A β-lactam inhibitor of cytosolic phospholipase A2 which acts in a competitive, reversible manner at the lipid/water interface

Journal of Enzyme Inhibition

Volumn 13, Issue 3, 1998, Pages 195-206

  Burke, James R ^a,b   Gregor, Kurt R ^a   Padmanabha, Ramesh ^a   Banville, Jacques ^a   Witmer, Mark R ^a,b   Davern, Lynda B ^a   Manly, Susan P ^a   Tramposch, Kenneth M ^a  

^a Dept of Dermatol Discov Research ^*  (United States)

^b BRISTOL MYERS SQUIBB   (United States)

Author keywords

Cytosolic phospholipase A2; Inhibition; Interfacial catalysis

Indexed keywords

ARACHIDONIC ACID; BETA LACTAM; CELL ENZYME; ENZYME INHIBITOR; PHOSPHOLIPASE A2; PHOSPHOLIPASE A2 INHIBITOR; PHOSPHOLIPID;

ARACHIDONIC ACID METABOLISM; ARTICLE; BILAYER MEMBRANE; COMPETITIVE INHIBITION; CONTROLLED STUDY; DISSOCIATION CONSTANT; DOSE RESPONSE; DRUG DEGRADATION; DRUG MECHANISM; DRUG POTENCY; DRUG SELECTIVITY; DRUG SYNTHESIS; ENZYME ACTIVE SITE; ENZYME ASSAY; HUMAN; PRIORITY JOURNAL;

THIA;

EID: 0031774708     PISSN: 87555093     EISSN: None     Source Type: Journal    
DOI: 10.3109/14756369809028340     Document Type: Article

References (38)

1. Diez, E., Louis-Flamberg, P., Hall, R.H. and Mayer, R.J. (1992). J. Biol. Chem., 267, 18342.
2. Diez, E., Chilton, F.H., Stroup, G., Mayer, R.J., Winkler, J.D. and Fonteh, A.N. (1994). Biochem. J., 301, 721.
3. Nakamura, T., Lin, L -L , Kharbanda, S., Knopf, J.L. and Kufe, D. (1992). EMBO J., 11, 4917.
4. Kramer, R.M., Roberts, E.F., Manetta, J.V., Hyslop, P.A. and Jakubowski, J.A. (1993). J. Biol. Chem., 268, 26796.
5. Ramesha, C.S. and Ives, D.L. (1993). Biochim. Biophys. Acta, 1168, 37.
6. Channon, J.Y. and Leslie, C.C. (1990). J. Biol Chem., 265, 5409.
7. Clark, J.D , Lin, L -L., Kriz, R.W., Ramesha, C.S., Sultzman, L.A., Lin, A.Y., Milona, N. and Knopf, J.L (1991). Cell, 65, 1043.
8. Schievella, A.R., Regier, M.K., Smith, W.L. and Lin, L.-L. (1995). J. Biol. Chem., 270, 30749.
9. Burke, J.R., Guenther, M G., Witmer, M.R., Tredup, J.A., Micanovic, R. and Villafranca, J.J. (1997) Arch. Biochem. Biophys., 341, 177.
10. Burke, J.R., Davern, L.B., Gregor, K.R., Todderud, G., Alford, J.G. and Tramposch, K.M. (1997). Biochim. Biophys. Acta, 1341, 223.
11. Burke, J.R., Witmer, M.R., Tredup, J., Micanovic, R., Gregor, K., Lahiri, J., Tramposch, K.M. and Villafranca, J J. (1995). Biochemistry, 34, 15165.
12. Sharp, J.D., Pickard, R.T., Chiou, X.G., Manetta, J.V., Kovacevic, S., Miller, J.R., Varshavsky, A.D., Roberts, E.F., Strifler, B.A., Brems, D.N. and Kramer, R.M. (1994). J. Biol. Chem., 269, 23250.
13. Huang, Z., Laliberte, F , Tremblay, N M., Weech, P.K. and Street, I.P. (1994). Anal. Biochem., 222, 110.
14. Reynolds, L.J., Hughes, L.L., Louis, A.I., Kramer, R.M. and Dennis, E.A. (1993). Biochim. Biophys. Acta, 1167, 272.
15. Hanel, A.M. and Gelb, M.H. (1995). Biochemistry, 34, 7807.
16. Street, I.P., Lin, H.-K., Laliberte, F., Ghomaschchi, F., Wang, Z., Perrier, H., Tremblay, N.M., Huang, Z., Weech, P.K. and Gelb, M.H. (1993). Biochemistry, 32, 5935.
17. Trimble, L.A., Street, I.P., Perrier, H., Tremblay, N.M., Weech, P.K. and Bernstein, M.A. (1993). Biochemistry, 32, 12560.
18. Ulevitch, R.J., Watanabe, Y., Sano, M., Lister, M.D., Deems, R.A. and Dennis, E.A. (1988). J. Biol. Chem , 263, 3079.
19. Verger, R. (1980). Meth. Enzymol., 64, 340-392.
20. Nalefski, E.A., Sultzman, L.A., Martin, D.M., Kriz, R W., Towler, P.S., Knopf, J.L. and Clark, J.D. (1994). J Biol. Chem., 269, 18239.
21. Ramirez, F. and Jain, M K. (1991). Proteins, 9, 229.
22. Yu, L. and Dennis, E.A. (1992) Bioorg. Med. Chem. Lett., 2, 1343.
23. Berg, O.G., Yu, B.Z., Rogers, J. and Jain, M.K. (1991). Biochemistry, 30, 7283.
24. Gelb, M.K., Jain, M.K. and Berg, O. (1992). Bioorg. Med. Chem. Lett., 2, 1335.
25. Rasmupathi, R. and Franson, R C. (1987). Fed. Proc., 46, 1945
26. Jain, M.K , Yuan, W. and Gelb, M.H. (1989) Biochemistry, 28, 4135.
27. Jain, M.K and Gelb, M H (1991). Meth Enzymol., 197, 112.
28. Tramposch, K.M , Sterner, S.A , Stanley, P L , Nettleton, D.O., Franson, R D., Lewin, A.H. and Carroll, F.I (1992). Biochem Biophys. Res. Commun., 189, 272.
29. Jain, M.K., Rogers, J., Jahagirdar, D.V., Marecek, J.F. and Ramirez, F. (1986). Biochem. Biophys. Acta, 860, 435.
30. Glaser, K.B., Mobilio, D., Chang, J.Y. and Senko, N. (1993). Trends Pharm. Sci., 14, 92.
31. Silverman, R.B. (1992). The Organic Chemistry of Drug Design and Drug Action, pp 181-185. San Diego: Academic Press.
32. Jung, M.J. and Metcalf, B.W. (1975). Biochem. Biophys. Res. Commun., 67, 301.
33. Burke, J.R., Gregor, K.R. and Tramposch, K.M. (1995). J. Biol. Chem., 270, 274.
34. Natto, T., Nakagawa, S., Okumura, J., Konishi, M. and Kawaguchu, H. (1965). J. Antibiotics, Ser. A., 18, 145.
35. Burke, J.R., Witmer, M.R., Tredup, J., Micanovic, R., Gregor, K., Lahiri, J., Tramposch, K.M. and Villafranca, J.J. (1997). Biochemistry, 36, 6854.
36. This equation is valid since the active site dissociation constant for DMPM has been shown to be more than 330-times greater than the value for PAPC (see Reference 35).
37. M is the active site dissociation constant for DMPM at the interface (see Reference 35).
38. o in equation (1) equals the mole fraction of substrate phospholipid without inhibitor. The mole fraction of substrate in the presence of the inhibitor is correspondingly less.