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Volumn 272, Issue 6 35-6, 1997, Pages

Bombesin-stimulated ceramide production and MAP kinase activation in rabbit rectosigmoid smooth muscle cells

Author keywords

Bombesin; Mitogen activated protein

Indexed keywords

BOMBESIN; CALPHOSTIN C; CERAMIDE; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 0030760220     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.1997.272.6.g1615     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0025120244 scopus 로고
    • Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
    • Anderson, N. G., J. L. Maller, N. K. Tonks, and T. W. Sturgill. Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase. Nature 343: 651-653, 1990.
    • (1990) Nature , vol.343 , pp. 651-653
    • Anderson, N.G.1    Maller, J.L.2    Tonks, N.K.3    Sturgill, T.W.4
  • 2
    • 0023062987 scopus 로고
    • Inositol trisphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M. J. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 56: 159-183, 1987.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 159-183
    • Berridge, M.J.1
  • 3
    • 0025356574 scopus 로고
    • Regulation and cellular functions of phosphatidylcholine hydrolysis
    • Billah, M. M., and J. C. Anthes. Regulation and cellular functions of phosphatidylcholine hydrolysis. Biochem. J. 269: 281-291, 1990.
    • (1990) Biochem. J. , vol.269 , pp. 281-291
    • Billah, M.M.1    Anthes, J.C.2
  • 6
    • 0020120872 scopus 로고
    • Receptors on smooth muscle cells: Characterization by contraction and specific antagonists
    • Gastrointest. Liver Physiol. 5
    • Bitar, K. N., and M. G. Makhlouf. Receptors on smooth muscle cells: characterization by contraction and specific antagonists. Am. J. Physiol. 242 (Gastrointest. Liver Physiol. 5): G400-G407, 1982.
    • (1982) Am. J. Physiol. , vol.242
    • Bitar, K.N.1    Makhlouf, M.G.2
  • 7
    • 0028835590 scopus 로고
    • Modulation of smooth muscle contraction by sphingosylphosphorylcholine
    • Gastrointest. Liver Physiol. 32
    • Bitar, K. N., and H. Yamada. Modulation of smooth muscle contraction by sphingosylphosphorylcholine. Am. J. Physiol. 269 (Gastrointest. Liver Physiol. 32): G370-G377, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Bitar, K.N.1    Yamada, H.2
  • 8
    • 0028031699 scopus 로고
    • Neutral sphingomyelinase action stimulates signal transduction of tumor necrosis factor-α in the synthesis of cholesteryl esters in human fibroblasts
    • Chatterjee, S. Neutral sphingomyelinase action stimulates signal transduction of tumor necrosis factor-α in the synthesis of cholesteryl esters in human fibroblasts. J. Biol. Chem. 269: 879-882, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 879-882
    • Chatterjee, S.1
  • 9
    • 0026300729 scopus 로고
    • Extracellular signal-regulated kinases: ERKs in progress
    • Cobb, M. H., T. G. Boulton, and D. J. Robbins. Extracellular signal-regulated kinases: ERKs in progress. Cell Regul. 2: 965-978, 1991.
    • (1991) Cell Regul. , vol.2 , pp. 965-978
    • Cobb, M.H.1    Boulton, T.G.2    Robbins, D.J.3
  • 10
    • 0025707230 scopus 로고
    • Mass measurement of inositol 1,4,5-trisphosphate and sn-1,2- diacylglycerol in bombesin-stimulated Swiss 3T3 mouse fibroblasts
    • Cook, S. J., S. Palmer, R. Plevin, and M. J. Wakelam. Mass measurement of inositol 1,4,5-trisphosphate and sn-1,2- diacylglycerol in bombesin-stimulated Swiss 3T3 mouse fibroblasts. Biochem. J. 265: 617-620, 1990.
