메뉴 건너뛰기




Volumn 118, Issue 3, 2005, Pages 278-289

Protein response of insect cells to bioreactor environmental stresses

Author keywords

Anoxia; Bioreactor; Ethanol; Heat shock protein; pH change; Salinity; Shear stress; Stress protein

Indexed keywords

BIOREACTORS; CELLS; ENVIRONMENTAL IMPACT; ETHANOL; INSECT CONTROL; OXYGEN; PH EFFECTS; SHEAR STRESS;

EID: 22544476835     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.05.009     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 0026124852 scopus 로고
    • Microscopic visualization of insect cell-bubble interactions. I. Rising bubbles, air-medium interface, and the foam layer
    • F. Bavarian, L.S. Fan, and J.J. Chalmers Microscopic visualization of insect cell-bubble interactions. I. Rising bubbles, air-medium interface, and the foam layer Biotechnol. Prog. 7 1991 140 150
    • (1991) Biotechnol. Prog. , vol.7 , pp. 140-150
    • Bavarian, F.1    Fan, L.S.2    Chalmers, J.J.3
  • 2
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • J. Becker, and E.A. Craig Heat-shock proteins as molecular chaperones Eur. J. Biochem. 219 1994 11 23
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 4
    • 0026124851 scopus 로고
    • Microscopic visualization of insect cell-bubble interactions. II. the bubble film and bubble rupture
    • J.J. Chalmers, and F. Bavarian Microscopic visualization of insect cell-bubble interactions. II. The bubble film and bubble rupture Biotechnol. Prog. 7 1991 151 158
    • (1991) Biotechnol. Prog. , vol.7 , pp. 151-158
    • Chalmers, J.J.1    Bavarian, F.2
  • 5
    • 0026473369 scopus 로고
    • Cell death in the thin films of bursting bubbles
    • R.S. Cherry, and C.T. Hulle Cell death in the thin films of bursting bubbles Biotechnol. Prog. 8 1992 11 18
    • (1992) Biotechnol. Prog. , vol.8 , pp. 11-18
    • Cherry, R.S.1    Hulle, C.T.2
  • 6
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • J. Ellis Proteins as molecular chaperones Nature 328 1987 378 379
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 7
    • 0027925677 scopus 로고
    • The general concept of molecular chaperones
    • R.J. Ellis The general concept of molecular chaperones Philos. Trans. R. Soc. Lond. B 339 1993 257 261
    • (1993) Philos. Trans. R. Soc. Lond. B , vol.339 , pp. 257-261
    • Ellis, R.J.1
  • 8
    • 33044502888 scopus 로고
    • Intracellular pH response of cells subjected to sublethal hydrodynamic shear stress: Measurement methodology and modeling
    • Abstract No. 180i, Chicago, ILL, USA, November
    • Garapati, B., Mutharasan, R., 1986. Intracellular pH response of cells subjected to sublethal hydrodynamic shear stress: measurement methodology and modeling, Abstract No. 180i, Presented at Annual AIChE Meeting, Chicago, ILL, USA, November, pp. 10-15.
    • (1986) Annual AIChE Meeting , pp. 10-15
    • Garapati, B.1    Mutharasan, R.2
  • 9
    • 0026764943 scopus 로고
    • Cell-bubble interactions: Mechanisms of suspended cell damage
    • M. Garcia-Briones, and J.J. Chalmers Cell-bubble interactions: mechanisms of suspended cell damage Ann. N. Y. Acad. Sci. 665 1992 219 229
    • (1992) Ann. N. Y. Acad. Sci. , vol.665 , pp. 219-229
    • Garcia-Briones, M.1    Chalmers, J.J.2
  • 10
    • 0025486769 scopus 로고
    • Protective effect of methylcellulose and other polymers on insect cells subjected to laminar shear stress
    • S. Goldblum, Y.-K. Bae, W.F. Hink, and J. Chalmers Protective effect of methylcellulose and other polymers on insect cells subjected to laminar shear stress Biotechnol. Prog. 6 1990 383 390
    • (1990) Biotechnol. Prog. , vol.6 , pp. 383-390
    • Goldblum, S.1    Bae, Y.-K.2    Hink, W.F.3    Chalmers, J.4
  • 11
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • J.P. Henrick, and F.-U. Hartl Molecular chaperone functions of heat-shock proteins Annu. Rev. Biochem. 62 1993 349 384
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Henrick, J.P.1    Hartl, F.-U.2
