메뉴 건너뛰기




Volumn 353, Issue 2, 2007, Pages 475-480

IP3-independent signalling of OX1 orexin/hypocretin receptors to Ca2+ influx and ERK

Author keywords

Extracellular signal regulated kinase; G protein coupled receptor; Hypocretin; Orexin; Phosphoinositide; Phospholipase C; Receptor operated Ca2+ channel

Indexed keywords

INOSITOL 1,3,4,5 TETRAKISPHOSPHATE; INOSITOL 1,4 BISPHOSPHATE; INOSITOL 1,4,5 TRISPHOSPHATE; INOSITOL TRISPHOSPHATE 3 KINASE; MITOGEN ACTIVATED PROTEIN KINASE; OREXIN 1 RECEPTOR; UNCLASSIFIED DRUG; CALCIUM; G PROTEIN COUPLED RECEPTOR; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; NEUROPEPTIDE RECEPTOR; OREXIN RECEPTORS; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE;

EID: 33845803795     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.045     Document Type: Article
Times cited : (32)

References (42)
  • 1
    • 0025195367 scopus 로고
    • 'Quantal' Ca2+ release and the control of Ca2+ entry by inositol phosphates-a possible mechanism
    • Irvine R.F. 'Quantal' Ca2+ release and the control of Ca2+ entry by inositol phosphates-a possible mechanism. FEBS Lett. 263 (1990) 5-9
    • (1990) FEBS Lett. , vol.263 , pp. 5-9
    • Irvine, R.F.1
  • 2
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge M.J. Inositol trisphosphate and calcium signalling. Nature 361 (1993) 315-325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 3
    • 0032497845 scopus 로고    scopus 로고
    • The diversity and possible functions of the inositol polyphosphate 5-phosphatases
    • Erneux C., Govaerts C., Communi D., and Pesesse X. The diversity and possible functions of the inositol polyphosphate 5-phosphatases. Biochim. Biophys. Acta 1436 (1998) 185-199
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 185-199
    • Erneux, C.1    Govaerts, C.2    Communi, D.3    Pesesse, X.4
  • 5
    • 0035960037 scopus 로고    scopus 로고
    • Intracellular signalling. Receptor-specific messenger oscillations
    • Nash M.S., Young K.W., Challiss R.A., and Nahorski S.R. Intracellular signalling. Receptor-specific messenger oscillations. Nature 413 (2001) 381-382
    • (2001) Nature , vol.413 , pp. 381-382
    • Nash, M.S.1    Young, K.W.2    Challiss, R.A.3    Nahorski, S.R.4
  • 7
    • 0031303719 scopus 로고    scopus 로고
    • The multiplying roles of inositol lipids and phosphates in cell control processes
    • Michell R.H. The multiplying roles of inositol lipids and phosphates in cell control processes. Essays Biochem. 32 (1997) 31-47
    • (1997) Essays Biochem. , vol.32 , pp. 31-47
    • Michell, R.H.1
  • 8
    • 0033574526 scopus 로고    scopus 로고
    • The role of phosphatases in inositol signaling reactions
    • Majerus P.W., Kisseleva M.V., and Norris F.A. The role of phosphatases in inositol signaling reactions. J. Biol. Chem. 274 (1999) 10669-10672
    • (1999) J. Biol. Chem. , vol.274 , pp. 10669-10672
    • Majerus, P.W.1    Kisseleva, M.V.2    Norris, F.A.3
  • 9
    • 1842839883 scopus 로고    scopus 로고
    • Ins(1,4,5)P3 metabolism and the family of IP3-3Kinases
    • Pattni K., and Banting G. Ins(1,4,5)P3 metabolism and the family of IP3-3Kinases. Cell. Signal. 16 (2004) 643-654
    • (2004) Cell. Signal. , vol.16 , pp. 643-654
    • Pattni, K.1    Banting, G.2
  • 10
    • 0027523451 scopus 로고
    • Purification and characterization of a 43-kDa membrane-associated inositol polyphosphate 5-phosphatase from human placenta
    • Laxminarayan K.M., Matzaris M., Speed C.J., and Mitchell C.A. Purification and characterization of a 43-kDa membrane-associated inositol polyphosphate 5-phosphatase from human placenta. J. Biol. Chem. 268 (1993) 4968-4974
    • (1993) J. Biol. Chem. , vol.268 , pp. 4968-4974
    • Laxminarayan, K.M.1    Matzaris, M.2    Speed, C.J.3    Mitchell, C.A.4
  • 11
    • 0028011094 scopus 로고
    • The control of intracellular signal molecules at the level of their hydrolysis: the example of inositol 1,4,5-trisphosphate 5-phosphatase
