DETECTION AND SUBCELLULAR-LOCALIZATION OF RABBIT PLATELET PHOSPHOLIPASE-A2 WHICH PREFERENTIALLY HYDROLYZES AN ARACHIDONOYL RESIDUE

被引:37
作者
KIM, DK [1 ]
KUDO, I [1 ]
FUJIMORI, Y [1 ]
MIZUSHIMA, H [1 ]
MASUDA, M [1 ]
KIKUCHI, R [1 ]
IKIZAWA, K [1 ]
INOUE, K [1 ]
机构
[1] UNIV TOKYO,FAC PHARMACEUT SCI,TOKYO 113,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123311
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Like rat platelets, rabbit platelets contain a secretory 14-kDa group II phospholipase A2 [Mizushima, H., Kudo, I., Horigome, K., Murakami, M., Hayakawa, M., Kim, D.K., Kondo, E., Tomita, M., & Inoue, K. (1989) J. Biochem. 105, 520-525]. The present study was undertaken to determine whether or not, in addition to that of the 14-kDa group II enzyme, rabbit platelets exhibit another phospholipase A2 activity. A rabbit platelet soluble fraction was prepared by sonication and centrifugation. When this soluble fraction was subjected to heparin-Sepharose column chromatography, phospholipase A2 activity was detected in both heparin-binding and heparin-non-binding fractions. The activity detected in the heparin-binding fraction appeared to belong to the secretory 14-kDa phospholipase A2, because it bound to anti-human 14-kDa group II phospholipase A2 monoclonal antibody. The activity found in the heparin-non-binding fraction did not appreciably react with the same antibody. When platelets were gently disrupted by the nitrogen cavitation method, the heparin-non-binding activity was mainly recovered in the platelet cytosolic fraction. The heparin-non-binding phospholipase A2 hydrolyzed a phospholipid bearing an arachidonoyl residue at the sn-2 position more effectively than one with a linoleoyl residue. The biochemical features of the activity observed in the heparin-non-binding fraction generally resembled those of human platelet soluble phospholipase A2 [Kim, D.K., Kudo, I., & Inoue, K. (1988) J. Biochem. 104, 492-494]. It can be concluded that rabbit platelets contain two kinds of phospholipase A2; one is the secretory 14-kDa group II phospholipase A2 in the granule fraction and the other is a cytosolic phospholipase A2 with a preference for arachidonoyl residues. © 1990 Copyright, 1990 by the Journal of Biochemistry.
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页码:903 / 906
页数:4
相关论文
共 21 条
[1]  
AARSMAN AJ, 1989, J BIOL CHEM, V264, P10008
[2]   A CYTOSOLIC PHOSPHOLIPASE IN HUMAN-NEUTROPHILS THAT HYDROLYZES ARACHIDONOYL-CONTAINING PHOSPHATIDYLCHOLINE [J].
ALONSO, F ;
HENSON, PM ;
LESLIE, CC .
BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 878 (02) :273-280
[3]   PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR PHOSPHOLIPASE-A2 FROM PERITONEAL-CAVITY OF CASEINATE-TREATED RAT [J].
CHANG, HW ;
KUDO, I ;
TOMITA, M ;
INOUE, K .
JOURNAL OF BIOCHEMISTRY, 1987, 102 (01) :147-154
[4]   STRUCTURAL AND FUNCTIONAL-PROPERTIES OF A PHOSPHOLIPASE-A2 PURIFIED FROM AN INFLAMMATORY EXUDATE [J].
FORST, S ;
WEISS, J ;
ELSBACH, P ;
MARAGANORE, JM ;
REARDON, I ;
HEINRIKSON, RL .
BIOCHEMISTRY, 1986, 25 (26) :8381-8385
[5]   PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR PHOSPHOLIPASE-A2 FROM HUMAN SYNOVIAL-FLUID IN RHEUMATOID-ARTHRITIS [J].
HARA, S ;
KUDO, I ;
CHANG, HW ;
MATSUTA, K ;
MIYAMOTO, T ;
INOUE, K .
JOURNAL OF BIOCHEMISTRY, 1989, 105 (03) :395-399
[6]   PURIFICATION AND CHARACTERIZATION OF MEMBRANE-BOUND PHOSPHOLIPASE-A2 FROM RAT PLATELETS [J].
HAYAKAWA, M ;
KUDO, I ;
TOMITA, M ;
INOUE, K .
JOURNAL OF BIOCHEMISTRY, 1988, 103 (02) :263-266
[7]   PURIFICATION AND CHARACTERIZATION OF PHOSPHOLIPASE-A2 RELEASED FROM RAT PLATELETS [J].
HORIGOME, K ;
HAYAKAWA, M ;
INOUE, K ;
NOJIMA, S .
JOURNAL OF BIOCHEMISTRY, 1987, 101 (03) :625-631
[8]   SELECTIVE RELEASE OF PHOSPHOLIPASE-A2 AND LYSOPHOSPHATIDYLSERINE-SPECIFIC LYSOPHOSPHOLIPASE FROM RAT PLATELETS [J].
HORIGOME, K ;
HAYAKAWA, M ;
INOUE, K ;
NOJIMA, S .
JOURNAL OF BIOCHEMISTRY, 1987, 101 (01) :53-61
[9]  
KAUSHAL V, 1986, ANAL BIOCHEM, V235, P2595
[10]   DETECTION IN HUMAN-PLATELETS OF PHOSPHOLIPASE-A2 ACTIVITY WHICH PREFERENTIALLY HYDROLYZES AN ARACHIDONOYL RESIDUE [J].
KIM, DK ;
KUDO, I ;
INOUE, K .
JOURNAL OF BIOCHEMISTRY, 1988, 104 (04) :492-494