메뉴 건너뛰기




Volumn 101, Issue 2, 2007, Pages 331-347

Apoptosis in medfly hemocytes is regulated during pupariation through FAK, Src, ERK, PI-3K p85a, and Akt survival signaling

Author keywords

Apoptosis; ERK; FAK Src; Insect hemocytes; PI 3K Akt; Signaling

Indexed keywords

FOCAL ADHESION KINASE; GENE PRODUCT; MITOGEN ACTIVATED PROTEIN KINASE; P85A PROTEIN; PROTEIN KINASE B; STEROID RECEPTOR COACTIVATOR; UNCLASSIFIED DRUG;

EID: 34247854888     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.21175     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding
    • Bradford M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 2
    • 15944362764 scopus 로고    scopus 로고
    • Genetic control of programmed cell death in Drosophila melanogaster
    • Cashio P, Lee TV, Bergmann A. 2005. Genetic control of programmed cell death in Drosophila melanogaster. Semin Cell Dev Biol 16:225-235.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 225-235
    • Cashio, P.1    Lee, T.V.2    Bergmann, A.3
  • 3
    • 0029012670 scopus 로고
    • Lipopolysaccharide-stimulated exocytosis of nonself recognition protein from insect hemocytes depends on protein tyrosine phosphorylation
    • Charalambidis ND, Zervas CG, Lambropoulou M, Katsoris PG, Marmaras VJ. 1995. Lipopolysaccharide-stimulated exocytosis of nonself recognition protein from insect hemocytes depends on protein tyrosine phosphorylation. Eur J Cell Biol 67:32-41.
    • (1995) Eur J Cell Biol , vol.67 , pp. 32-41
    • Charalambidis, N.D.1    Zervas, C.G.2    Lambropoulou, M.3    Katsoris, P.G.4    Marmaras, V.J.5
  • 4
    • 0030003494 scopus 로고    scopus 로고
    • Covalent association of lipopolysaccharide at the hemocyte surface of insects is an initial step for its internalization-protein-tyrosine phosphorylation requirement
    • Charalambidis ND, Foukas LC, Marmaras VJ. 1996. Covalent association of lipopolysaccharide at the hemocyte surface of insects is an initial step for its internalization-protein-tyrosine phosphorylation requirement. Eur J Biochem 236:200-206.
    • (1996) Eur J Biochem , vol.236 , pp. 200-206
    • Charalambidis, N.D.1    Foukas, L.C.2    Marmaras, V.J.3
  • 5
    • 0141997715 scopus 로고    scopus 로고
    • Insect defences against virus infection: The role of apoptosis
    • Clarke TE, Clem RJ. 2003. Insect defences against virus infection: The role of apoptosis. Int Rev Immunol 22:401-424.
    • (2003) Int Rev Immunol , vol.22 , pp. 401-424
    • Clarke, T.E.1    Clem, R.J.2
  • 6
    • 15744404027 scopus 로고    scopus 로고
    • Cooray S, Jin L, Best JM. 2005. The involvement of survival signaling pathways in rubella-virus induced apoptosis. J Virol 2: 1(Open Access article in BioMed Central).
    • Cooray S, Jin L, Best JM. 2005. The involvement of survival signaling pathways in rubella-virus induced apoptosis. J Virol 2: 1(Open Access article in BioMed Central).
  • 7
  • 8
    • 0033593001 scopus 로고    scopus 로고
    • Expression of DFak56, a Drosophila homolog of vertebrate focal adhesion kinase, supports a role in cell migration in vivo
    • Fox GL, Rebay I, Hynes RO. 1999. Expression of DFak56, a Drosophila homolog of vertebrate focal adhesion kinase, supports a role in cell migration in vivo. Proc Natl Acad Sci USA 96:14978-14983.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14978-14983
    • Fox, G.L.1    Rebay, I.2    Hynes, R.O.3
  • 12
    • 0344643401 scopus 로고    scopus 로고
    • Csk regulates integrin-mediated signals: Involvement of differential activation of ERK and Akt
    • Gu J, Nada S, Okada M, Sekiguchi K. 2003. Csk regulates integrin-mediated signals: Involvement of differential activation of ERK and Akt. Biochem Biophys Res Commun 303:973-977.
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 973-977
    • Gu, J.1    Nada, S.2    Okada, M.3    Sekiguchi, K.4
  • 14
    • 0015797002 scopus 로고
    • Preparation, molecular weight, base composition, and secondary structure of giant nuclear ribonucleic acid
    • Holmes DS, Bonner J. 1973. Preparation, molecular weight, base composition, and secondary structure of giant nuclear ribonucleic acid. Biochemistry 12:2330-2338.
    • (1973) Biochemistry , vol.12 , pp. 2330-2338
    • Holmes, D.S.1    Bonner, J.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemli UK. 1970. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemli, U.K.1
  • 17
    • 18844440752 scopus 로고    scopus 로고
    • Uptake of LPS/E. coli/latex beads via distinct signalling pathways in medfly hemocytes: The role of MAP kinases activation and protein secretion
    • Lamprou I, Tsakas S, Theodorou GL, Karakantza M, Lampropoulou M, Marmaras VJ. 2005. Uptake of LPS/E. coli/latex beads via distinct signalling pathways in medfly hemocytes: The role of MAP kinases activation and protein secretion Biochim. Biophys Acta 1744:1-10.
    • (2005) Biochim. Biophys Acta , vol.1744 , pp. 1-10
    • Lamprou, I.1    Tsakas, S.2    Theodorou, G.L.3    Karakantza, M.4    Lampropoulou, M.5    Marmaras, V.J.6
  • 18
    • 0028238346 scopus 로고
    • Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain
