메뉴 건너뛰기




Volumn 41, Issue 5, 2005, Pages 235-245

Ca2+ clearance in smooth muscle: Lessons from gene-altered mice

Author keywords

Ca2+; NCX; NKA; PMCA; SERCA; Transgenic mice

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM; SODIUM CALCIUM EXCHANGE PROTEIN; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CATION TRANSPORT PROTEIN; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 31544466232     PISSN: 09168737     EISSN: 09168737     Source Type: Journal    
DOI: 10.1540/jsmr.41.235     Document Type: Review
Times cited : (27)

References (68)
  • 2
    • 0025835876 scopus 로고
    • Identification of intracellular calcium pools. Selective modification by thapsigargin
    • Bian, J.H., Ghosh, T.K., Wang, J.C. and Gill, D.L. (1991). Identification of intracellular calcium pools. Selective modification by thapsigargin. J. Biol. Chem. 266: 8801-8806.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8801-8806
    • Bian, J.H.1    Ghosh, T.K.2    Wang, J.C.3    Gill, D.L.4
  • 4
    • 0032801648 scopus 로고    scopus 로고
    • Sodium/calcium exchange: Its physiological implications
    • Blaustein, M.P. and Lederer, W.J. (1999). Sodium/calcium exchange: its physiological implications. Physiol. Rev. 79: 763-854.
    • (1999) Physiol. Rev. , vol.79 , pp. 763-854
    • Blaustein, M.P.1    Lederer, W.J.2
  • 5
    • 0034697029 scopus 로고    scopus 로고
    • 2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban
    • 2+ affinity by phospholamban in transgenic hearts overexpressing a non-phosphorylatable form of phospholamban. J. Biol. Chem. 275: 12129-12135.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12129-12135
    • Brittsan, A.G.1    Carr, A.N.2    Schmidt, A.G.3    Kranias, E.G.4
  • 6
    • 0022502914 scopus 로고
    • Regulatory systems for the cytoplasmic calcium concentration in smooth muscle
    • Casteels, R., Wuytack, F., Himpens, B. and Raeymaekers, L. (1986). Regulatory systems for the cytoplasmic calcium concentration in smooth muscle. Biomed. Biochim. Acta. 45: S147-S152.
    • (1986) Biomed. Biochim. Acta , vol.45
    • Casteels, R.1    Wuytack, F.2    Himpens, B.3    Raeymaekers, L.4
  • 7
    • 0036947172 scopus 로고    scopus 로고
    • From mouse to man: Understanding heart failure through genetically altered mouse models
    • Chu, G., Haghighi, K. and Kranias, E.G. (2002). From mouse to man: understanding heart failure through genetically altered mouse models. J. Card. Fail. 8: S432-S449.
    • (2002) J. Card. Fail. , vol.8
    • Chu, G.1    Haghighi, K.2    Kranias, E.G.3
  • 8
    • 0029115673 scopus 로고
    • Regulation of vascular tone: Crosstalk between sarcoplasmic reticulum and plasmalemma
    • Daniel, E.E., van Breemen, C., Schilling, W.P. and Kwan, C.Y. (1995). Regulation of vascular tone: crosstalk between sarcoplasmic reticulum and plasmalemma. Can. J. Physiol. Pharmacol. 73: 551-557.
    • (1995) Can. J. Physiol. Pharmacol. , vol.73 , pp. 551-557
    • Daniel, E.E.1    Van Breemen, C.2    Schilling, W.P.3    Kwan, C.Y.4
  • 10
    • 24944538808 scopus 로고    scopus 로고
    • Chair's introduction: Role of the sarcoplasmic reticulum in smooth muscle
    • Eisner, D. (2002). Chair's introduction: role of the sarcoplasmic reticulum in smooth muscle. Novartis Found. Symp. 246: 1-5.
    • (2002) Novartis Found. Symp. , vol.246 , pp. 1-5
    • Eisner, D.1
  • 11
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto, T. (1993). Calcium pump of the plasma membrane is localized in caveolae. J. Cell Biol. 120: 1147-1157.
    • (1993) J. Cell Biol. , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 12
    • 0141819124 scopus 로고    scopus 로고
    • Plasma membrane calcium ATPase overexpression in arterial smooth muscle increases vasomotor responsiveness and blood pressure
    • Gros, R., Afroze, T., You, X.M., Kabir, G., Van Wert, R., Kalair, W., Hoque, A.E., Mungrue, I.N. and Husain, M. (2003). Plasma membrane calcium ATPase overexpression in arterial smooth muscle increases vasomotor responsiveness and blood pressure. Circ. Res. 93: 614-621.