  • 12
    • 0028887686 scopus 로고
    • Induction of stress proteins in anoxic and hyperthermic Spodoptera frugiperda cells
    • W. Hugler, K.C. O'Connor, S.J. Landry, and J.E. Bivins Induction of stress proteins in anoxic and hyperthermic Spodoptera frugiperda cells Cytotechnol 17 1995 91 101
    • (1995) Cytotechnol , vol.17 , pp. 91-101
    • Hugler, W.1    O'Connor, K.C.2    Landry, S.J.3    Bivins, J.E.4
  • 13
    • 0026935588 scopus 로고
    • Heat-shock proteins and stress tolerance in microorganisms
    • S. Lindquist Heat-shock proteins and stress tolerance in microorganisms Curr. Opin. Genet. Dev. 2 1992 748 755
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 748-755
    • Lindquist, S.1
  • 15
    • 0002704281 scopus 로고
    • Cloning and expression of heterologous genes in insect baculovirus vectors
    • A. Prokop R.K. Bajbai C.S. Ho McCraw Hill NY, USA
    • V.A. Luckow Cloning and expression of heterologous genes in insect baculovirus vectors A. Prokop R.K. Bajbai C.S. Ho Recombinant DNA Technology and Applications 1992 McCraw Hill NY, USA 97 152
    • (1992) Recombinant DNA Technology and Applications , pp. 97-152
    • Luckow, V.A.1
  • 16
    • 0001806571 scopus 로고
    • The stress response, function of the proteins and perspectives
    • R.I. Morimoto A. Tissières C. Georgopoulos Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY, USA
    • R.I. Morimoto, A. Tissières, and C. Georgopoulos The stress response, function of the proteins and perspectives R.I. Morimoto A. Tissières C. Georgopoulos Stress Proteins in Biology and Medicine 1990 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY, USA 1 36
    • (1990) Stress Proteins in Biology and Medicine , pp. 1-36
    • Morimoto, R.I.1    Tissières, A.2    Georgopoulos, C.3
  • 17
    • 0025486770 scopus 로고
    • Sparged animal cell bioreactors: Mechanisms of cell damage and pluronic F-68 protection
    • D.W. Murhammer, and C.F. Goochee Sparged animal cell bioreactors: mechanisms of cell damage and pluronic F-68 protection Biotechnol. Prog. 6 1990 391 397
    • (1990) Biotechnol. Prog. , vol.6 , pp. 391-397
    • Murhammer, D.W.1    Goochee, C.F.2
  • 18
    • 85140938701 scopus 로고
    • Inducers of hsp synthesis: Heat shock and chemical stressors
    • L. Nover CRC Press Boca Raton, FL, USA
    • L. Nover Inducers of hsp synthesis: heat shock and chemical stressors L. Nover Heat Shock Response 1991 CRC Press Boca Raton, FL, USA 5 40
    • (1991) Heat Shock Response , pp. 5-40
    • Nover, L.1
  • 20
    • 0342632836 scopus 로고    scopus 로고
    • Evidence of pluronic F-68 direct interaction with insect cells: Impact on shear protection, recombinant protein, and baculovirus production
    • L.A. Palomares, M. Gonzalez, and O.T. Ramirez Evidence of pluronic F-68 direct interaction with insect cells: impact on shear protection, recombinant protein, and baculovirus production Enzyme Microb. Technol. 26 2000 324 331
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 324-331
    • Palomares, L.A.1    Gonzalez, M.2    Ramirez, O.T.3
  • 22
    • 0025513915 scopus 로고
    • The role of the plasma membrane fluidity on the shear sensitivity of hybridomas grown under hydrodynamic stress
    • O.T. Ramirez, and R. Mutharasan The role of the plasma membrane fluidity on the shear sensitivity of hybridomas grown under hydrodynamic stress Biotechnol. Bioeng. 36 1990 911 920
    • (1990) Biotechnol. Bioeng. , vol.36 , pp. 911-920
    • Ramirez, O.T.1    Mutharasan, R.2
  • 23
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • F. Ritossa A new puffing pattern induced by temperature shock and DNP in Drosophila Experientia 18 1962 571 573
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 24
    • 0028276119 scopus 로고
    • How the cell copes with stress and the function of heat shock proteins