    • (1990) Biochem. J. , vol.265 , pp. 617-620
    • Cook, S.J.1    Palmer, S.2    Plevin, R.3    Wakelam, M.J.4
  • 11
    • 0024470869 scopus 로고
    • Analysis of the water-soluble products of phosphatidylcholine breakdown by ion-exchange chromatography. Bombesin and TPA (12-O- tetradecanoylphorbol 13-acetate) stimulate choline generation in Swiss 3T3 cells by a common mechanism
    • Cook, S. J., and M. J. Wakelam. Analysis of the water-soluble products of phosphatidylcholine breakdown by ion-exchange chromatography. Bombesin and TPA (12-O- tetradecanoylphorbol 13-acetate) stimulate choline generation in Swiss 3T3 cells by a common mechanism. Biochem. J. 263: 581-587, 1989.
    • (1989) Biochem. J. , vol.263 , pp. 581-587
    • Cook, S.J.1    Wakelam, M.J.2
  • 13
    • 0027165150 scopus 로고
    • Mitogen-activated protein kinase signal transduction pathway
    • Davis, R. J. Mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268: 14553-14556, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14553-14556
    • Davis, R.J.1
  • 14
    • 0025869402 scopus 로고
    • Role of phospholipases in generating lipid second messengers in signal transduction
    • Dennis, E. A., S. G. Rhee, M. M. Billah, and Y. A. Hannun. Role of phospholipases in generating lipid second messengers in signal transduction. FASEB J. 5: 2068-2077, 1991.
    • (1991) FASEB J. , vol.5 , pp. 2068-2077
    • Dennis, E.A.1    Rhee, S.G.2    Billah, M.M.3    Hannun, Y.A.4
  • 15
    • 0025162155 scopus 로고
    • Signaling through phosphatidylcholine breakdown
    • Exton, J. H. Signaling through phosphatidylcholine breakdown. J. Biol. Chem. 265: 1-4, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1-4
    • Exton, J.H.1
  • 16
    • 0027263039 scopus 로고
    • Direct evidence for tyrosine and threonine phosphorylation and activation of mitogen-activated protein kinase by vasopressin in cultured rat vascular smooth muscle cells
    • Granot, Y., E. Erikson, H. Fridman, V. V. Putten, B. Williams, R. W. Schrier, and J. L. Maller. Direct evidence for tyrosine and threonine phosphorylation and activation of mitogen-activated protein kinase by vasopressin in cultured rat vascular smooth muscle cells. J. Biol. Chem. 268: 9564-9569, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9564-9569
    • Granot, Y.1    Erikson, E.2    Fridman, H.3    Putten, V.V.4    Williams, B.5    Schrier, R.W.6    Maller, J.L.7
  • 17
    • 0024541436 scopus 로고
    • Functions of sphingolipids and sphingolipid breakdown products in cellular regulation
    • Hannun, Y. A., and R. M. Bell. Functions of sphingolipids and sphingolipid breakdown products in cellular regulation. Science 243: 500-507, 1989.
    • (1989) Science , vol.243 , pp. 500-507
    • Hannun, Y.A.1    Bell, R.M.2
  • 19
    • 0027669148 scopus 로고
    • Sphingolipids as mediators of effects of platelet-derived growth factor in vascular smooth muscle cells
    • Cell Physiol. 34
    • Jacobs, L. S., and M. Kester. Sphingolipids as mediators of effects of platelet-derived growth factor in vascular smooth muscle cells. Am. J. Physiol. 265 (Cell Physiol. 34): C740-C747, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Jacobs, L.S.1    Kester, M.2
  • 20
    • 0024358172 scopus 로고
    • A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita, I., and H. Fujisawa. A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal. Biochem. 183: 139-143, 1989.
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.2
  • 21
    • 0026649431 scopus 로고
    • 2+-independent isoforms of protein kinase C differentially translocate in smooth muscle
    • Cell Physiol. 32
    • 2+-independent isoforms of protein kinase C differentially translocate in smooth muscle. Am. J. Physiol. 263 (Cell Physiol. 32): C714-C719, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Khalil, R.A.1    Lajoie, C.2    Resnick, M.S.3    Morgan, K.G.4
  • 22
    • 0026739870 scopus 로고
    • Phenylephrine-induced translocation of protein kinase C and shortening of two types of vascular cells of the ferret
    • Khalil, R. A., and K. G. Morgan. Phenylephrine-induced translocation of protein kinase C and shortening of two types of vascular cells of the ferret. J. Physiol. (Lond.) 455: 585-599, 1992.
