Abstract
The title of this chapter was chosen to emphasize a point, namely, that PLs are classified as a group solely on the basis that they hydrolyze phospholipids. Beyond this commonality, this is a diverse group of enzymes, both in structure and in function.1 One or more of these enzymes have been described in almost every, if not all organisms analyzed for their presence. The sites of hydrolysis and nomenclature for the PLs are given in Fig. 1.
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References
M. Waite, The Phospholipases, in: “Handbook of Lipid Research,” D. J. Hanahan, ed., vol. 5, 332 pages, Plenum Publishing Corporation, New York (1987).
H. van den Bosch, A. J. Aarsman, A. J. Slotboom, andL. L. M. van Deenen, On the specificity of rat liver lysophospholipase Biochim. Biophys. Acta 164:215 (1968).
R. M. Kramer, C. R. Pritzker, and D. Deykin, Coenzyme A-mediated arachidonic acid transacylation in human platelets, J. Biol. Chem. 259:2403 (1984).
C. E. Walsh, M. Waite, M. J. Thomas, and L. R. DeChatelet, Release and metabolism of arachidonic acid in human neutrophils, J. Biol. Chem. 256:7228 (1981).
M. R. Hokin, and L. E. Hokin, The role of phosphatidic acid and phosphoinositide in transmembrane transport elicited by acetylcholine and other humoral agents, Int. Rev. Neurobiol. 2:99 (1960).
L. W. Daniel, M. Waite, and R. L. Wykle, A novel mechanism of diglyceride formation: 12–0-tetradecanoyl-phorbol-13-acetate stimulates the cyclic breakdown and resynthesis of phosphatidylcholine J. Biol. Chem. 261:9128 (1986).
J.-K. Pai, M. I. Siegel, R. W. Egan, and M. Billah, Phospholipase D catalyzes phospholipid metabolism in chemotactic peptide-stimulated HL-60 granulocytes, J. Biol. Chem. 263:12472 (1988).
W. Siess, P. C. Weber, and E. G. Lapetina, Activation of phospholipase C is dissociated from arachidonate metabolism during platelet shape change induced by thrombin or platelet-activating factor: epinephrine does not induce phospholipase C activation or platelet shape change, J. Biol. Chem. 259:8286 (1984).
S. F. Rittenhouse, Activation of human platelet phospholipase C by ionophore A23187 is totally dependent upon cyclo-oxygenase products and ADP, Biochem. J. 222:103 (1984).
G. Lindblom, and L. Rilfors, Cubic phases and isotropic structures formed by membrane lipids — possible biological relevance, Biochim. Biophys. Acta 988:221 (1989).
H. B. M. Lenting, K. Nicolay, and H. van den Bosch, Regulatory aspects of mitochondrial phospholipase A2: correlation of hydrolysis rates with substrate configuration as evidenced by 31P-NMR, Biochim. Biophys. Acta 958:405 (1988).
M. Robinson, and M. Waite, Physical-chemical requirements for the catalysis of substrates by lysosomal phospholipase A1 J. Biol. Chem. 258:14371 (1983).
F. Pattus, A. J. Slotboom, and G. H. deHaas, Regulation of phospholipase A2 activity by the lipid-water interface: a monolayer approach, Biochemistry 18:2691 (1979).
M. C. Komaromy, and M. C. Schotz, Cloning of rat hepatic lipase cDNA: evidence for a lipase gene family, Proc. Natl. Acad. Sci. USA 84:1526 (1987)
T. Kuwae, P. C. Schmid, and H. H. O. Schmid, Assessment of phospholipid deacylation-reacylation cycles by a stable isotope technique, Biochem. Biophys. Res. Commun. 142:86 (1987).
F. R. Cochran, V. L. Roddick, J. R. Connor, J. T. Thornburg, and M. Waite, Regulation of arachidonic acid metabolism in resident and BCG-activated macrophages: role of lyso(bis)phosphatidic acid, J. Immunol. 138:1877 (1987).
N. Kawasaki, and K. Saito, Purification and some properties of lysophospholipase from Penicillium notatum, Biochim. Biophys. Acta 296:426 (1973).
N. Kawasaki, J. Sugatani, and K. Saito, Studies on a phospholipase B from Penicillium notatum, J. Biochem. 77:1233 (1975).
H. van den Bosch, Phospholipases, In: “Phospholipids,” J. N. Hawthorne and G. B. Ansell, eds., vol. 4, pp. 313–357, Elsevier Biomedical, Amsterdam (1982).
K. Saito, and M. Kates, Substrate specificity of a highly-purified phospholipase B from Penicillium notatum, Biochim. Biophys. Acta 369:245 (1974).
M. Waite, and P. Sisson, Studies on the substrate specificity of the phospholipase A1 of the plasma membrane of rat liver, J. Biol. Chem. 249:6401 (1974).
R. W. Gross, and B. E. Sobel, Rabbit myocardial cytosolic lysophospholipase: purification, characterization, and competitive inhibition by L-palmitoyl carnitine, J. Biol. Chem. 258:5221 (1983).
