Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins
Pro-Inflammatory non-pancreatic phospholipase A2 (sPLA2) is markedly over-expressed in acute systemic and chronic local inflammatory processes. Since in acute phase reaction sPLA2 is often over-expressed simultaneously with acute phase proteins (APP), it is important to determine whether APP interac...
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| Format: | Article |
| Language: | English |
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Wiley
1996-01-01
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| Series: | Mediators of Inflammation |
| Online Access: | http://dx.doi.org/10.1155/S0962935196000270 |
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| author | W. Pruzanski E. Stefanski P. Vadas |
| author_facet | W. Pruzanski E. Stefanski P. Vadas |
| author_sort | W. Pruzanski |
| collection | DOAJ |
| description | Pro-Inflammatory non-pancreatic phospholipase A2 (sPLA2) is markedly over-expressed in acute systemic and chronic local inflammatory processes. Since in acute phase reaction sPLA2 is often over-expressed simultaneously with acute phase proteins (APP), it is important to determine whether APP interacts with sPLA2. We tested ten APPs for interaction with sPLA2 using as a substrate multilamellar Hposomes composed either of PC:Lyso PC or PE:Lyso PE. Using PC:Lyso PC substrate, CRP, lactoferrin and SAP were found to inhibit sPLA2 activity with an IC50 of 25 μg/ml, 7.5 μg/ml and 50 μg/ml, respectively, corresponding to 0.21 μM, 0.1 μM and 0.21 μM respectively. Using PE:Lyso PE substrate only SAP was inhibitory, with an IC50 of 10 μg/ml (0.04 μM). Phosphorylcholine abolished the inhibitory activity of CRP but not of SAP or lactoferrin. Addition of phosphorylethanolamine or of excess calcium had no effect on the inhibitory activity of APP. Limulin, lysozyme, transferrin, β2-microglobulin, α2-macroglobulin, human and bovine albumins had no effect on sPLA2 activity. Therefore neither the structure of pentraxins, or ironbinding, bacteriostatic property or amyloidogenic property preclude whether APP modulates sPLA2 activity. Inhibition of pro-inflammatory sPLA2 by APP may be one of the protective mechanisms of the acute phase reaction. |
| format | Article |
| id | doaj-art-5a7a79ae8daf431f80ff5a088fd2040e |
| institution | Kabale University |
| issn | 0962-9351 1466-1861 |
| language | English |
| publishDate | 1996-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Mediators of Inflammation |
| spelling | doaj-art-5a7a79ae8daf431f80ff5a088fd2040e2025-08-20T03:34:26ZengWileyMediators of Inflammation0962-93511466-18611996-01-015319620110.1155/S0962935196000270Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteinsW. Pruzanski0E. Stefanski1P. Vadas2Inflammation Research Group, The Wellesley Hospital Research Institute, University of Toronto, Ontario M4Y 1J3, CanadaInflammation Research Group, The Wellesley Hospital Research Institute, University of Toronto, Ontario M4Y 1J3, CanadaInflammation Research Group, The Wellesley Hospital Research Institute, University of Toronto, Ontario M4Y 1J3, CanadaPro-Inflammatory non-pancreatic phospholipase A2 (sPLA2) is markedly over-expressed in acute systemic and chronic local inflammatory processes. Since in acute phase reaction sPLA2 is often over-expressed simultaneously with acute phase proteins (APP), it is important to determine whether APP interacts with sPLA2. We tested ten APPs for interaction with sPLA2 using as a substrate multilamellar Hposomes composed either of PC:Lyso PC or PE:Lyso PE. Using PC:Lyso PC substrate, CRP, lactoferrin and SAP were found to inhibit sPLA2 activity with an IC50 of 25 μg/ml, 7.5 μg/ml and 50 μg/ml, respectively, corresponding to 0.21 μM, 0.1 μM and 0.21 μM respectively. Using PE:Lyso PE substrate only SAP was inhibitory, with an IC50 of 10 μg/ml (0.04 μM). Phosphorylcholine abolished the inhibitory activity of CRP but not of SAP or lactoferrin. Addition of phosphorylethanolamine or of excess calcium had no effect on the inhibitory activity of APP. Limulin, lysozyme, transferrin, β2-microglobulin, α2-macroglobulin, human and bovine albumins had no effect on sPLA2 activity. Therefore neither the structure of pentraxins, or ironbinding, bacteriostatic property or amyloidogenic property preclude whether APP modulates sPLA2 activity. Inhibition of pro-inflammatory sPLA2 by APP may be one of the protective mechanisms of the acute phase reaction.http://dx.doi.org/10.1155/S0962935196000270 |
| spellingShingle | W. Pruzanski E. Stefanski P. Vadas Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins Mediators of Inflammation |
| title | Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins |
| title_full | Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins |
| title_fullStr | Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins |
| title_full_unstemmed | Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins |
| title_short | Inhibition of the activity of pro-inflammatory secretory phospholipase A2 by acute phase proteins |
| title_sort | inhibition of the activity of pro inflammatory secretory phospholipase a2 by acute phase proteins |
| url | http://dx.doi.org/10.1155/S0962935196000270 |
| work_keys_str_mv | AT wpruzanski inhibitionoftheactivityofproinflammatorysecretoryphospholipasea2byacutephaseproteins AT estefanski inhibitionoftheactivityofproinflammatorysecretoryphospholipasea2byacutephaseproteins AT pvadas inhibitionoftheactivityofproinflammatorysecretoryphospholipasea2byacutephaseproteins |