    • Verjans B., Moreau C., and Erneux C. The control of intracellular signal molecules at the level of their hydrolysis: the example of inositol 1,4,5-trisphosphate 5-phosphatase. Mol. Cell. Endocrinol. 98 (1994) 167-171
    • (1994) Mol. Cell. Endocrinol. , vol.98 , pp. 167-171
    • Verjans, B.1    Moreau, C.2    Erneux, C.3
  • 12
    • 0033035605 scopus 로고    scopus 로고
    • Underexpression of the 43 kDa inositol polyphosphate 5-phosphatase is associated with spontaneous calcium oscillations and enhanced calcium responses following endothelin-1 stimulation
    • Speed C.J., Neylon C.B., Little P.J., and Mitchell C.A. Underexpression of the 43 kDa inositol polyphosphate 5-phosphatase is associated with spontaneous calcium oscillations and enhanced calcium responses following endothelin-1 stimulation. J. Cell Sci. 112 Pt 5 (1999) 669-679
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 5 , pp. 669-679
    • Speed, C.J.1    Neylon, C.B.2    Little, P.J.3    Mitchell, C.A.4
  • 13
    • 0030878394 scopus 로고    scopus 로고
    • Isoprenylated human brain type I inositol 1,4,5-trisphosphate 5-phosphatase controls Ca2+ oscillations induced by ATP in Chinese hamster ovary cells
    • De Smedt F., Missiaen L., Parys J.B., Vanweyenberg V., De Smedt H., and Erneux C. Isoprenylated human brain type I inositol 1,4,5-trisphosphate 5-phosphatase controls Ca2+ oscillations induced by ATP in Chinese hamster ovary cells. J. Biol. Chem. 272 (1997) 17367-17375
    • (1997) J. Biol. Chem. , vol.272 , pp. 17367-17375
    • De Smedt, F.1    Missiaen, L.2    Parys, J.B.3    Vanweyenberg, V.4    De Smedt, H.5    Erneux, C.6
  • 14
    • 0025860881 scopus 로고
    • Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme
    • Takazawa K., Perret J., Dumont J.E., and Erneux C. Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme. Biochem. J. 278 (1991) 883-886
    • (1991) Biochem. J. , vol.278 , pp. 883-886
    • Takazawa, K.1    Perret, J.2    Dumont, J.E.3    Erneux, C.4
  • 15
    • 0034531694 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C
    • Dewaste V., Pouillon V., Moreau C., Shears S., Takazawa K., and Erneux C. Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C. Biochem. J. 352 (2000) 343-351
    • (2000) Biochem. J. , vol.352 , pp. 343-351
    • Dewaste, V.1    Pouillon, V.2    Moreau, C.3    Shears, S.4    Takazawa, K.5    Erneux, C.6
  • 16
    • 18944403234 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate 3-kinases: functions and regulations
    • Xia H.J., and Yang G. Inositol 1,4,5-trisphosphate 3-kinases: functions and regulations. Cell Res. 15 (2005) 83-91
    • (2005) Cell Res. , vol.15 , pp. 83-91
    • Xia, H.J.1    Yang, G.2
  • 17
    • 0026320446 scopus 로고
    • Agonist-induced calcium signaling is impaired in fibroblasts overproducing inositol 1,3,4,5-tetrakisphosphate
    • Balla T., Sim S.S., Iida T., Choi K.Y., Catt K.J., and Rhee S.G. Agonist-induced calcium signaling is impaired in fibroblasts overproducing inositol 1,3,4,5-tetrakisphosphate. J. Biol. Chem. 266 (1991) 24719-24726
    • (1991) J. Biol. Chem. , vol.266 , pp. 24719-24726
    • Balla, T.1    Sim, S.S.2    Iida, T.3    Choi, K.Y.4    Catt, K.J.5    Rhee, S.G.6
  • 18
    • 0034672135 scopus 로고    scopus 로고
    • Effects of elevated expression of inositol 1,4,5-trisphosphate 3-kinase B on Ca2+ homoeostasis in HeLa cells
    • Millard T.H., Cullen P.J., and Banting G. Effects of elevated expression of inositol 1,4,5-trisphosphate 3-kinase B on Ca2+ homoeostasis in HeLa cells. Biochem. J. 352 (2000) 709-715
    • (2000) Biochem. J. , vol.352 , pp. 709-715
    • Millard, T.H.1    Cullen, P.J.2    Banting, G.3
  • 19
    • 0037184051 scopus 로고    scopus 로고
    • Determinants of metabotropic glutamate receptor-5-mediated Ca2+ and inositol 1,4,5-trisphosphate oscillation frequency. Receptor density versus agonist concentration
    • Nash M.S., Schell M.J., Atkinson P.J., Johnston N.R., Nahorski S.R., and Challiss R.A. Determinants of metabotropic glutamate receptor-5-mediated Ca2+ and inositol 1,4,5-trisphosphate oscillation frequency. Receptor density versus agonist concentration. J. Biol. Chem. 277 (2002) 35947-35960
