메뉴 건너뛰기




Volumn 262, Issue 3, 1999, Pages 850-857

Purification and cDNA cloning of a protein derived from Flammulina velutipes that increases the permeability of the intestinal Caco-2 cell monolayer

Author keywords

Amino acid sequence; CDNA cloning; Flammulina velutipes; Intestinal epithelial cells; TEER decreasing protein

Indexed keywords

FLAMMUTOXIN; FUNGAL PROTEIN; LUCIFER YELLOW; UNCLASSIFIED DRUG;

EID: 0033564749     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00440.x     Document Type: Article
Times cited : (27)

References (30)
  • 1
    • 0029167043 scopus 로고
    • Regulation of tight-junction permeability during nutrient absorption across the intestinal epithelium
    • 1. Ballard, S.T., Hunter, J.H. & Taylor, A.E. (1995) Regulation of tight-junction permeability during nutrient absorption across the intestinal epithelium. Annu. Rev. Nutr. 15, 35-55,.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 35-55
    • Ballard, S.T.1    Hunter, J.H.2    Taylor, A.E.3
  • 2
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • 2. Denker, B.M. & Nigam, S.K. (1998) Molecular structure and assembly of the tight junction. Am. J. Physiol. 274, F1-F9.
    • (1998) Am. J. Physiol. , vol.274
    • Denker, B.M.1    Nigam, S.K.2
  • 3
    • 0026752739 scopus 로고
    • Structure, function, and regulation of cellular tight junctions
    • 3. Schneeberger, E.E. & Lynch, R.D. (1992) Structure, function, and regulation of cellular tight junctions. Am. J. Physiol. 262, L647-L661.
    • (1992) Am. J. Physiol. , vol.262
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 4
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • 4. Anderson, J.M. & Van Itallie, C.M. (1995) Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269, G467-G475.
    • (1995) Am. J. Physiol. , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 5
    • 0029074142 scopus 로고
    • Modulation of epithelial permeability by extracellular macromolecules
    • 5. Lewis, S.A., Berg, J.R. & Kleine, T.J. (1995) Modulation of epithelial permeability by extracellular macromolecules. Physiol. Rev. 75, 561-589.
    • (1995) Physiol. Rev. , vol.75 , pp. 561-589
    • Lewis, S.A.1    Berg, J.R.2    Kleine, T.J.3
  • 7
    • 0031021481 scopus 로고    scopus 로고
    • Effect of capsianoside, a diterpene glycoside, on tight-junctional permeability
    • 7. Hashimoto, K., Kawagishi, H., Nakayama, T. & Shimizu, M. (1997) Effect of capsianoside, a diterpene glycoside, on tight-junctional permeability. Biochim. Biophys. Acta 1323, 281-290.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 281-290
    • Hashimoto, K.1    Kawagishi, H.2    Nakayama, T.3    Shimizu, M.4
  • 8
    • 0029383212 scopus 로고
    • Stabilization of the tight junction of the intestinal Caco-2 cell monolayer by milk whey proteins
    • 8. Hashimoto, K., Takeda, K., Nakayama, T. & Shimizu, M. (1995) Stabilization of the tight junction of the intestinal Caco-2 cell monolayer by milk whey proteins. Biosci. Biotech. Biochem. 59, 1951-1952.
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 1951-1952
    • Hashimoto, K.1    Takeda, K.2    Nakayama, T.3    Shimizu, M.4
  • 10
    • 0027830396 scopus 로고
    • Epithelial properties of human intestinal Caco-2 cells cultured in a serum-free medium
    • 10. Hashimoto, K. & Shimizu, M. (1993) Epithelial properties of human intestinal Caco-2 cells cultured in a serum-free medium. Cytotechnology 13, 175-184.
    • (1993) Cytotechnology , vol.13 , pp. 175-184
    • Hashimoto, K.1    Shimizu, M.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 11. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0023785178 scopus 로고
    • Purification of a 31,000-dalton insulin-like growth factor binding protein from human amniotic fluid. Isolation of two forms with different biologic actions
    • 12. Busby, W.H. Jr, Klapper, D.G. & Clemmons, D.R. (1988) Purification of a 31,000-dalton insulin-like growth factor binding protein from human amniotic fluid. Isolation of two forms with different biologic actions. J. Biol. Chem. 263, 14203-14210.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14203-14210
    • Busby W.H., Jr.1    Klapper, D.G.2    Clemmons, D.R.3
  • 13
    • 78651153791 scopus 로고
    • Method and application to human serum proteins
    • 13. Davis, B. (1964) Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 121, 404-427.
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.1
  • 14
    • 0027213003 scopus 로고
    • Phosphorylation of insulin-like growth factor-binding protein-1 increases in human amniotic fluid and decidua from early to late pregnancy
    • 14. Koistinen, R., Angervo, M., Leinonen, P., Hakala, T. & Seppälä, M. (1993) Phosphorylation of insulin-like growth factor-binding protein-1 increases in human amniotic fluid and decidua from early to late pregnancy. Clinica Chimica Acta 215, 189-199.
