Abstract
Calmodulin, a low molecular weight (16,700 dalton), heat-stable acidic protein, has been identified and isolated from a wide variety of tissues [1]. The protein displays multi-functions, controlling the activities of cyclic nucleotide phosphodiesterase [2, 3], adenylate cyclase [4, 5], Ca2+-ATPase [6, 7], myosin light chain kinase [8, 9], NAD kinase [10], phosphorylase kinase [11], and quanylate cyclase [12]. In addition, it regulates Ca2+ transport in erythrocytes and sarcoplasmic reticulum [13], phosphorylation of membrane proteins [14],and disassembly of microtubules [15]. Recently we have presented preliminary evidence suggesting that the stimulation of phospholipase A2, by Ca2+ in human blood platelet is mediated through calmodulin [16]. Phospholipase A2, controls the intracellular level of arachidonic acid, which is rate-limiting for the synthesis of thromboxane A2, a potent inducer of platelet aggregation and release reaction [17]. Thus, calmodulin may play an important role in platelet function.
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References
W. Y. Cheung, Science, 207: 19–27 (1980).
W. Y. Cheung, Biochem. Biophys. Res. Commun., 29: 478–482 (1967).
W. Y. Cheung, Biochem. Biophys. Res. Commun., 38: 533–538 (1970).
C. O. Brostrom, Y. C. Huang, B. M. Breckenridge, and D. J. Wolff, Proc. Natl. Acad. Sci., USA, 72: 64–68 (1975).
H. Charbonneau and M. J. Cormier, Biochem. Biophys. Res. Commun., 90: 1039–1047 (1979).
R. M. Gopinath and F. F. Vincenzi, Biochem. Biophys. Res. Commun., 77: 1203–1209 (1977).
H. W. Jarrett and J. T. Penniston, Biochem. Res. Commun., 77: 1210–1216 (1977).
R. Dabrowska, J. M. F. Sherry, D. K. Aromatorio, and D. J. Hartshorne, Biochemistry, 17: 253–258 (1978).
D. R. Hathaway and R. S. Adelstein, Proc. Natl. Acad. Sci., USA, 76: 1653–1657 (1979).
J. M. Anderson and M. J. Cormier, Biochem. Biophys. Res. Commun., 84: 595–602 (1978).
P. Cohen, A. Burchell, J. C. Foulkes, P. T. W. Cohen, T. C. Vanaman, and A. C. Nairn, FEBS Lett., 92: 287–293 (1978).
S. Nagao, Y. Suzuki, Y. Watanabe, and Y. Nozawal, Biochem. Biophys. Res. Commun., 90: 261–268 (1979).
T. R. Hinds, F. L. Larsen, and F. F. Vincenzi, Biochem. Biophys. Res. Commun., 81: 455–461 (1978).
H. Schulman and P. Greengard, Nature, 271: 478–479 (1978).
J. M. Marcum, J. R. Dedman, B. R. Brinkley, and A. R. Means, Proc. Natl. Acad. Sci., USA, 75: 3771–3775 (1978).
P. Y-K Wong and W. Y. Cheung, Biochem. Biophys. Res. Commun., 90: 473–480 (1979).
M. Hamburg, J. Svensson, and B. Samuelsson, Proc. Natl. Acad Sci., USA, 72: 2994–2998 (1975).
E. Anggard, C. Larsson, and B. Samuelsson, Acta. Physiol. Scand., 81: 396–412 (1971).
J. C. McGiff, N. A. Terragno, J. C. Strand, J. B. Lee, A. J. Lonigro, and K. K. F. Ng, Nature, 223: 742–747 (1962).
P. Y-K Wong, F. F. Sun, and J. C. McGiff, J. Biol. Chem., 253: 5555–5557 (1978).
R. Gorman, G. L. Bundy, D. C. Peterson, F. F. Sun, O. V. Miller, and F. A. Fitzpatrick, Proc. Natl. Acad. Sci., USA, 74: 4007–4011 (1977).
S. C. Lee and L. Levin, J. Biol. Chem., 250: 548–552 (1975).
O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem., 193: 265–275 (1951).
T. Yoshimoto, S. Yamamoto, and O. Hayaishi, Prostaglandins, 16: 529–540 (1978).
F. Fitzpatrick, R. Gorman, G. Bundy, T. Honohan, J. McGuire, and F. F. Sun, Biochim. Biophys. Acta, 573: 238–244 (1979).
J. A. Norman and B. Weiss, J. Pharmacol. Exptl. Ther., 208: 454–459 (1979).
W. C. Pickett, R. L. Jesse, and P. Cohen, Biochim. Biophys. Acta, 486: 209–213 (1977).
S. Rittenhouse-Simmons and D. Deykin, Biochim. Biophys. Acta, 543: 409–422 (1978).
G. A. Rodan and M. B. Feinstein, Proc. Natl. Acad. Sci., USA, 73: 1829–1833 (1976).
R. M. Lyons and J. O. Shaw, Journ. Clin. Invest., 65: 242–255 (1980).
M. B. Feinstein, J. Fiekers, and C. Fraser, Journ. Pharmacol. Exptl. Therap., 197: 215–228 (1976).
J. F. Mustard, D. W. Perry, R. L. Kinlough-Rathbone, and M. A. Packham, Am. J. Physiol., 228: 1757–1765 (1975).
S. H. Ferreira and J. R. Vane, Nature, 216: 868 (1967).
K. Bukhave, in: “Advances in Prostaglandin and Thromboxane Research,” Vol. 2 (B. Samuelsson and R. Paoletti, eds.), Raven Press, New York, p. 863 (1976).
M. Hamberg and B. Samuelsson, J. Biol. Chem., 246: 6713–6718 (1971).
J. Nakano and A. V. Prancan, Proc. Soc. Exp. Biol. Med., 144: 506–510 (1973).
P. Y-K Wong, P. H-W Chao, W. H. Lee, and W. Y. Cheung, in: Calmodulin and Cell Function, “Annals of New York Academy of Sciences, 356:179–189 (1980).
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© 1983 Plenum Press, New York
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Wong, P.YK. (1983). Calmodulin Regulates Thromboxane and Prostacyclin Biosynthesis and Metabolism. In: Berti, F., Folco, G., Velo, G.P. (eds) Leukotrienes and Prostacyclin. NATO Advanced Science Institutes Series, vol 54. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4391-2_11
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DOI: https://doi.org/10.1007/978-1-4684-4391-2_11
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