The effect of dioleoylglycerol on cytosolic phospholipase A2 activity using a continuous fluorescence displacement assay

1995 ◽  
Vol 23 (4) ◽  
pp. 569S-569S
Author(s):  
ANN CREANEY ◽  
DAVID C. WILTON
Keyword(s):  
Phospholipase A2 ◽  
Cytosolic Phospholipase A2 ◽  
Cytosolic Phospholipase ◽  
Displacement Assay ◽  
Phospholipase A2 Activity

scholarly journals Characterization of phospholipase A2 in monocytic cell lines. Functional and biochemical aspects of membrane association

1991 ◽  
Vol 276 (3) ◽  
pp. 631-636 ◽  
Author(s):  
W Rehfeldt ◽  
R Hass ◽  
M Goppelt-Struebe
Keyword(s):  
Substrate Specificity ◽  
Phospholipase A2 ◽  
Cell Lines ◽  
Cytosolic Phospholipase A2 ◽  
Biologically Active ◽  
Ph Optimum ◽  
Monocytic Cell ◽  
Cytosolic Phospholipase ◽  
Membrane Bound ◽  
Phospholipase A2 Activity

Phospholipase A2 activity was characterized in the human monocytic tumour-cell lines U937 and THP1. The enzyme showed an alkaline pH optimum and substrate specificity for arachidonoyl-phosphatidylcholine. The activation of phospholipase A2 required bivalent cations (Ca2+ greater than Mg2+ = Sr2+ greater than Ba2+). Investigation of the subcellular distribution of the enzyme revealed that the phospholipase A2 activity was shifted to the cytosol in the presence of EDTA, indicating that the association of the enzyme with the cellular membranes is Ca2+ (bivalent-cation)-dependent. Stimulation of THP1 cells for 2-4 h with the phorbol ester phorbol 12-myristate 13-acetate (PMA) activated cytosolic and membrane-bound phospholipase A2. At this time, no effect of PMA on phospholipase A2 activity was observed in the less mature U937 cells. However, when both cell lines were induced to differentiate along the monocytic pathway by a 2-3-day treatment with PMA, the cells released significant amounts of arachidonic acid and prostanoids. Compared with undifferentiated control cells, these PMA-differentiated cells showed a decrease in cytosolic phospholipase A2 activity and an increase in membrane-bound activity. Membrane-bound and cytosolic enzyme showed the same pH optimum, Ca(2+)-dependency and substrate specificity. These data indicate that membrane-bound and cytosolic phospholipase A2 activities represent one enzyme and that the membrane-bound form is the biologically active phospholipase A2.

Compounds stimulating cytosolic phospholipase A2 activity with a combinational action mode

2004 ◽  
Vol 325 (2) ◽  
pp. 632-638
Author(s):  
Yoe-Sik Bae ◽  
Eun-Young Park ◽  
Ha-Young Lee ◽  
Hyun Kyu Kang ◽  
Pann-Ghill Suh ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Cytosolic Phospholipase A2 ◽  
Action Mode ◽  
Cytosolic Phospholipase ◽  
Phospholipase A2 Activity

Increased glomerular cytosolic phospholipase A2 activity of OLETF rats with early diabetes

2009 ◽  
Vol 107 (05) ◽  
pp. 299-305 ◽  
Author(s):  
Y. Furuya ◽  
S. Tagami ◽  
A. Hasegawa ◽  
J. Ishii ◽  
J. Hirokawa ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Cytosolic Phospholipase A2 ◽  
Early Diabetes ◽  
Oletf Rats ◽  
Cytosolic Phospholipase ◽  
Phospholipase A2 Activity

scholarly journals Endothelin-1 stimulates cytosolic phospholipase A2 activity and gene expression in rat glomerular mesangial cells

1994 ◽  
Vol 46 (6) ◽  
pp. 1644-1652 ◽  
Author(s):  
Herbert Schramek ◽  
Yizheng Wang ◽  
Martha Konieczkowski ◽  
Michael S. Simonson ◽  
Michael J. Dunn
Keyword(s):  
Gene Expression ◽  
Phospholipase A2 ◽  
Mesangial Cells ◽  
Cytosolic Phospholipase A2 ◽  
Glomerular Mesangial Cells ◽  
Endothelin 1 ◽  
Cytosolic Phospholipase ◽  
Phospholipase A2 Activity
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