    • M.J. Schlesinger How the cell copes with stress and the function of heat shock proteins Pediatr. Res. 36 1994 1 6
    • (1994) Pediatr. Res. , vol.36 , pp. 1-6
    • Schlesinger, M.J.1
  • 25
    • 0022536553 scopus 로고
    • Stress protein systems of mammalian cells
    • J.R. Subjeck, and T.-T. Shyy Stress protein systems of mammalian cells Am. J. Physiol. 250 1986 C1 C17
    • (1986) Am. J. Physiol. , vol.250
    • Subjeck, J.R.1    Shyy, T.-T.2
  • 26
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • A. Tissières, H.K. Mitchell, and U.M. Tracy Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs J. Mol. Biol. 85 1974 389 398
    • (1974) J. Mol. Biol. , vol.85 , pp. 389-398
    • Tissières, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 27
    • 0342815688 scopus 로고
    • Bubble-column design for growth of fragile insect cells
    • J. Tramper, D. Smit, J. Straatman, and J.M. Valk Bubble-column design for growth of fragile insect cells Bioprocess Eng. 3 1988 37 41
    • (1988) Bioprocess Eng. , vol.3 , pp. 37-41
    • Tramper, J.1    Smit, D.2    Straatman, J.3    Valk, J.M.4
  • 29
    • 0028764598 scopus 로고
    • Quantification of damage to suspended insect cells as a result of bubble rupture
    • K. Trinh, M. Garcia-Briones, F. Hink, and J.J. Chalmers Quantification of damage to suspended insect cells as a result of bubble rupture Biotechnol. Bioeng. 43 1994 37 45
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 37-45
    • Trinh, K.1    Garcia-Briones, M.2    Hink, F.3    Chalmers, J.J.4
  • 30
    • 0017475358 scopus 로고
    • The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae)
    • J.L. Vaughn, R.H. Goodwin, G.J. Tompkins, and P. McCawley The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae) In Vitro 13 1977 213 217
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Tompkins, G.J.3    McCawley, P.4
  • 31
    • 0001860842 scopus 로고
    • The mammalian stress response: Cell physiology and biochemistry of stress proteins
    • R.I. Morimoto A. Tissières C. Georgepoulos Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY, USA
    • W.J. Welch The mammalian stress response: cell physiology and biochemistry of stress proteins R.I. Morimoto A. Tissières C. Georgepoulos Stress Proteins in Biology and Medicine 1990 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY, USA 223 277
    • (1990) Stress Proteins in Biology and Medicine , pp. 223-277
    • Welch, W.J.1
  • 32
    • 0027925653 scopus 로고
    • Heat shock proteins functioning as molecular chaperones: Their roles in normal and stressed cells
    • W.J. Welch Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells Philos. Trans. R. Soc. Lond. B 339 1993 327 333
    • (1993) Philos. Trans. R. Soc. Lond. B , vol.339 , pp. 327-333
    • Welch, W.J.1
  • 33
    • 0029559547 scopus 로고
    • Evaluation of the killing volume of gas bubbles in sparged animal cell culture bioreactors
    • J. Wu, and M.F.A. Goosen Evaluation of the killing volume of gas bubbles in sparged animal cell culture bioreactors Enzyme Microb. Technol. 1995 17 pp. 241-247 & 1036-1042
    • (1995) Enzyme Microb. Technol. , pp. 17
    • Wu, J.1    Goosen, M.F.A.2
  • 34
    • 0028701355 scopus 로고
    • Effect of taxol and diamide on shear tolerance of hybridoma and insect cells
    • S. Wu, and R. Mutharasan Effect of taxol and diamide on shear tolerance of hybridoma and insect cells Ann. N. Y. Acad. Sci. 745 1994 167 176
    • (1994) Ann. N. Y. Acad. Sci. , vol.745 , pp. 167-176
    • Wu, S.1    Mutharasan, R.2
  • 35
    • 0028466527 scopus 로고
    • Molecular chaperones: Heat-shock proteins, foldases, and matchmakers
    • R.M. Wynn, J.R. Davie, R.P. Cox, and D.T. Chuang Molecular chaperones: heat-shock proteins, foldases, and matchmakers J. Lab. Clin. Med. 124 1994 31 36
    • (1994) J. Lab. Clin. Med. , vol.124 , pp. 31-36
    • Wynn, R.M.1    Davie, J.R.2    Cox, R.P.3    Chuang, D.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.