    • Lukashev ME, Sheppard D, Pytela R. 1994. Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain. J Biol Chem 269:18311-18314.
    • (1994) J Biol Chem , vol.269 , pp. 18311-18314
    • Lukashev, M.E.1    Sheppard, D.2    Pytela, R.3
  • 19
    • 0030884103 scopus 로고    scopus 로고
    • PKB/Akt: Connecting phosphoinositide 3-kinase to cell survival and beyond
    • Marte BM, Downward J. 1997. PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond. Trends Biochem Sci 22:355-358.
    • (1997) Trends Biochem Sci , vol.22 , pp. 355-358
    • Marte, B.M.1    Downward, J.2
  • 20
    • 20444377685 scopus 로고    scopus 로고
    • MAP kinases mediate phagocytosis and melanization via prophenoloxidase activation in medfly hemocytes
    • Mavrouli MD, Tsakas S, Theodorou GL, Lampropoulou M, Marmaras VJ. 2005. MAP kinases mediate phagocytosis and melanization via prophenoloxidase activation in medfly hemocytes. Biochim Biophys Acta 1744:145-156.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 145-156
    • Mavrouli, M.D.1    Tsakas, S.2    Theodorou, G.L.3    Lampropoulou, M.4    Marmaras, V.J.5
  • 21
    • 0344153292 scopus 로고    scopus 로고
    • Apoptosis and development
    • McCarthy JV. 2003. Apoptosis and development. Essays Biochem 39:11-24.
    • (2003) Essays Biochem , vol.39 , pp. 11-24
    • McCarthy, J.V.1
  • 22
    • 0036240265 scopus 로고    scopus 로고
    • Induction of neutrophil apoptosis and secondary necrosis during endotoxin-induced pulmonary inflammation in mice
    • Medan D, Wang L, Yang X, Dokka S, Castranova V, Rojanasakul Y. 2002. Induction of neutrophil apoptosis and secondary necrosis during endotoxin-induced pulmonary inflammation in mice. Cell Physiol 191:320-326.
    • (2002) Cell Physiol , vol.191 , pp. 320-326
    • Medan, D.1    Wang, L.2    Yang, X.3    Dokka, S.4    Castranova, V.5    Rojanasakul, Y.6
  • 24
    • 0035805104 scopus 로고    scopus 로고
    • Involvement of FAK/Src complex in the processes of Escherichia coli phagocytosis by insect hemocytes
    • Metheniti A, Paraskevopoulou N, Lampropoulou M, Marmaras VJ. 2001. Involvement of FAK/Src complex in the processes of Escherichia coli phagocytosis by insect hemocytes. FEBS Lett 496:55-59.
    • (2001) FEBS Lett , vol.496 , pp. 55-59
    • Metheniti, A.1    Paraskevopoulou, N.2    Lampropoulou, M.3    Marmaras, V.J.4
  • 25
  • 27
    • 0000826497 scopus 로고
    • The circulatory system and associated cells and tissues
    • Ashburner M, Wright TRF, editors, New York: Academic Press. pp
    • Rizki TM. 1978. The circulatory system and associated cells and tissues. In: Ashburner M, Wright TRF, editors. The genetics and biology of Drosophila. New York: Academic Press. pp 409-413.
    • (1978) The genetics and biology of Drosophila , pp. 409-413
    • Rizki, T.M.1
  • 28
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • Schaller MD. 2001. Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim Biophys Acta 1540:1-21.
    • (2001) Biochim Biophys Acta , vol.1540 , pp. 1-21
    • Schaller, M.D.1
  • 29
    • 0028122650 scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • Schaller MD, Parsons JT. 1994. Biochemical signals and biological responses elicited by the focal adhesion kinase. Curr Opin Cell Biol 6:705-710.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 30
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P. 1994. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372:786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    van der Geer, P.4
  • 32
    • 0034717285 scopus 로고    scopus 로고
    • Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60
    • Sonoda Y, Matsumoto Y, Funakoshi M, Yamamoto D, Hanks SK, Kasahara T. 2000. Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60. J Biol Chem 275:16309-16315.
    • (2000) J Biol Chem , vol.275 , pp. 16309-16315
    • Sonoda, Y.1    Matsumoto, Y.2    Funakoshi, M.3    Yamamoto, D.4    Hanks, S.K.5    Kasahara, T.6
  • 33
    • 0028054017 scopus 로고
    • T-cell apoptosis detected in situ during positive and negative selection in the thymus
    • Surh CD, Sprent J. 1994. T-cell apoptosis detected in situ during positive and negative selection in the thymus. Nature 372:100-103.
    • (1994) Nature , vol.372 , pp. 100-103
    • Surh, C.D.1    Sprent, J.2
  • 34
    • 24044451906 scopus 로고    scopus 로고
    • Pathways of apoptosis and importance in development
    • Twomey C, McCarthy JV. 2005. Pathways of apoptosis and importance in development. J Cell Mol Med 9:345-359.
    • (2005) J Cell Mol Med , vol.9 , pp. 345-359
    • Twomey, C.1    McCarthy, J.V.2
  • 35
    • 0030911015 scopus 로고    scopus 로고
    • p60 is an adaptor for the Drosophila phosphoinositide 3-kinase, Dp110
    • Weinkove D, Leevers SJ, MacDougall LK, Waterfield MD. 1997. p60 is an adaptor for the Drosophila phosphoinositide 3-kinase, Dp110. J Biol Chem 272:14606-14610.
    • (1997) J Biol Chem , vol.272 , pp. 14606-14610
    • Weinkove, D.1    Leevers, S.J.2    MacDougall, L.K.3    Waterfield, M.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.