R. W. Gross, R. C. Drisdel, and B. E. Sobel, Rabbit myocardial lysophospholipase-transacylase: purification, characterization, and inhibition by endogenous cardiac amphiphiles, J. Biol. Chem. 258:15165 (1983).
A. J. Slotboom, H. M. Verheij, and G. H. deHaas, On the mechanism of phospholipase A2, in: “Phospholipids,” J. N. Hawthorne and G. B. Ansell, eds., vol. 4, ch. 10, pp. 359–434, Elsevier Biomedical, Amsterdam (1982).
R. L. Heinrikson, E. T. Krueger, and P. S. Keim, Amino acid sequence of phospholipase A2-α from the venom of Crotalus adamanteus: a new classification of phospholipase A2 based upon structural determinants, J. Biol. Chem. 252:4913 (1977).
H. Tojo, T. Ono, S. Kuramitsu, H. Kagamiyama, and M. Okamoto, A phospholipase A2 in the supernatant fraction of rat spleen: its similarity to rat pancreatic phospholipase A2, J. Biol. Chem. 263:5724(1988)
T. Ono, H. Tojo, S. Kuramitsu, H. Kagamiyama, and M. Okamoto, Purification and characterization of a membrane-associated phospholipase A2 from rat spleen: its comparison with a cytosolic phospholipase A2 S-1, J. Biol. Chem. 263:5732 (1988).
O. Ohara, M. Tamaki, E. Nakamura, Y. Tsuruta, Y. Fujii, M. Shin, H. Teraoka, and M. Okamoto, Dog and rat pancreatic phospholipases A2: complete amino acid sequences deduced from complementary DNAs, J. Biochem. 99:733 (1986).
H. Tojo, T. Ono, and M. Okamoto, A pancreatic-type phospholipase A2 in rat gastric mucosa, Biochem. Biophys. Res. Commun. 151:1188 (1988).
A. J. Aarsman, J. G. N. deJong, E. Arnoldussen, F. W. Neys, P. D. van Wassenaar, and H. van den Bosch, Immunoaffinity purification, partial sequence, and subcellular localization of rat liver phospholipase A2, J. Biol. Chem. 264:10008 (1989).
S. Hara, I. Kudo, K. Matsuta, T. Miyamoto, and K. Inoue, Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid, J. Biochem. 104:326 (1988).
R. M. Kramer, C. Hess ion, B. Johansen, G. Hayes, P. McGray, E. P. Chow, R. Tizard, and R. B. Pepinsky, Structure and properties of a human non-pancreatic phospholipase A2, J. Biol. Chem. 264:5768 (1989).
C.-Y. Lai, and K. Wada, Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme, Biochem. Biophys. Res. Commun. 157:488 (1988).
J. J. Seilhamer, T. L. Randall, M. Yamanaka, and L. K. Johnson, Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung, DNA 5:519 (1986).
H. M. Verheij, J. Westerman, B. Sternby, and G. H. deHaas, The complete primary structure of phospholipase A2 from human pancreas, Biochim. Biophys. Acta 747:93 (1983).
H. W. Chang, I. Kudo, M. Tomita, and K. Inoue, Purification and characterization of extracellular phospholipase A2 from peritoneal cavity of caseinate-treated rat, J. Biochem. 102:147 (1987)
M. Hayakawa, K. Horigome, I. Kudo, M. Tomita, S. Nojima, and K. Inoue, Amino acid composition and NH2-terminal amino acid sequence of rat platelet secretory phospholipase A2, J. Biochem. 101:1311 (1987).
H. Mizushima, I. Kudo, K. Horigome, M. Murakami, M. Hayakawa, D.-K. Kim, E. Kondo, M. Tomita, and K. Inoue, Purification of rabbit platelet secretory phospholipase A2 and its characteristics, J. Biochem. 105:520 (1989).
S. Forst, J. Weiss, and P. Elsbach, Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate, Biochemistry 25:8381 (1986).
G. C. Wright, C. E. Ooi, J. Weiss, and P. Elsbach, Purification of a cellular (granulocyte) and an extracellular (serum) phospholipase A2 that participate in the destruction of Escherichia coli in a rabbit inflammatory exudate, J. Biol. Chem., submitted (1989).
M. J. Dufton, and R. C. Hider, Classification of phospholipases A2 according to sequence: evolutionary and pharmacological implications, Eur. J. Biochem 137:5454 (1983).
C. J. van den Bergh, A. J. Slotboom, H. M. Verheij, and G. H. deHaas, The role of aspartic acid-49 in the active site of phospholipase A2: a site-specific mutagenesis study of porcine pancreatic phospholipase A2 and the rationale of the enzymatic activity of [ lysine49 ]-phospholipase A2 Agkistrodon piscivorus piscivorus’ venom, Eur. J. Biochem. 176:353 (1988).
C. J. van den Bergh, A. C. A. P. A. Bekkers, H. M. Verheij, and G. H. deHaas, Glutamic acid 71 and aspartic acid 66 control the binding of the second calcium ion in porcine pancreatic phospholipase A2, Eur. J. Biochem. 182:307 (1989).
