Detection and Characterization of Novel Extracellular Phospholipase $A_2$ in Urine of Patients with Acute Pyelonephritis

  • Park, Jae-Hyeun (College of Pharmacy, Yeungnam University) ;
  • Lee, Jee-Hye (College of Pharmacy, Yeungnam University) ;
  • Baek, Suk-Hwan (College of Pharmacy, Yeungnam University) ;
  • Moon, Tae-Chul (College of Pharmacy, Yeungnam University) ;
  • Lee, Jong-Myung (Deparlment of Internal Medicine, School of Medicine Kyungpook National University) ;
  • Kim, Nung-Soo (IDeparlment of Internal Medicine, School of Medicine Kyungpook National University) ;
  • Nam, Kyung-Soo (Department of Pharmacology, College of Medicine, Dongguk University) ;
  • Chang, Hyeun-Wook (College of Pharmacy, Yeungnam University)
  • Received : 1996.12.15
  • Published : 1997.03.31


Extracellular phospholipase $A_2$ activity has been detected in urine of patients with acute pyelonephritis (APN). This enzyme required micromolar $Ca^{2+}$ ion for its maximum activity and showed a broad range of pH (4.5~10) optimum. Urine enzyme hydrolyzed phosphatidylethanolamine (PE) and phosphatidylserine (PS) more effectively than phosphatidylcholine (PC). $PLA_2$ activity in the urine of patients with APN was about 5-fold higher than that of healthy individuals. When urine was subjected to heparinSepharose column chromatography, phospholipase $A_2$ activity was detected in both heparin-non-binding and binding fractions. Both phospholipase $A_2$ activities were sensitive less than a micromolar calcium concentration and did not react with anti-human 14-kDa group II phospholipase $A_2$ monoclonal antibody, HP-l. These findings suggest that two kinds of novel extracellular phospholipase $A_2$. which may not belong to the 14-kDa group II phospholipase $A_2$ family, exist in the urine of patients with APN.


  1. Inflammation v.18 Andersen, S.;Sjursen, W.;Laegreid, A.;Volden, G.;Johansen, B.
  2. J. Biochem. v.97 Arai, H.;Inoue, K.;Natori, Y.;Banno, Y.;Nozawa, Y.;Nojima, S.
  3. J. Biochem. v.102 Chang, H.W.;Kudo, I.;Tomita, M.;Inoue, K.
  4. J. Biol. Chem. v.269 Dennis, E.A.
  5. J. Biol. Chem. v.147 Dijkstra, B.W.;Kalk, K.H.;Hol, E.G.;Drenth, J.
  6. J. Biol. Chem. v.253 Dole, V.P.;Meinertz, H.
  7. Cell Calcium v.4 Duraham, C.H.
  8. Proc. Natl. Acad. Sci. USA v.90 Fremont, D.H.;Aderson, D.;Wilson, I.A.;Dennis, E.A.;Xuong, N.H.
  9. J. Biochem. v.104 Hayakawa, M.;Horigome, K.;Kudo, I.;Tomita, M.;Inoue, K.
  10. J. Biochem. v.105 Hara, S.;Kudo, I.;Chang, H.W.;Matsuda, K.;Miyamoto, T.;Inoue, K.
  11. Biochim. Biophys. Acta v.1257 Hara, S.;Kudo, I.;Komatani, T.;Takahashi, K.;Nakatani, Y.;Natori, Y.;Ohshima, M.;Inoue, K.
  12. J. Biol. Chem. v.252 Heinrikson, R.L.;Kruger, E.T.;Keim, P.S.
  13. Anal. Biochem. v.157 Kaushal, V.;Barnes, L.D.
  14. Biophys. Biochem. Acta v.1083 Kim, D.K.;Kudo, K.;Inoue, K.
  15. Biochem. Biophys. Acta v.117 Kudo, I.;Murakami, M.;Hara, S.;Inoue, K.
  16. J. Biol. Chem. v.266 Oka, S.;Arita, H.
  17. J. Biol. Chem. v.263 Ono, T.;Tojo, H.;Kawamatsu, K.;Okamoto, M.
  18. Kidney Int. v.29 Schlondorff, D.;Aradaillou, R.
  19. Biochem. Biophys. Res. Commun. v.167 Takayama, K.;Kudo, I.;Hara, S.;Murakami, M.;Matsuda, M.;Miyamoto, T.;Inoue, K.
  20. J. Lipid Res. v.26 Waite, M.
  21. J. Biol. Chem. v.260 Wolf, R.A.;Gross, R.W.