha confers increased multidrug resistance to MCF-7 cells expressing P-glycoprotein
    • (1991) Cancer Commun. , vol.3 , pp. 181-189
    • Yu, G.1
  • 5
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 9
    • 0025142335 scopus 로고
    • Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane
    • (1990) J. Biol. Chem. , vol.265 , pp. 1919-1923
    • Urbani, L.1    Simoni, R.D.2
  • 11
    • 0030459196 scopus 로고    scopus 로고
    • Intracellular transport of low density lipoprotein derived free cholesterol begins at clathrin-coated pits and terminates at cell surface caveolae
    • (1996) Biochemistry , vol.35 , pp. 14932-14938
    • Fielding, P.E.1    Fielding, C.J.2
  • 12
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • (1996) J. Biol. Chem. , vol.271 , pp. 29427-29435
    • Smart, E.J.1
  • 13
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking
    • (1998) J. Biol. Chem. , vol.273 , pp. 6525-6532
    • Uittenbogaard, A.1
  • 19
    • 0030027901 scopus 로고    scopus 로고
    • Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes
    • (1996) J. Biol. Chem. , vol.271 , pp. 568-573
    • Li, S.1
  • 20
    • 0030591426 scopus 로고    scopus 로고
    • Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol
    • (1996) FEBS Lett. , vol.388 , pp. 143-149
    • Monier, S.1
  • 21
    • 0033596725 scopus 로고    scopus 로고
    • Intracellular cholesterol transport in synchronized human skin fibroblasts
    • (1999) Biochemistry , vol.38 , pp. 2506-2513
    • Fielding, C.J.1
  • 22
    • 0033145517 scopus 로고    scopus 로고
    • Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains
    • (1999) Nat. Cell Biol. , vol.1 , pp. 98-105
    • Roy, S.1
  • 23
    • 0032842826 scopus 로고    scopus 로고
    • Co-expression of scavenger receptor-BI and caveolin-1 is associated with enhanced selective cholesteryl ester uptake in THP-1 macrophages
    • (1999) J. Lipid Res. , vol.40 , pp. 1647-1654
    • Matveev, S.1
  • 25
    • 0030982565 scopus 로고    scopus 로고
    • Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10693-10698
    • Bist, A.1
  • 26
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • (1993) EMBO J. , vol.12 , pp. 1597-1605
    • Dupree, P.1
  • 27
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1
  • 28
    • 0030997431 scopus 로고    scopus 로고
    • Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae
    • (1997) J. Biol. Chem. , vol.272 , pp. 13242-13249
    • Babitt, J.1
  • 29
    • 0001137203 scopus 로고    scopus 로고
    • The class B, type I scavenger receptor promotes the selective uptake of high density lipoprotein cholesterol ethers into caveolae
    • (1999) J. Biol. Chem. , vol.274 , pp. 12043-12048
    • Graf, G.A.1
  • 31
    • 0031872767 scopus 로고    scopus 로고
    • Elevated expression of caveolin is associated with prostate and breast cancer
    • (1998) Clin. Cancer Res. , vol.4 , pp. 1873-1880
    • Yang, G.1
  • 33
    • 0032546319 scopus 로고    scopus 로고
    • Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells
    • (1998) Oncogene , vol.16 , pp. 1391-1397
    • Lee, S.W.1
  • 35
    • 0030960332 scopus 로고    scopus 로고
    • Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth
    • (1997) J. Biol. Chem. , vol.272 , pp. 16374-16381
    • Engelman, J.A.1
  • 36
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • (1998) EMBO J. , vol.17 , pp. 6633-6648
    • Galbiati, F.1
  • 37
    • 0032484149 scopus 로고    scopus 로고
    • Up-regulation of caveolae and caveolar constituents in multidrug-resistant cancer cells
    • (1998) J. Biol. Chem. , vol.273 , pp. 32380-32383
    • Lavie, Y.1
  • 38
    • 0031763007 scopus 로고    scopus 로고
    • Upregulation of caveolin-1 and caveolae organelles in Taxol-resistant A549 cells
    • (1998) FEBS Lett. , vol.439 , pp. 368-372
    • Yang, C.-P.H.1
  • 39
    • 0029761340 scopus 로고    scopus 로고
    • Accumulation of glucosylceramides in multidrug-resistant cancer cells
    • (1996) J. Biol. Chem. , vol.271 , pp. 19530-19536
    • Lavie, Y.1
  • 40
    • 0032509356 scopus 로고    scopus 로고
    • Separation of 'glycosphingolipid signaling domain' from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling
    • (1998) J. Biol. Chem. , vol.273 , pp. 33766-33773
    • Iwabuchi, K.1
  • 41
    • 0032910932 scopus 로고    scopus 로고
    • Correlation between cholesterol esterification, MDR1 gene expression and rate of cell proliferation in CEM and MOLT4 cell lines
    • (1999) Cell Prolif. , vol.32 , pp. 49-61
    • Batetta, B.1
  • 42
    • 0027179609 scopus 로고
    • Cytoplasmic membrane cholesterol and doxorubicin cytotoxicity in drug-sensitive and multidrug-resistant human ovarian cancer cells
    • (1993) Oncol. Res. , vol.5 , pp. 75-82
    • Mazzoni, A.1    Trave, F.2
  • 43
    • 0033963650 scopus 로고    scopus 로고
    • P-glycoprotein is localized in caveolae in resistant cells and in brain capillaries
    • (2000) FEBS Lett. , vol.466 , pp. 219-224
    • Demeule, M.1
  • 45
    • 9344255443 scopus 로고    scopus 로고
    • Multidrug resistance and malignancy in human osteosarcoma
    • (1996) Cancer Res. , vol.56 , pp. 2434-2439
    • Scotlandi, K.1
  • 46
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • (2000) EMBO J. , vol.19 , pp. 892-901
    • Schutz, G.J.1
  • 50
    • 0031013536 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoprotein in cholesterol esterification
    • (1997) J. Biol. Chem. , vol.272 , pp. 1026-1031
    • Debry, P.1
  • 52
    • 0033548572 scopus 로고    scopus 로고
    • Multidrug resistance (MDR1) P-glycoprotein enhances esterification of plasma membrane cholesterol
    • (1999) J. Biol. Chem. , vol.274 , pp. 6979-6991
    • Luker, G.D.1
  • 53
    • 0029558068 scopus 로고
    • Clinical drug resistance: The role of factors other than P-glycoprotein
    • (1995) Am. J. Med. , vol.99
    • Kaye, S.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.