    • (2002) J. Biol. Chem. , vol.277 , pp. 35947-35960
    • Nash, M.S.1    Schell, M.J.2    Atkinson, P.J.3    Johnston, N.R.4    Nahorski, S.R.5    Challiss, R.A.6
  • 21
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: the return of the inositol phosphates
    • Irvine R.F., and Schell M.J. Back in the water: the return of the inositol phosphates. Nat. Rev. Mol. Cell. Biol. 2 (2001) 327-338
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 22
    • 33646415110 scopus 로고    scopus 로고
    • Intracellular signal pathways utilized by the hypocretin/orexin receptors
    • de Lecea L., and Sutcliffe J.G. (Eds), Springer Science+Business Media, Berlin
    • Kukkonen J.P., and Åkerman K.E.O. Intracellular signal pathways utilized by the hypocretin/orexin receptors. In: de Lecea L., and Sutcliffe J.G. (Eds). Hypocretins as Integrators of Physiological Signals (2005), Springer Science+Business Media, Berlin 221-231
    • (2005) Hypocretins as Integrators of Physiological Signals , pp. 221-231
    • Kukkonen, J.P.1    Åkerman, K.E.O.2
  • 24
    • 0035800213 scopus 로고    scopus 로고
    • Orexin receptors couple to Ca2+ channels different from store-operated Ca2+ channels
    • Kukkonen J.P., and Akerman K.E. Orexin receptors couple to Ca2+ channels different from store-operated Ca2+ channels. Neuroreport 12 (2001) 2017-2020
    • (2001) Neuroreport , vol.12 , pp. 2017-2020
    • Kukkonen, J.P.1    Akerman, K.E.2
  • 25
    • 0034916496 scopus 로고    scopus 로고
    • 2-aminoethoxydiphenyl borate reveals heterogeneity in receptor-activated Ca(2+) discharge and store-operated Ca(2+) influx
    • Kukkonen J.P., Lund P.E., and Åkerman K.E.O. 2-aminoethoxydiphenyl borate reveals heterogeneity in receptor-activated Ca(2+) discharge and store-operated Ca(2+) influx. Cell Calcium 30 (2001) 117-129
    • (2001) Cell Calcium , vol.30 , pp. 117-129
    • Kukkonen, J.P.1    Lund, P.E.2    Åkerman, K.E.O.3
  • 27
    • 0037189920 scopus 로고    scopus 로고
    • Orexin signaling in recombinant neuron-like cells
    • Holmqvist T., Akerman K.E., and Kukkonen J.P. Orexin signaling in recombinant neuron-like cells. FEBS Lett. 526 (2002) 11-14
    • (2002) FEBS Lett. , vol.526 , pp. 11-14
    • Holmqvist, T.1    Akerman, K.E.2    Kukkonen, J.P.3
  • 28
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells
    • Stauffer T.P., Ahn S., and Meyer T. Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells. Curr. Biol. 8 (1998) 343-346
    • (1998) Curr. Biol. , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 29
    • 29444436827 scopus 로고    scopus 로고
    • OX1 orexin receptors activate extracellular signal-regulated kinase in Chinese hamster ovary cells via multiple mechanisms: the role of Ca2+ influx in OX1 receptor signaling
    • Ammoun S., Johansson L., Ekholm M.E., Holmqvist T., Danis A.S., Korhonen L., Sergeeva O.A., Haas H.L., Akerman K.E., and Kukkonen J.P. OX1 orexin receptors activate extracellular signal-regulated kinase in Chinese hamster ovary cells via multiple mechanisms: the role of Ca2+ influx in OX1 receptor signaling. Mol. Endocrinol. 20 (2006) 80-99
    • (2006) Mol. Endocrinol. , vol.20 , pp. 80-99
    • Ammoun, S.1    Johansson, L.2    Ekholm, M.E.3    Holmqvist, T.4    Danis, A.S.5    Korhonen, L.6    Sergeeva, O.A.7    Haas, H.L.8    Akerman, K.E.9    Kukkonen, J.P.10
  • 31
    • 0038576209 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-activated phosphoinositide turnover
    • Xu C., Watras J., and Loew L.M. Kinetic analysis of receptor-activated phosphoinositide turnover. J. Cell Biol. 161 (2003) 779-791
    • (2003) J. Cell Biol. , vol.161 , pp. 779-791
    • Xu, C.1    Watras, J.2    Loew, L.M.3
  • 32
    • 4644257566 scopus 로고    scopus 로고
    • Phospholipase C activator m-3M3FBS affects Ca2+ homeostasis independently of phospholipase C activation
