Phospholipase A2 Activation Influences the Processing and Secretion of the Amyloid Precursor Protein
The phospholipase A2 (PLA2) inhibitors quinacrine, manoalide and scalaradial inhibit the carbachol-stimulated secretion of the amyloid precursor protein (APP) from cells transfected with the human m1 muscarinic receptor. Conversely, activation of PLA2 by melittin increases secretion of an apparently...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1993-11, Vol.197 (1), p.292-297 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Emmerling, M.R. Moore, C.J. Doyle, P.D. Carroll, R.T. Davis, R.E. |
| description | The phospholipase A2 (PLA2) inhibitors quinacrine, manoalide and scalaradial inhibit the carbachol-stimulated secretion of the amyloid precursor protein (APP) from cells transfected with the human m1 muscarinic receptor. Conversely, activation of PLA2 by melittin increases secretion of an apparently immature species of APP from these cells. These results implicate PLA2 in regulating APP processing and secretion, which may have important implications for understanding the pathogenesis of Alzheimer′s Disease. |
| doi_str_mv | 10.1006/bbrc.1993.2474 |
| format | Article |
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Conversely, activation of PLA2 by melittin increases secretion of an apparently immature species of APP from these cells. These results implicate PLA2 in regulating APP processing and secretion, which may have important implications for understanding the pathogenesis of Alzheimer′s Disease.</description><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Amyloid beta-Protein Precursor - secretion</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbachol - pharmacology</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Enzyme Activation</subject><subject>Homosteroids</subject><subject>Medical sciences</subject><subject>Melitten - pharmacology</subject><subject>Neurology</subject><subject>Phospholipases A - antagonists & inhibitors</subject><subject>Phospholipases A - metabolism</subject><subject>Phospholipases A2</subject><subject>Protein Processing, Post-Translational</subject><subject>Quinacrine - pharmacology</subject><subject>Receptors, Muscarinic - metabolism</subject><subject>Sesterterpenes</subject><subject>Terpenes - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1LwzAYh4Moc06v3oQexFtnknZpcxzDj8HAgQreQpq8cZGumUk72H9vuo3dPL2B3_N-5EHoluAxwZg9VpVXY8J5NqZ5kZ-hIcEcp5Tg_BwNcSRSysnXJboK4QdjQnLGB2hQ0gnmWTlEerlyYbNytd3IAMmUJlPV2q1srWuSeWPqDhoFIWlXkCy9i89gm-9ENjp5B-Vhzzmzz6frXe2sjhyozgfn-44WbHONLoysA9wc6wh9Pj99zF7TxdvLfDZdpCoryjblxkhSgJGSV4zx0rB8QpiimaTaFESbihNNKWdFUZUFB8V0JbWsFCWcGmWyEXo4zN1499tBaMXaBgV1LRtwXRAFi5_GOY_g-AAq70LwYMTG27X0O0Gw6LWKXqvotYpea2y4O07uqjXoE370GPP7Yy6DkrXxslE2nLBIlHy_tzxgEC1sLXgRlO0FaxudtUI7-98Ff7IRlWk</recordid><startdate>19931130</startdate><enddate>19931130</enddate><creator>Emmerling, M.R.</creator><creator>Moore, C.J.</creator><creator>Doyle, P.D.</creator><creator>Carroll, R.T.</creator><creator>Davis, R.E.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>19931130</creationdate><title>Phospholipase A2 Activation Influences the Processing and Secretion of the Amyloid Precursor Protein</title><author>Emmerling, M.R. ; Moore, C.J. ; Doyle, P.D. ; Carroll, R.T. ; Davis, R.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-9ffa17efaa9b6698f64516c23a2df71dfb91d229677b879ec6dbadabc2192fcf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amyloid beta-Protein Precursor - metabolism</topic><topic>Amyloid beta-Protein Precursor - secretion</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbachol - pharmacology</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Enzyme Activation</topic><topic>Homosteroids</topic><topic>Medical sciences</topic><topic>Melitten - pharmacology</topic><topic>Neurology</topic><topic>Phospholipases A - antagonists & inhibitors</topic><topic>Phospholipases A - metabolism</topic><topic>Phospholipases A2</topic><topic>Protein Processing, Post-Translational</topic><topic>Quinacrine - pharmacology</topic><topic>Receptors, Muscarinic - metabolism</topic><topic>Sesterterpenes</topic><topic>Terpenes - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Emmerling, M.R.</creatorcontrib><creatorcontrib>Moore, C.J.</creatorcontrib><creatorcontrib>Doyle, P.D.</creatorcontrib><creatorcontrib>Carroll, R.T.</creatorcontrib><creatorcontrib>Davis, R.E.</creatorcontrib><collection>Pascal-Francis</collection><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Emmerling, M.R.</au><au>Moore, C.J.</au><au>Doyle, P.D.</au><au>Carroll, R.T.</au><au>Davis, R.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phospholipase A2 Activation Influences the Processing and Secretion of the Amyloid Precursor Protein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1993-11-30</date><risdate>1993</risdate><volume>197</volume><issue>1</issue><spage>292</spage><epage>297</epage><pages>292-297</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The phospholipase A2 (PLA2) inhibitors quinacrine, manoalide and scalaradial inhibit the carbachol-stimulated secretion of the amyloid precursor protein (APP) from cells transfected with the human m1 muscarinic receptor. 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| ispartof | Biochemical and biophysical research communications, 1993-11, Vol.197 (1), p.292-297 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amyloid beta-Protein Precursor - metabolism Amyloid beta-Protein Precursor - secretion Animals Biological and medical sciences Carbachol - pharmacology CHO Cells Cricetinae Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Enzyme Activation Homosteroids Medical sciences Melitten - pharmacology Neurology Phospholipases A - antagonists & inhibitors Phospholipases A - metabolism Phospholipases A2 Protein Processing, Post-Translational Quinacrine - pharmacology Receptors, Muscarinic - metabolism Sesterterpenes Terpenes - pharmacology |
| title | Phospholipase A2 Activation Influences the Processing and Secretion of the Amyloid Precursor Protein |
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