    • (2003) Circ. Res. , vol.93 , pp. 614-621
    • Gros, R.1    Afroze, T.2    You, X.M.3    Kabir, G.4    Van Wert, R.5    Kalair, W.6    Hoque, A.E.7    Mungrue, I.N.8    Husain, M.9
  • 18
    • 0032997363 scopus 로고    scopus 로고
    • Identification of a specific role for the Na,K-ATPase α2 isoform as a regulator of calcium in the heart
    • James, P.F., Grupp, I.L., Grupp, G., Woo, A.L., Askew, G.R., Croyle, M.L., Walsh, R.A. and Lingrel, J.B. (1999). Identification of a specific role for the Na,K-ATPase α2 isoform as a regulator of calcium in the heart. Mol. Cell 3: 555-563.
    • (1999) Mol. Cell , vol.3 , pp. 555-563
    • James, P.F.1    Grupp, I.L.2    Grupp, G.3    Woo, A.L.4    Askew, G.R.5    Croyle, M.L.6    Walsh, R.A.7    Lingrel, J.B.8
  • 20
    • 0031052476 scopus 로고    scopus 로고
    • + pump low and high ouabain affinity α subunit isoforms are differently distributed in cells
    • + pump low and high ouabain affinity α subunit isoforms are differently distributed in cells. Proc. Natl. Acad. Sci. USA. 94: 1800-1805.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1800-1805
    • Juhaszova, M.1    Blaustein, M.P.2
  • 21
    • 3042657304 scopus 로고    scopus 로고
    • 2+ and contraction in smooth muscle
    • 2+ and contraction in smooth muscle. Trends Pharmacol. Sci. 25: 388-393.
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 388-393
    • Karaki, H.1
  • 24
    • 0030910704 scopus 로고    scopus 로고
    • Targeted ablation of the phospholamban gene is associated with a marked decrease in sensitivity in aortic smooth muscle
    • Lalli, J., Harrer, J.M., Luo, W., Kranias, E.G. and Paul, R.J. (1997). Targeted ablation of the phospholamban gene is associated with a marked decrease in sensitivity in aortic smooth muscle. Circ. Res. 80: 506-513.
    • (1997) Circ. Res. , vol.80 , pp. 506-513
    • Lalli, J.1    Harrer, J.M.2    Luo, W.3    Kranias, E.G.4    Paul, R.J.5
  • 26
    • 0036362723 scopus 로고    scopus 로고
    • Relationship between the sarcoplasmic reticulum and the plasma membrane
    • Lee, C.H., Poburko, D., Kuo, K.H., Seow, C. and van Breemen, C. (2002). Relationship between the sarcoplasmic reticulum and the plasma membrane. Novartis Found. Symp. 246: 26-41; discussion 41-27, 48-51.
    • (2002) Novartis Found. Symp. , vol.246 , pp. 26-41
    • Lee, C.H.1    Poburko, D.2    Kuo, K.H.3    Seow, C.4    Van Breemen, C.5
  • 30
    • 0027422272 scopus 로고
    • ++-pump ATPase inhibit relaxation by nitroglycerin and atrial natriuretic factor of the rabbit aorta contracted by phenylephrine
    • ++-pump ATPase inhibit relaxation by nitroglycerin and atrial natriuretic factor of the rabbit aorta contracted by phenylephrine. J. Pharmacol. Exp. Ther. 265: 1187-1192.
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 1187-1192
    • Luo, D.L.1    Nakazawa, M.2    Ishibashi, T.3    Kato, K.4    Imai, S.5
  • 31
    • 0029144315 scopus 로고
    • Reciprocal regulation of cardiac Na-K-ATPase and Na/Ca exchanger: Hypertension, thyroid hormone, development
    • Magyar, C.E., Wang, J., Azuma, K.K. and McDonough, A.A. (1995). Reciprocal regulation of cardiac Na-K-ATPase and Na/Ca exchanger: hypertension, thyroid hormone, development. Am. J. Physiol. 269: C675-C682.
    • (1995) Am. J. Physiol. , vol.269
    • Magyar, C.E.1    Wang, J.2    Azuma, K.K.3    McDonough, A.A.4
  • 32
  • 34
    • 2142742940 scopus 로고
    • Movements of Ca in frog heart ventricles at rest and during contractures
    • Niedergerke, R. (1963). Movements of Ca in frog heart ventricles at rest and during contractures. J. Physiol. (Lond.) 167: 515-550.
