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Characterization of phospholipase A2 activity in rat RPAR-induced pleurisy
At 10 min, 2 h and 4 h after induction of a reverse passive Arthus reaction (RPAR) in the pleural cavity of rats, pleural exudate was collected and analyzed in vitro for phospholipase A2 (PLA2) acyl hydrolytic activity. Inasmuch as exudate PLA2 was inhibited by addition of EDTA, the acyl hydrolytic...
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Published in: | Agents and Actions 1991-09, Vol.34 (1-2), p.97-99 |
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creator | Marinari, L R Berkenkopf, J W Weichman, B M |
description | At 10 min, 2 h and 4 h after induction of a reverse passive Arthus reaction (RPAR) in the pleural cavity of rats, pleural exudate was collected and analyzed in vitro for phospholipase A2 (PLA2) acyl hydrolytic activity. Inasmuch as exudate PLA2 was inhibited by addition of EDTA, the acyl hydrolytic activity appeared calcium-dependent. However, addition of exogenous calcium to the exudate had only a minor effect on the activity. Maximum hydrolysis in all exudates was observed over a pH range of 6-9 with a neutral optimum. The 4 h exudate PLA2 activity was almost fully inhibited by para-bromophenacyl bromide (pBPB), whereas the acyl hydrolytic activity in the 10 min and 2 h exudates was reduced by 44% and 46%, respectively, by 200 microM pBPB. Although the PLA2 in the 4 h exudate displayed an increased sensitivity to high exogenous calcium concentrations and to pBPB inactivation, the basic properties of the exudate PLA2 at the three time points appeared similar. |
doi_str_mv | 10.1007/BF01993248 |
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Inasmuch as exudate PLA2 was inhibited by addition of EDTA, the acyl hydrolytic activity appeared calcium-dependent. However, addition of exogenous calcium to the exudate had only a minor effect on the activity. Maximum hydrolysis in all exudates was observed over a pH range of 6-9 with a neutral optimum. The 4 h exudate PLA2 activity was almost fully inhibited by para-bromophenacyl bromide (pBPB), whereas the acyl hydrolytic activity in the 10 min and 2 h exudates was reduced by 44% and 46%, respectively, by 200 microM pBPB. 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Inasmuch as exudate PLA2 was inhibited by addition of EDTA, the acyl hydrolytic activity appeared calcium-dependent. However, addition of exogenous calcium to the exudate had only a minor effect on the activity. Maximum hydrolysis in all exudates was observed over a pH range of 6-9 with a neutral optimum. The 4 h exudate PLA2 activity was almost fully inhibited by para-bromophenacyl bromide (pBPB), whereas the acyl hydrolytic activity in the 10 min and 2 h exudates was reduced by 44% and 46%, respectively, by 200 microM pBPB. Although the PLA2 in the 4 h exudate displayed an increased sensitivity to high exogenous calcium concentrations and to pBPB inactivation, the basic properties of the exudate PLA2 at the three time points appeared similar.</description><subject>Acetophenones - pharmacology</subject><subject>Animals</subject><subject>Arthus Reaction - complications</subject><subject>Arthus Reaction - enzymology</subject><subject>Calcium - physiology</subject><subject>Exudates and Transudates - enzymology</subject><subject>Phospholipases A - antagonists & inhibitors</subject><subject>Phospholipases A - metabolism</subject><subject>Phospholipases A2</subject><subject>Pleurisy - enzymology</subject><subject>Pleurisy - etiology</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Serum Albumin, Bovine - immunology</subject><issn>0065-4299</issn><issn>1420-908X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNpFkM1LwzAchoMoc04v3oWcPAjV_JK0TY6zOD8YKEPBW8lXWaRra9IK86-3ssEOL-_led_Dg9AlkFsgJL-7XxCQklEujtAUOCWJJOLzGE0JydKEUylP0VmMX4SkKQiYoAkIJiSBKXop1ioo07vgf1Xv2wa3Fe7WbRxT-05Fh-cUj4D_8f0W-wYH1ePV23yV-MYOxlnc1W4IPm7P0Uml6ugu9j1DH4uH9-IpWb4-PhfzZWKooH1SMUlZKpl0SoJhlkjuGE8rRRXX2giey9RypiwFpZnNNdciHxeaaRA8BTZD17vfLrTfg4t9ufHRuLpWjWuHWOY0y_IM6Aje7EAT2hiDq8ou-I0K2xJI-S-uPIgb4av966A3zh7QnSn2B4CbZz8</recordid><startdate>199109</startdate><enddate>199109</enddate><creator>Marinari, L R</creator><creator>Berkenkopf, J W</creator><creator>Weichman, B M</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199109</creationdate><title>Characterization of phospholipase A2 activity in rat RPAR-induced pleurisy</title><author>Marinari, L R ; Berkenkopf, J W ; Weichman, B M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c282t-f39235939ea91c3d094e345fa2a4bbc84795d43ad21ab3d7b4b87235b3b184513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Acetophenones - pharmacology</topic><topic>Animals</topic><topic>Arthus Reaction - complications</topic><topic>Arthus Reaction - enzymology</topic><topic>Calcium - physiology</topic><topic>Exudates and Transudates - enzymology</topic><topic>Phospholipases A - antagonists & inhibitors</topic><topic>Phospholipases A - metabolism</topic><topic>Phospholipases A2</topic><topic>Pleurisy - enzymology</topic><topic>Pleurisy - etiology</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>Serum Albumin, Bovine - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marinari, L R</creatorcontrib><creatorcontrib>Berkenkopf, J W</creatorcontrib><creatorcontrib>Weichman, B M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Agents and Actions</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marinari, L R</au><au>Berkenkopf, J W</au><au>Weichman, B M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of phospholipase A2 activity in rat RPAR-induced pleurisy</atitle><jtitle>Agents and Actions</jtitle><addtitle>Agents Actions</addtitle><date>1991-09</date><risdate>1991</risdate><volume>34</volume><issue>1-2</issue><spage>97</spage><epage>99</epage><pages>97-99</pages><issn>0065-4299</issn><eissn>1420-908X</eissn><abstract>At 10 min, 2 h and 4 h after induction of a reverse passive Arthus reaction (RPAR) in the pleural cavity of rats, pleural exudate was collected and analyzed in vitro for phospholipase A2 (PLA2) acyl hydrolytic activity. 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subjects | Acetophenones - pharmacology Animals Arthus Reaction - complications Arthus Reaction - enzymology Calcium - physiology Exudates and Transudates - enzymology Phospholipases A - antagonists & inhibitors Phospholipases A - metabolism Phospholipases A2 Pleurisy - enzymology Pleurisy - etiology Proteins - metabolism Rats Serum Albumin, Bovine - immunology |
title | Characterization of phospholipase A2 activity in rat RPAR-induced pleurisy |
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