    • (1992) J. Physiol. (Lond.) , vol.455 , pp. 585-599
    • Khalil, R.A.1    Morgan, K.G.2
  • 23
    • 0027203852 scopus 로고
    • PKC-mediated redistribution of mitogen-activated protein kinase during smooth muscle cell activation
    • Cell Physiol. 34
    • Khalil, R. A., and K. G. Morgan. PKC-mediated redistribution of mitogen-activated protein kinase during smooth muscle cell activation. Am. J. Physiol. 265 (Cell Physiol. 34): C406-C411, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Khalil, R.A.1    Morgan, K.G.2
  • 24
    • 0024550448 scopus 로고
    • Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C
    • Kobayashi, E., H. Nakano, M. Morimoto, and T. Tamaoki. Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C. Biochem. Biophys. Res. Commun. 159: 548-553, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 548-553
    • Kobayashi, E.1    Nakano, H.2    Morimoto, M.3    Tamaoki, T.4
  • 25
    • 0023925318 scopus 로고
    • 1,2-Diacylglycerols, but not phorbol esters, activate a potential inhibitory pathway for protein kinase C in GH3 pituitary cells. Evidence for involvement of a sphingomyelinase
    • Kolesnick, R. N., and S. Clegg. 1,2-Diacylglycerols, but not phorbol esters, activate a potential inhibitory pathway for protein kinase C in GH3 pituitary cells. Evidence for involvement of a sphingomyelinase. J. Biol. Chem. 263: 6534-6537, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6534-6537
    • Kolesnick, R.N.1    Clegg, S.2
  • 26
    • 0026098922 scopus 로고
    • Molecular species of diacylglycerols and phosphoglycerides and the postmortem changes in the molecular species of diacylglycerols in rat brains
    • Lee, C. H., and A. K. Hajra. Molecular species of diacylglycerols and phosphoglycerides and the postmortem changes in the molecular species of diacylglycerols in rat brains. J. Neurochem. 56: 370-379, 1991.
    • (1991) J. Neurochem. , vol.56 , pp. 370-379
    • Lee, C.H.1    Hajra, A.K.2
  • 27
    • 0024344354 scopus 로고
    • Endothelin stimulates a sustained 1,2-diacylglycerol increase and protein kinase C activation in bovine aortic smooth muscle cells
    • Lee, T. S., T. Chao, K. Q. Hu, and G. L. King. Endothelin stimulates a sustained 1,2-diacylglycerol increase and protein kinase C activation in bovine aortic smooth muscle cells. Biochem. Biophys. Res. Commun. 162: 381-386, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 381-386
    • Lee, T.S.1    Chao, T.2    Hu, K.Q.3    King, G.L.4
  • 28
    • 0026509971 scopus 로고
    • MAP kinase activator from insulin-stimulated skeletal muscle is a protein threonine/tyrosine kinase
    • Nakielny, S., P. Cohen, J. Wu, and T. Sturgill. MAP kinase activator from insulin-stimulated skeletal muscle is a protein threonine/tyrosine kinase. EMBO J. 11: 2123-2129, 1992.
    • (1992) EMBO J. , vol.11 , pp. 2123-2129
    • Nakielny, S.1    Cohen, P.2    Wu, J.3    Sturgill, T.4
  • 29
    • 0027094804 scopus 로고
    • Sphingomyelinase and cell-permeable ceramide analogs stimulate cellular proliferation in quiescent Swiss 3T3 fibroblasts
    • Olivera, A., N. E. Buckley, and S. Spiegel. Sphingomyelinase and cell-permeable ceramide analogs stimulate cellular proliferation in quiescent Swiss 3T3 fibroblasts. J. Biol. Chem. 267: 26121-26127, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26121-26127
    • Olivera, A.1    Buckley, N.E.2    Spiegel, S.3
  • 30
    • 0027371722 scopus 로고
    • Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens
    • Olivera, A., and S. Spiegel. Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens. Nature 365: 557-560, 1993.