    • (1963) J. Physiol. (Lond.) , vol.167 , pp. 515-550
    • Niedergerke, R.1
  • 35
    • 0035884612 scopus 로고    scopus 로고
    • Phospholamban regulation of bladder contractility: Evidence from gene-altered mouse models
    • Nobe, K., Sutliff, R.L., Kranias, E.G. and Paul, R.J. (2001). Phospholamban regulation of bladder contractility: evidence from gene-altered mouse models. J. Physiol. (Lond.) 535: 867-878.
    • (2001) J. Physiol. (Lond.) , vol.535 , pp. 867-878
    • Nobe, K.1    Sutliff, R.L.2    Kranias, E.G.3    Paul, R.J.4
  • 37
    • 0026467046 scopus 로고
    • Simultaneous presence of two distinct endoplasmic-reticulum-type calcium-pump isoforms in human cells. Characterization by radio-immunoblotting and inhibition by 2,5-di-(t-butyl)-1,4-benzohydroquinone
    • Papp, B., Enyedi, A., Paszty, K., Kovacs, T., Sarkadi, B., Gardos, G., Magnier, C., Wuytack, F. and Enouf, J. (1992). Simultaneous presence of two distinct endoplasmic-reticulum-type calcium-pump isoforms in human cells. Characterization by radio-immunoblotting and inhibition by 2,5-di-(t-butyl)-1,4- benzohydroquinone. Biochem. J. 288: 297-302.
    • (1992) Biochem. J. , vol.288 , pp. 297-302
    • Papp, B.1    Enyedi, A.2    Paszty, K.3    Kovacs, T.4    Sarkadi, B.5    Gardos, G.6    Magnier, C.7    Wuytack, F.8    Enouf, J.9
  • 38
    • 0036355978 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum and smooth muscle function: Evidence from transgenic mice
    • Paul, R.J., Shull, G.E. and Kranias, E.G. (2002). The sarcoplasmic reticulum and smooth muscle function: evidence from transgenic mice. Novartis Found. Symp. 246: 228-238; discussion 238-243, 272-226.
    • (2002) Novartis Found. Symp. , vol.246 , pp. 228-238
    • Paul, R.J.1    Shull, G.E.2    Kranias, E.G.3
  • 41
    • 0000045099 scopus 로고
    • Role of metabolism in K-induced tension changes in guinea pig taenia coli
    • Pfaffman, M., Urakawa, N. and Holland, W.C. (1965). Role of metabolism in K-induced tension changes in guinea pig taenia coli. Am. J. Physiol. 208: 1203-1205.
    • (1965) Am. J. Physiol. , vol.208 , pp. 1203-1205
    • Pfaffman, M.1    Urakawa, N.2    Holland, W.C.3
  • 42
    • 0033852625 scopus 로고    scopus 로고
    • Sodium-calcium exchange: A molecular perspective
    • Philipson, K.D. and Nicoll, D.A. (2000). Sodium-calcium exchange: a molecular perspective. Ann. Rev. Physiol. 62: 111-133.
    • (2000) Ann. Rev. Physiol. , vol.62 , pp. 111-133
    • Philipson, K.D.1    Nicoll, D.A.2
  • 48
    • 0034862131 scopus 로고    scopus 로고
    • Invited review: Mechanisms of calcium handling in smooth muscles
    • Sanders, K.M. (2001). Invited review: mechanisms of calcium handling in smooth muscles. J. Appl. Physiol. 91: 1438-1449.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1438-1449
    • Sanders, K.M.1
  • 50
    • 84960988768 scopus 로고
    • Herzglykoside als Hemmstoffe für den activen Kalium und Natrium-Transport durch die Erythrocytemembran
    • Schatzmann, H.J. (1953). Herzglykoside als Hemmstoffe für den activen Kalium und Natrium-Transport durch die Erythrocytemembran. Helv. Physiol. Pharmacol. Acta 11: 346-354.
    • (1953) Helv. Physiol. Pharmacol. Acta , vol.11 , pp. 346-354
    • Schatzmann, H.J.1
  • 51
    • 0018304863 scopus 로고
    • Mechanism of beta-adrenergic relaxation of smooth muscle
    • Scheid, C.R., Honeyman, T.W. and Fay, F.S. (1979). Mechanism of beta-adrenergic relaxation of smooth muscle. Nature 277: 32-36.
