메뉴 건너뛰기




Volumn 26, Issue 6 A, 2006, Pages 4033-4041

Mechanisms of small globular protein-induced plasma membrane permeability and cytotoxicity in U87-MG human malignant glioblastoma cells

Author keywords

Ca2+ influx; Calcein; DAPI; Glioblastoma; LDH efflux; Permeability; Small globular protein; U87 MG

Indexed keywords

4',6 DIAMIDINO 2 PHENYLINDOLE; CALCEIN; CALCIUM ION; FLUORESCENT DYE; GLOBULAR PROTEIN; LACTATE DEHYDROGENASE;

EID: 33845956454     PISSN: 02507005     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (4)

References (19)
  • 1
    • 0024961641 scopus 로고
    • Structure of the membrane-pore-forming fragment of colicin A
    • Parker MW, Pattus F, Tucker AD and Tsernoglou D: Structure of the membrane-pore-forming fragment of colicin A. Nature 337: 93-96, 1989.
    • (1989) Nature , vol.337 , pp. 93-96
    • Parker, M.W.1    Pattus, F.2    Tucker, A.D.3    Tsernoglou, D.4
  • 2
    • 0030964855 scopus 로고    scopus 로고
    • De novo design, synthesis, and characterization of a pore-forming small globular protein and its insertion into lipid bilayers
    • Lee S, Kiyota T, Kunitake T, Matsumoto E, Yamashita S and Anzai K: De novo design, synthesis, and characterization of a pore-forming small globular protein and its insertion into lipid bilayers. Biochemistry 36: 3782-3791, 1997.
    • (1997) Biochemistry , vol.36 , pp. 3782-3791
    • Lee, S.1    Kiyota, T.2    Kunitake, T.3    Matsumoto, E.4    Yamashita, S.5    Anzai, K.6
  • 3
    • 0034425007 scopus 로고    scopus 로고
    • Study on the packing geometry, stoichiometry, and membrane interaction of three analogs related to a poreforming small globular protein
    • Matsumoto E, Kiyota T, Lee S, Sugihara G, Yamashita S and Meno H: Study on the packing geometry, stoichiometry, and membrane interaction of three analogs related to a poreforming small globular protein. Biopolymers 56: 96-108, 2000.
    • (2000) Biopolymers , vol.56 , pp. 96-108
    • Matsumoto, E.1    Kiyota, T.2    Lee, S.3    Sugihara, G.4    Yamashita, S.5    Meno, H.6
  • 5
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y, Peterson DA, Kimura H and Schubert D: Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J Neurochem 69: 581-593, 1997.
    • (1997) J Neurochem , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 6
    • 0025899234 scopus 로고
    • Use of an aqueous soluble tetrazolium/formazan assay for cell growth assays in culture
    • Cory AH, Owen TC, Barltrop JA and Cory JG: Use of an aqueous soluble tetrazolium/formazan assay for cell growth assays in culture. Cancer Commun 3: 207-212, 1991.
    • (1991) Cancer Commun , vol.3 , pp. 207-212
    • Cory, A.H.1    Owen, T.C.2    Barltrop, J.A.3    Cory, J.G.4
  • 7
    • 0017615868 scopus 로고
    • DIPI and DAPI: Fluorescence banding with only negligible fading
    • Schnedl W, Mikelsaar AV, Breitenbach M and Dann O: DIPI and DAPI: fluorescence banding with only negligible fading. Hum Genet 36: 167-172, 1977.
    • (1977) Hum Genet , vol.36 , pp. 167-172
    • Schnedl, W.1    Mikelsaar, A.V.2    Breitenbach, M.3    Dann, O.4
  • 8
    • 0028036069 scopus 로고
    • Quantitative precision of an automated image cytometric system for the measurement of DNA content and distribution in cells labeled with fluorescent nucleic acid stains
    • Poulin N, Harrison A and Palcic B: Quantitative precision of an automated image cytometric system for the measurement of DNA content and distribution in cells labeled with fluorescent nucleic acid stains. Cytometry 16: 227-235, 1994.
    • (1994) Cytometry , vol.16 , pp. 227-235
    • Poulin, N.1    Harrison, A.2    Palcic, B.3
  • 10
    • 0029168716 scopus 로고    scopus 로고
    • Levesque A, Paquet A and Page M: Measurement of tumor necrosis factor activity by flow cytometry. Cytometry 20: 181-184, 1995.
    • Levesque A, Paquet A and Page M: Measurement of tumor necrosis factor activity by flow cytometry. Cytometry 20: 181-184, 1995.
  • 11
    • 0021038289 scopus 로고
    • An enzyme-release assay for natural cytotoxicity
    • Korzeniewski C and Callewaert DM: An enzyme-release assay for natural cytotoxicity. J Immunol Methods 64: 313-320, 1983.
    • (1983) J Immunol Methods , vol.64 , pp. 313-320
    • Korzeniewski, C.1    Callewaert, D.M.2
  • 12
    • 0023738916 scopus 로고
    • A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity
    • Decker T and Lohmann-Matthes ML: A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity. J Immunol Methods 115: 61-69, 1988.
    • (1988) J Immunol Methods , vol.115 , pp. 61-69
    • Decker, T.1    Lohmann-Matthes, M.L.2
  • 13
    • 3242666765 scopus 로고
    • Ca(2+)-dependent mechanisms of cytotoxicity and programmed cell death
    • Orrenius S, McCabe MJ Jr and Nicotera P: Ca(2+)-dependent mechanisms of cytotoxicity and programmed cell death. Toxicol Lett 64-65 Spec No: 357-364, 1992.
    • (1992) Toxicol Lett , vol.64-65 , Issue.SPEC 357-364
    • Orrenius, S.1    McCabe Jr, M.J.2    Nicotera, P.3
  • 14
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J Biol Chem 260: 3440-3450, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 15
    • 0019972712 scopus 로고
    • Calcium homeostasis in intact lymphocytes: Cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator
    • Tsien RY, Pozzan T and Rink TJ: Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator. J Cell Biol 94: 325-334, 1982.
    • (1982) J Cell Biol , vol.94 , pp. 325-334
    • Tsien, R.Y.1    Pozzan, T.2    Rink, T.J.3
  • 16
    • 0032492542 scopus 로고    scopus 로고
    • Importance of hydrophobic region in amphiphilic structures of alpha-helical peptides for their gene transfer-ability into cells
    • Ohmori N, Niidome T, Kiyota T, Lee S, Sugihara G and Wada A: Importance of hydrophobic region in amphiphilic structures of alpha-helical peptides for their gene transfer-ability into cells. Biochem Biophys Res Commun 245: 259-265, 1998.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 259-265
    • Ohmori, N.1    Niidome, T.2    Kiyota, T.3    Lee, S.4    Sugihara, G.5    Wada, A.6
  • 19
    • 33845942944 scopus 로고    scopus 로고
    • Anti-tumor activity exhibited by a de novo designed Small Globular Protein (SGP): An in vivo experimental design
    • Tsugu H, Onishi H, Fukushima T and Lee S: Anti-tumor activity exhibited by a de novo designed Small Globular Protein (SGP): An in vivo experimental design. Anticancer Res 26: 4043-4046, 2006.
    • (2006) Anticancer Res , vol.26 , pp. 4043-4046
    • Tsugu, H.1    Onishi, H.2    Fukushima, T.3    Lee, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.