    • (1993) Clinica Chimica Acta , vol.215 , pp. 189-199
    • Koistinen, R.1    Angervo, M.2    Leinonen, P.3    Hakala, T.4    Seppälä, M.5
  • 15
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • 15. Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 16
    • 0027482224 scopus 로고
    • Freshly isolated cells and cell lines from the intestine as an in vitro model for toxicological studies
    • 16. Zucco, F. (1993) Freshly isolated cells and cell lines from the intestine as an in vitro model for toxicological studies. Toxicol. In Vitro 7, 397-402.
    • (1993) Toxicol. In Vitro , vol.7 , pp. 397-402
    • Zucco, F.1
  • 17
    • 0030748918 scopus 로고    scopus 로고
    • Rapid decrease in transepithelial electrical resistance of human intestinal Caco-2 cell monolayters by cytotoxic membrane perturbents
    • 17. Narai, A., Arai, S. & Shimizu, M. (1997) Rapid decrease in transepithelial electrical resistance of human intestinal Caco-2 cell monolayters by cytotoxic membrane perturbents. Toxicol. In Vitro 11, 347-354.
    • (1997) Toxicol. In Vitro , vol.11 , pp. 347-354
    • Narai, A.1    Arai, S.2    Shimizu, M.3
  • 19
    • 0016777651 scopus 로고
    • Toxicity of the cardiotoxic protein flammutoxin, isolate from edible mushroom Flammulina velutipes
    • 19. Lin, J.-Y., Lin, Y.-J., Chen, C.-C., Wu, H.-L., Shi, G.-Y. & Jeng, T.-W. (1975) Toxicity of the cardiotoxic protein flammutoxin, isolate from edible mushroom Flammulina velutipes. Toxicon 13, 323-331.
    • (1975) Toxicon , vol.13 , pp. 323-331
    • Lin, J.-Y.1    Lin, Y.-J.2    Chen, C.-C.3    Wu, H.-L.4    Shi, G.-Y.5    Jeng, T.-W.6
  • 20
    • 0024593744 scopus 로고
    • Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability
    • 20. Hidalgo, I.J., Raub, T.J. & Borchardt, R.T. (1989) Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 96, 763-749.
    • (1989) Gastroenterology , vol.96 , pp. 763-1749
    • Hidalgo, I.J.1    Raub, T.J.2    Borchardt, R.T.3
  • 21
    • 0032127174 scopus 로고    scopus 로고
    • Assembly of flammutoxin, a cytolytic protein from the edible mushroom Flammulina velutipes, into a pore-forming ring-shaped oligomer on the target cell
    • 21. Tomita, T., Ishikawa, D., Noguchi, T., Katayama, E. & Hashimoto, Y. (1998) Assembly of flammutoxin, a cytolytic protein from the edible mushroom Flammulina velutipes, into a pore-forming ring-shaped oligomer on the target cell. Biochem. J. 333, 129-137.
    • (1998) Biochem. J. , vol.333 , pp. 129-137
    • Tomita, T.1    Ishikawa, D.2    Noguchi, T.3    Katayama, E.4    Hashimoto, Y.5
  • 22
    • 0023464950 scopus 로고
    • Some properties of flammutoxin from the edible mushroom Flammulina velutipes
    • 22. Bernheimer, A.W. & Oppenheim, J.D. (1987) Some properties of flammutoxin from the edible mushroom Flammulina velutipes. Toxicon 25, 1145-1152.
    • (1987) Toxicon , vol.25 , pp. 1145-1152
    • Bernheimer, A.W.1    Oppenheim, J.D.2
  • 23
    • 0030804395 scopus 로고    scopus 로고
    • Pore-forming proteins in pathogenic protozoan parasites
    • 23. Horta, M.F. (1997) Pore-forming proteins in pathogenic protozoan parasites. Trends Microbiol. 5, 363-366.
    • (1997) Trends Microbiol. , vol.5 , pp. 363-366
    • Horta, M.F.1
  • 24
    • 0026483703 scopus 로고
    • Calcium signaling in cell volume regulation
    • 24. McCarty, N.A. & O'Neil, R.G. (1992) Calcium signaling in cell volume regulation. Physiol. Rev. 72, 1037-1061.
    • (1992) Physiol. Rev. , vol.72 , pp. 1037-1061
    • McCarty, N.A.1    O'Neil, R.G.2
  • 25
    • 0022654450 scopus 로고
    • Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores
    • 25. Bhakdi, S., Mackman, N., Nicaud, J.-M. & Holland, I.B. (1986) Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores. Infect. Immun. 52, 63-69,.
    • (1986) Infect. Immun. , vol.52 , pp. 63-69
    • Bhakdi, S.1    Mackman, N.2    Nicaud, J.-M.3    Holland, I.B.4
  • 27
    • 0030796817 scopus 로고    scopus 로고
    • Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: Pore formation and the role of cationic amino acid residues
    • 27. Chen, D., Kini, M. & Yuen, R. & Khoo, H.E. (1997) Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues. Biochem. J. 325, 685-691.
    • (1997) Biochem. J. , vol.325 , pp. 685-691
    • Chen, D.1    Kini, M.2    Yuen, R.3    Khoo, H.E.4
  • 28
    • 0000576265 scopus 로고
    • Pore size distribution analysis of gel substances by size exclusion chromatography
    • 28. Kuga, S. (1981) Pore size distribution analysis of gel substances by size exclusion chromatography. J. Chromatogr. 206, 499-461.
    • (1981) J. Chromatogr. , vol.206 , pp. 499-1461
    • Kuga, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.