    • (1979) Nature , vol.277 , pp. 32-36
    • Scheid, C.R.1    Honeyman, T.W.2    Fay, F.S.3
  • 53
    • 0142039852 scopus 로고    scopus 로고
    • Regulation of vascular tone in animals overexpressing the sarcolemmal calcium pump
    • Schuh, K., Quaschning, T., Knauer, S., Hu, K., Kocak, S., Roethlein, N. and Neyses, L. (2003). Regulation of vascular tone in animals overexpressing the sarcolemmal calcium pump. J. Biol. Chem. 278: 41246-41252.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41246-41252
    • Schuh, K.1    Quaschning, T.2    Knauer, S.3    Hu, K.4    Kocak, S.5    Roethlein, N.6    Neyses, L.7
  • 55
    • 0014274422 scopus 로고
    • Effects of ouabain on calcium exchange and tension in taenia coli
    • Shimo, Y., Porter, M.T. and Holland, W.C. (1968). Effects of ouabain on calcium exchange and tension in taenia coli. Am. J. Physiol. 214: 804-807.
    • (1968) Am. J. Physiol. , vol.214 , pp. 804-807
    • Shimo, Y.1    Porter, M.T.2    Holland, W.C.3
  • 56
    • 0024459688 scopus 로고
    • Cell calcium and its regulation in smooth muscle
    • Somlyo, A.P. and Himpens, B. (1989). Cell calcium and its regulation in smooth muscle. FASEB J. 3: 2266-2276.
    • (1989) FASEB J. , vol.3 , pp. 2266-2276
    • Somlyo, A.P.1    Himpens, B.2
  • 58
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler, E.E. and Zacharias, D.A. (2001). Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81: 21-50.
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 59
    • 0033006097 scopus 로고    scopus 로고
    • Phospholamban is present in endothelial cells and modulates endothelium-dependent relaxation. Evidence from phospholamban gene-ablated mice
    • Sutliff, R.L., Hoying, J.B., Kadambi, V.J., Kranias, E.G. and Paul, R.J. (1999). Phospholamban is present in endothelial cells and modulates endothelium-dependent relaxation. Evidence from phospholamban gene-ablated mice. Circ. Res. 84: 360-364.
    • (1999) Circ. Res. , vol.84 , pp. 360-364
    • Sutliff, R.L.1    Hoying, J.B.2    Kadambi, V.J.3    Kranias, E.G.4    Paul, R.J.5
  • 60
    • 0035321725 scopus 로고    scopus 로고
    • Smooth muscle excitation-contraction coupling: A role for caveolae and caveolins?
    • Taggart, M.J. (2001). Smooth muscle excitation-contraction coupling: a role for caveolae and caveolins? News Physiol. Sci. 16: 61-65.
    • (2001) News Physiol. Sci. , vol.16 , pp. 61-65
    • Taggart, M.J.1
  • 61
    • 2042451621 scopus 로고    scopus 로고
    • Gene expression and functional activity of sodium/calcium exchanger enhanced in vascular smooth muscle cells of spontaneously hypertensive rats
    • Taniguchi, S., Furukawa, K., Sasamura, S., Ohizumi, Y., Seya, K. and Motomura, S. (2004). Gene expression and functional activity of sodium/calcium exchanger enhanced in vascular smooth muscle cells of spontaneously hypertensive rats. J. Cardiovasc. Pharmacol. 43: 629-637.
    • (2004) J. Cardiovasc. Pharmacol. , vol.43 , pp. 629-637
    • Taniguchi, S.1    Furukawa, K.2    Sasamura, S.3    Ohizumi, Y.4    Seya, K.5    Motomura, S.6
  • 62
    • 0035542931 scopus 로고    scopus 로고
    • Kinetics of inhibition of the plasma membrane calcium pump by vanadate in intact human red cells
    • Tiffert, T. and Lew, V.L. (2001). Kinetics of inhibition of the plasma membrane calcium pump by vanadate in intact human red cells. Cell Calcium 30: 337-342.
    • (2001) Cell Calcium , vol.30 , pp. 337-342
    • Tiffert, T.1    Lew, V.L.2
  • 67
    • 3042526077 scopus 로고    scopus 로고
    • Acetylcholine-related bowel dysmotility in homozygous mutant NCX/HOX11L.1-deficient (NCX-/-) mice-evidence that acetylcholine is implicated in causing intestinal neuronal dysplasia
    • Yanai, T., Kobayashi, H., Yamataka, A., Lane, G.J., Miyano, T., Hayakawa, T., Satoh, K., Kase, Y. and Hatano, M. (2004). Acetylcholine-related bowel dysmotility in homozygous mutant NCX/HOX11L.1-deficient (NCX-/-) mice-evidence that acetylcholine is implicated in causing intestinal neuronal dysplasia. J. Pediatr. Surg. 39: 927-930.
    • (2004) J. Pediatr. Surg. , vol.39 , pp. 927-930
    • Yanai, T.1    Kobayashi, H.2    Yamataka, A.3    Lane, G.J.4    Miyano, T.5    Hayakawa, T.6    Satoh, K.7    Kase, Y.8    Hatano, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.