    • (1993) Nature , vol.365 , pp. 557-560
    • Olivera, A.1    Spiegel, S.2
  • 31
    • 0026696360 scopus 로고
    • Mitogen-activated protein kinases: Versatile transducers for cell signaling
    • Pelech, S. L., and J. S. Sanghera. Mitogen-activated protein kinases: versatile transducers for cell signaling. Trends Biochem. Sci. 17: 233-238, 1992.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 233-238
    • Pelech, S.L.1    Sanghera, J.S.2
  • 32
    • 0023626217 scopus 로고
    • Protein kinase C in the regulation of smooth muscle contraction
    • Rasmussen, H., Y. Takuwa, and S. Park. Protein kinase C in the regulation of smooth muscle contraction. FASEB J. 1: 177-185, 1987.
    • (1987) FASEB J. , vol.1 , pp. 177-185
    • Rasmussen, H.1    Takuwa, Y.2    Park, S.3
  • 33
    • 0026458406 scopus 로고
    • TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown
    • Schutze, S., K. Potthoff, T. Machleidt, D. Berkovic, K. Wiegmann, and M. Kronke. TNF activates NF-κB by phosphatidylcholine-specific phospholipase C-induced "acidic" sphingomyelin breakdown. Cell 71: 765-776, 1992.
    • (1992) Cell , vol.71 , pp. 765-776
    • Schutze, S.1    Potthoff, K.2    Machleidt, T.3    Berkovic, D.4    Wiegmann, K.5    Kronke, M.6
  • 34
    • 0023202617 scopus 로고
    • A tumour promoter, 12-O-tetradecanoylphorbol 13-acetate, increases cellular 1,2-diacylglycerol content through a mechanism other than phosphoinositide hydrolysis in Swiss-mouse 3T3 fibroblasts
    • Takuwa, N., Y. Takuwa, and H. Rasmussen. A tumour promoter, 12-O-tetradecanoylphorbol 13-acetate, increases cellular 1,2-diacylglycerol content through a mechanism other than phosphoinositide hydrolysis in Swiss-mouse 3T3 fibroblasts. Biochem. J. 243: 647-653, 1987.
    • (1987) Biochem. J. , vol.243 , pp. 647-653
    • Takuwa, N.1    Takuwa, Y.2    Rasmussen, H.3
  • 36
    • 0026728723 scopus 로고
    • Angiotensin II stimulates two myelin basic protein/microtubule-associated protein 2 kinases in cultured vascular smooth muscle cells
    • Tsuda, T., Y. Kawahara, Y. Ishida, M. Koide, K. Shii, and M. Yokoyama. Angiotensin II stimulates two myelin basic protein/microtubule-associated protein 2 kinases in cultured vascular smooth muscle cells. Circ. Res. 71: 620-630, 1992.
    • (1992) Circ. Res. , vol.71 , pp. 620-630
    • Tsuda, T.1    Kawahara, Y.2    Ishida, Y.3    Koide, M.4    Shii, K.5    Yokoyama, M.6
  • 37
    • 0024341209 scopus 로고
    • Enzymatic quantification of sphingosine in the picomole range in cultured cells
    • Van Veldhoven, P. P., W. R. Bishop, and R. M. Bell. Enzymatic quantification of sphingosine in the picomole range in cultured cells. Anal. Biochem. 183: 177-189, 1989.
    • (1989) Anal. Biochem. , vol.183 , pp. 177-189
    • Van Veldhoven, P.P.1    Bishop, W.R.2    Bell, R.M.3
  • 38
    • 0028863441 scopus 로고
    • Activation of MAP kinase and translocation with HSP27 in bombesin-induced contraction of rectosigmoid smooth muscle
    • Gastrointest. Liver Physiol. 32
    • Yamada, H., J. Strahler, M. J. Welsh, and K. N. Bitar. Activation of MAP kinase and translocation with HSP27 in bombesin-induced contraction of rectosigmoid smooth muscle. Am. J. Physiol. 269 (Gastrointest. Liver Physiol. 32): G683-G691, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Yamada, H.1    Strahler, J.2    Welsh, M.J.3    Bitar, K.N.4


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