PREFERENTIAL DISTRIBUTION OF GROUP-II-LIKE PHOSPHOLIPASE-A2 IN MONONUCLEAR PHAGOCYTIC-CELLS IN RAT SPLEEN AND LIVER

被引:41
作者
INADA, M [1 ]
TOJO, H [1 ]
KAWATA, S [1 ]
TARUI, S [1 ]
OKAMOTO, M [1 ]
机构
[1] OSAKA UNIV, SCH MED, DEPT MOLEC PHYSIOL CHEM, OSAKA, JAPAN
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 197卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1991.tb15914.x
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
The localization of calcium-dependent phospholipase A2, (PLA2) immunochemically closely related to the enzyme of the viperid and crotalid type (group II), in cells isolated from rat spleen and liver was examined using a polyclonal antibody directed against rat spleen group II, PLA2 (PLA2M). In isolated spleen cells, the monocyte/macrophage fraction had the highest PLA2 activity (1.28 +/- 0.35 . min-1 . 10(6) cells-1) which was almost completely inhibited by the anti-PLA2M antibody. An immunoblot analysis confirmed the presence of the enzyme in this fraction. An immunocytochemical study revealed that the PLA2 was present in spleen macrophages. In the isolated liver cells, Kupffer cells (0.92 +/- 0.22 nmol . min-1 . 10(6) cells-1) contained higher anti-PLA2M-antibody-inhibitable PLA2 activity than parenchymal cells (0.26 +/- 0.06 . min-1 . 10(6) cells-1). The immunocytochemical study showed that cells immunopositive with anti PLA2M antibody were Kupffer cells. These results suggest that the mononuclear phagocytic cells in rat spleen and liver have relatively high activity of group-II-like PLA2. Subcellular distribution patterns of the anti-PLA2M-antibody-inhibitable phospholipase A2 activity in different cell populations from spleen and liver were compared. A mode of the distribution of the enzyme in the spleen macrophages was essentially similar to that in the spleen lymphocytes. The distribution in Kupffer cells was similar to that in parenchymal cells.
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页码:323 / 329
页数:7
相关论文
共 34 条
[1]  
AARSMAN AJ, 1989, J BIOL CHEM, V264, P10008
[2]   BIOSYNTHESIS OF PROSTAGLANDINS IN PARENCHYMAL AND NON-PARENCHYMAL RAT-LIVER CELLS [J].
BARTOLINI, G ;
MERINGOLO, C ;
ORLANDI, M ;
TOMASI, V .
BIOCHIMICA ET BIOPHYSICA ACTA, 1978, 530 (03) :325-332
[3]   SUCCINIC DEHYDROGENASE [J].
BERNATH, P ;
SINGER, TP .
METHODS IN ENZYMOLOGY, 1962, 5 :597-614
[4]   SYNTHESIS OF PROSTANOIDS AND CYCLIC-NUCLEOTIDES BY PHAGOCYTOSING RAT KUPFFER CELLS [J].
BIRMELIN, M ;
DECKER, K .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1984, 142 (02) :219-225
[5]   TUMOR NECROSIS FACTOR (CACHECTIN) INDUCES PHOSPHOLIPASE-A2 ACTIVITY AND SYNTHESIS OF A PHOSPHOLIPASE-A2-ACTIVATING PROTEIN IN ENDOTHELIAL-CELLS [J].
CLARK, MA ;
CHEN, MJ ;
CROOKE, ST ;
BOMALASKI, JS .
BIOCHEMICAL JOURNAL, 1988, 250 (01) :125-132
[6]  
DEJONG JGN, 1987, EUR J BIOCHEM, V164, P129
[7]  
DIJKSTRA CD, 1985, IMMUNOLOGY, V54, P589
[8]  
ELSEBACH P, 1988, INFLAMMATION, P445
[9]   SYNTHETIC PARTIAL EXTENSION PEPTIDES OF P-450(SCC) AND ADRENODOXIN PRECURSORS - EFFECTS ON THE IMPORT OF MITOCHONDRIAL ENZYME PRECURSORS [J].
FURUYA, S ;
OKADA, M ;
ITO, A ;
AOYAGI, H ;
KANMERA, T ;
KATO, T ;
SAGARA, Y ;
HORIUCHI, T ;
OMURA, T .
JOURNAL OF BIOCHEMISTRY, 1987, 102 (04) :821-832
[10]   THE PRIMARY STRUCTURE OF RAT PLATELET PHOSPHOLIPASE-A2 [J].
HAYAKAWA, M ;
KUDO, I ;
TOMITA, M ;
NOJIMA, S ;
INOUE, K .
JOURNAL OF BIOCHEMISTRY, 1988, 104 (05) :767-772