    • Krjukova J., Holmqvist T., Danis A.S., Akerman K.E., and Kukkonen J.P. Phospholipase C activator m-3M3FBS affects Ca2+ homeostasis independently of phospholipase C activation. Br. J. Pharmacol. 143 (2004) 3-7
    • (2004) Br. J. Pharmacol. , vol.143 , pp. 3-7
    • Krjukova, J.1    Holmqvist, T.2    Danis, A.S.3    Akerman, K.E.4    Kukkonen, J.P.5
  • 33
    • 0033612242 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of inositol 1,4,5-trisphosphate that underlies complex Ca2+ mobilization patterns
    • Hirose K., Kadowaki S., Tanabe M., Takeshima H., and Iino M. Spatiotemporal dynamics of inositol 1,4,5-trisphosphate that underlies complex Ca2+ mobilization patterns. Science 284 (1999) 1527-1530
    • (1999) Science , vol.284 , pp. 1527-1530
    • Hirose, K.1    Kadowaki, S.2    Tanabe, M.3    Takeshima, H.4    Iino, M.5
  • 34
    • 33846256264 scopus 로고    scopus 로고
    • L. Johansson, M.E. Ekholm, J.P. Kukkonen, Regulation of OX1 orexin/hypocretin receptor-coupling to phospholipase C by Ca2+ influx, Br. J. Pharmacol. (2006), doi:10.1038/sj.bjp.0706959.
  • 35
    • 0029880626 scopus 로고    scopus 로고
    • Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation
    • De Smedt F., Boom A., Pesesse X., Schiffmann S.N., and Erneux C. Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation. J. Biol. Chem. 271 (1996) 10419-10424
    • (1996) J. Biol. Chem. , vol.271 , pp. 10419-10424
    • De Smedt, F.1    Boom, A.2    Pesesse, X.3    Schiffmann, S.N.4    Erneux, C.5
  • 36
    • 0042326882 scopus 로고    scopus 로고
    • The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells
    • Dewaste V., Moreau C., De Smedt F., Bex F., De Smedt H., Wuytack F., Missiaen L., and Erneux C. The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells. Biochem. J. 374 (2003) 41-49
    • (2003) Biochem. J. , vol.374 , pp. 41-49
    • Dewaste, V.1    Moreau, C.2    De Smedt, F.3    Bex, F.4    De Smedt, H.5    Wuytack, F.6    Missiaen, L.7    Erneux, C.8
  • 37
    • 0022549501 scopus 로고
    • Protein kinase C phosphorylates human platelet inositol trisphosphate 5'-phosphomonoesterase, increasing the phosphatase activity
    • Connolly T.M., Lawing Jr. W.J., and Majerus P.W. Protein kinase C phosphorylates human platelet inositol trisphosphate 5'-phosphomonoesterase, increasing the phosphatase activity. Cell 46 (1986) 951-958
    • (1986) Cell , vol.46 , pp. 951-958
    • Connolly, T.M.1    Lawing Jr., W.J.2    Majerus, P.W.3
  • 38
    • 0030891857 scopus 로고    scopus 로고
    • D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism
    • Communi D., Vanweyenberg V., and Erneux C. D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism. EMBO J. 16 (1997) 1943-1952
    • (1997) EMBO J. , vol.16 , pp. 1943-1952
    • Communi, D.1    Vanweyenberg, V.2    Erneux, C.3
  • 39
    • 0035914409 scopus 로고    scopus 로고
    • A novel receptor-mediated regulation mechanism of type I inositol polyphosphate 5-phosphatase by calcium/calmodulin-dependent protein kinase II phosphorylation
    • Communi D., Gevaert K., Demol H., Vandekerckhove J., and Erneux C. A novel receptor-mediated regulation mechanism of type I inositol polyphosphate 5-phosphatase by calcium/calmodulin-dependent protein kinase II phosphorylation. J. Biol. Chem. 276 (2001) 38738-38747
    • (2001) J. Biol. Chem. , vol.276 , pp. 38738-38747
    • Communi, D.1    Gevaert, K.2    Demol, H.3    Vandekerckhove, J.4    Erneux, C.5
  • 40
    • 0033555775 scopus 로고    scopus 로고
    • Receptor-activated Ca2+ inflow in animal cells: a variety of pathways tailored to meet different intracellular Ca2+ signalling requirements
    • Barritt G.J. Receptor-activated Ca2+ inflow in animal cells: a variety of pathways tailored to meet different intracellular Ca2+ signalling requirements. Biochem. J. 337 (1999) 153-169
    • (1999) Biochem. J. , vol.337 , pp. 153-169
    • Barritt, G.J.1
  • 41
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham D.E. TRP channels as cellular sensors. Nature 426 (2003) 517-524
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.