P. Kuipers, R. Dijkman, C. E. G. M. Pals, H. M. Verheij, and G. H. deHaas, Evidence for the involvement of tyrosine-69 in the control of stereospecificity of porcine pancreatic phospholipase A2, Protein Engr. 2:467 (1989).
P. Kuipers, M. M. G. M. Thunnissen, P. deGeus, B. W. Dijkstra, J. Drenth, H. M. Verheij, and G. H. deHaas, Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop, Science 244:82 (1989).
L. A. Loeb, and R. W. Gross, Identification and purification of sheep platelet phospholipase A2 isoforms: activation by physiologic concentrations of calcium ion, J. Biol. Chem. 261:10467 (1986).
Y. Suwa, I. Kudo, M. Okada, A. Imaizumi, Y. Suzuki, H. W. Chang, and K. Inoue, Novel proteinous inhibitors of phospholipase A2 purified from rat inflamed sites, submitted (1989).
F. F. Davidson, E. A. Dennis, M. Powell, and J. Glenney, Inhibition of phospholipase A2 by “lipocortins” and calpactins: an effect of binding to substrate phospholipids, J. Biol. Chem. 262:1698 (1987).
P. Elsbach, and J. Weiss, Phagocytosis of bacteria and phospholipid degradation, Biochim. Biophys. Acta 947:29 (1988).
K. Aalmo, L. Hansen, E. Hough, K. Jynge, J. Krane, C. Little, and C. B. Storm, An anion binding site in the active centre of phospholipase C from Bacillus cereus, Biochem. Int. 8:27 (1984).
D. P. Siegel, J. Banschbach, D. Alford, H. Ellens, L. J. Lis, P. J. Quinn, P. L. Yeagle, and J. Bentz, Physiological levels of diacylglycerols in phospholipid membranes induce membrane fusion and stabilize inverted phases, Biochemistry 28:3703 (1989).
S. G. Rhee, P.-G. Suh, S.-H. Ryu, and S. Y. Lee, Studies of inositol phospholipid-specific phospholipase C, Science 244:546 (1989).
R. A. Wolf, and R. W. Gross, Identification of neutral active phospholipase C which hydrolyzes choline glycerophospholipids and plasmalogen selective phospholipase A2 in canine myocardium, J. Biol. Chem. 260:7296.
G. Augert, S. B. Bocckino, P. F. Blackmore, and J. H. Exton, Hormonal stimulation of diacylglycerol formation in hepatocytes: evidence for phosphatidylcholine breakdown, J. Biol. Chem., in press (1989).
A. H. Merrill, Lipid modulators of cell function, Nutr. Rev. 47:161 (1989).
R. N. Kolesnick, 1, 2-Diacylglycerols but not phorbol esters stimulate sphingomyelin hydrolysis in GH3 pituitary cells, J. Biol. Chem. 262:16759 (1987).
R. N. Kolesnick, Sphingomyelinase action inhibits phorbol ester-induced differentiation of human promyelocytic leukemic (HL-60) cells, J. Biol. Chem. 264:7617 (1989).
H. Ikezawa, M. Yamanegi, R. Taguchi, T. Miyashita, and T. Ohyabu, Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. I. Purification, properties and phosphatase-releasing activity, Biochim. Biophys. Acta 450:154 (1976).
M. G. Low, Degradation of glycosyl-phosphatidylinositol anchors by specific phospholipases, in: “Glycosylphosphatidylinositol Membrane Protein Anchors and Cell Signalling Events,” A. J. Turner, ed., ch. 2, Ellis Horwood Publ., U.K., in press (1989).
M. G. Low, and A. R. Saltiel, Structural and functional roles of glycosylphosphatidylinositol in membranes, Science 239:268 (1988).
R. Bulow, and P. Overath, Purification and characterization of the membrane-form variant surface glycoprotein hydrolase of Trypanosoma brucei, J. Biol. Chem. 261:11918 (1986).
J. A. Fox, N. M. Soliz, and A. R. Saltiel, Purification of a phosphatidylinositol-glycan-specific phospholipase C from liver plasma membranes: a possible target of insulin action, Proc. Natl. Acad. Sci. USA 84:2663 (1987).
J. N. Kanfer, The base exchange enzymes and phospholipase D of mammalian tissue, Can. J. Biochem. 58:1370 (1980).
R. L. Wykle, and J. M. Schremmer, A lysophospholipase D pathway in the metabolism of ether-linked lipids in brain microsomes, J. Biol. Chem. 249:1742 (1974).
S. B. Bocckino, P. F. Blackmore, P. B. Wilson, and J. H. Exton, Phosphatidate accumulation in hormone-treated hepatocytes via a phospholipase D mechanism, J. Biol. Chem. 262:15309 (1987).
M. A. Davitz, J. Horn, and S. Schenkman, Purification of a glycosylphosphatidylinositol-specific phospholipase D from human plasma, J. Biol. Chem. 264:13760 (1989).
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Waite, M. (1990). Phospholipases, Enzymes That Share a Substrate Class. 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_1
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DOI: https://doi.org/10.1007/978-1-4613-0651-1_1
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