Abstract
From the point of view of protein structure and catalytic mechanism, phospholipases A2 (PLA2’s) are among the best characterized enzymes. Most of what is known about the structure and enzymology of PLA2 is based on studies using the enzymes purified from snake venom and mammalian pancreas (1, 2). Although it has been known for some time that PLA2 activity can be found in virtually every tissue and cell type (3, 4), these cellular PLA2’s are present in only trace amounts, and, until recently, efforts to purify and characterize them have been impeded. Thus, despite an extensive knowledge of the structure and enzymology of PLA2, based on the paradigm of the pancreatic and snake venom enzymes, much remains to be learned regarding different cellular forms of PLA2, their physiological roles, and how PLA2 activity is regulated in cells.
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References
Dennis, E.A. (1983) In: The Enzymes. Third Edition. Vol. 16, Boyer, P. (ed.). Academic Press, New York, pp.307–353.
Verheij, H.M., Slotbloom, A.J. and de Haas, G.H. (1981) Rev. Physiol. Biochem. Pharmacol. 91, 91–203.
Waite, M. (1985) J. Lipid Res. 26, 1379–1388.
Van den Bosch, H. (1980) Biochim. Biophvs. Acta 604, 191–246.
Dennis, E.A. (1987) Drug Dev. Res. 10, 205–220.
Ulevitch, R.J., Watanabe, Y., Sano, M., Lister, M.D., Deems, R.A. and Dennis, E.A. (1988) J. Biol. Chem. 263, 3079–3085.
Ono, T., Tojo, H., Kuramitsu, S., Kagamiyama, H. and Okamoto, M. (1988) J. Biol. Chem. 263, 5732–5738.
Aarsman, A.J., de Jong, J.G.N., Arnoldussen, E., Neys, F.W., van Wassenaar, P.D., and Van den Bosch, H. (1989) J. Biol. Chem. 2264, 10008–10014.
Hayakawa, M., Kudo, I., Tomita, M. and Inoue, K. (1988) J. Biochem. 103, 263–266.
Hayakawa, M., Kudo, I., Tomita, M., Nojima, S., and Inoue, K. (1988) J. Biochem. 104, 767–772.
Kramer, R.M., Wuthrich, C., Bollier, C., Allegrini, P.R. and Zahler, P. (1978) Biochim. Biophys. Acta 507, 381–394.
Okazaki, T., Sagawa, N., Bleasdale, J.E., Okita, J.R., MacDonald, P.C. and Johnston, J.M. (1981) Biol. of Reproduction 25, 103–109.
Levin, S.W., Butler, J.D., Schumacher, U.K., Wightman, P.D. and Mukherjee, A.B. (1986) Life Sciences 38, 1813–1819.
Wilson, T., Liggins, G.C., and Joe, L. (1989) Am. J. Obstet. Gynecol. 160, 602–606.
Lai, C.-Y., Wada, K. (1988) Biochem. & Biophvs. Res. Commun. 157, 488–493.
Wood, W.I., Gitschier, J., Laskey, L. A. and Lawn, R.M. (1985) Proc. Natl. Acad. Sci. 82, 1585–1588.
Silhavy, T.J., Berman, M.L. and Enquist, L.W. (1984) In: Experiments with Gene Fusions. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
Maniatis, T. Fritsch, E.F. and Sambrook, J. (1982) In: Molecular Cloning: a Laboratory Manual. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
Yanisch-Perron, C., Vieira J., and Messing J. (1985) Gene 33, 103–119.
Sanger, F., Nicklen, S. and Coulson, A.R. (1977) Proc. Natl. Acad. Sci. 74, 5463–5469.
Patriarca, P., Beckerdite, S. and Elsbach, P. (1972) Biochim. Biophvs. Acta 260, 593–600.
Cullen, B.R. (1987) Methods in Enzymology 152, 684–704.
Lathe, R. (1985) J. Mol. Biol. 183, 1–12.
Verheij, H.M., Westerman, J., Sternby, B., and De Haas, G. (1983) Biochim. Biophys. Acta 747, 93–99.
Seilhamer, J.J., Randall, T.L., Yamanaka, M., and Johnson, L.K. (1986) DNA 5, 519–527.
Tsai, I.H., Wu, S.H. and Lo T.B. (1981) Toxicon 19, 141–152.
Randolph, A. and Heinrikson, R.L. (1982) J. Biol. Chem. 257, 2155–2161.
Heinrikson, R.L., Kreuger, E.T. and Keim, P.S. (1977) J. Biol. Chem. 252, 4913–4921.
Cho, W., Tomasselli, A.G., Heinrikson, R.L., and Kezdy, F.J. (1988) J Biol. Chem. 263, 11237–11241.
Tomasselli, A.G., Hui, J., Fisher, J., Zürcher-Neely, H., Reardon, I.M., Oriaku, E., Kézdy, F.J. and Heinrikson, R.L. (1989) J. Biol. Chem. 264, 10041–10047.
Seilhamer, J.J., Pruzanski, W., Vadas, P., Plant. S., Miller, J.A., Kloss, J., and Johnson, L.K. (1989) J. Biol. Chem. 264, 5335–5338.
Kramer, R.M., Hession, C., Johanson, B., Hayes, G., McGray, P., Chow, E.P., Tizard, R., and Pepinsky, R.B. (1989) J. Biol. Chem. 264. 5768–5775.
Gallai-Hatchard, J.J. and Thompson, R.H.S. (1965) Biochim. Biophys. Acta 98, 128–135.
Ohara, O., Tamaki, M., Nakamura, E., Tsuruta, Y., Fujii, Y., Shin, M., Teraoka, H. and Okamoto, M. (1986) J. Biochem. 99, 733–739.
Ishizaki, J., Ohara, 0., Nakamura, E., Tamaki, M., Ono, T., Kanda, A., Yoshida, N., Teraoka, H., Tojo, H. and Okamoto, M. (1989) Biochem. & Biophvs. Res. Commun. 162, 1030–1036.
Andreadis, A., Gallego, M.E. and Nadal-Ginard, B. (1987) Ann. Rev. Cell Biol. 3, 207–242.
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Crowl, R., Stoner, C., Stoller, T., Pan, YC., Conroy, R. (1990). Isolation and Characterization of cDNA Clones from Human Placenta Coding for Phospholipase A2 . In: Mukherjee, A.B. (eds) Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors. Advances in Experimental Medicine and Biology, vol 279. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0651-1_11
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DOI: https://doi.org/10.1007/978-1-4613-0651-1_11
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