Competitive substrate inhibition in the histochemistry of cholinesterase activity in Alzheimer's disease
We used acetylcholine and butyrylcholine to competitively inhibit the cleavage of acetylthiocholine or butyrylthiocholine in plaques and tangles of Alzheimer's disease. Butyrylcholine was much more effective than acetylcholine in reducing the histochemical reaction for acetylcholinesterase not...
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| Veröffentlicht in: | Neuroscience letters 1990-09, Vol.117 (1), p.56-61 |
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| container_title | Neuroscience letters |
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| creator | Schätz, Christoph R. Geula, Changiz Mesulam, Marsel |
| description | We used acetylcholine and butyrylcholine to competitively inhibit the cleavage of acetylthiocholine or butyrylthiocholine in plaques and tangles of Alzheimer's disease. Butyrylcholine was much more effective than acetylcholine in reducing the histochemical reaction for acetylcholinesterase not only in neuronal fibers, but also in plaques and tangles. This is in keeping with biochemical data on acetylcholinesterase and supports the existence of true acetylcholinesterase activity within plaques and tangles. However, 2–4 times higher acetylcholine and buturylcholine concentrations were necessary to inhibit the plaque and tangle bound enzyme. Together with the previously reported different pH optima, this suggests that the plaque- and tangle-bound acetylcholinesterase may represent an altered form of this enzyme. |
| doi_str_mv | 10.1016/0304-3940(90)90119-T |
| format | Article |
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Butyrylcholine was much more effective than acetylcholine in reducing the histochemical reaction for acetylcholinesterase not only in neuronal fibers, but also in plaques and tangles. This is in keeping with biochemical data on acetylcholinesterase and supports the existence of true acetylcholinesterase activity within plaques and tangles. However, 2–4 times higher acetylcholine and buturylcholine concentrations were necessary to inhibit the plaque and tangle bound enzyme. Together with the previously reported different pH optima, this suggests that the plaque- and tangle-bound acetylcholinesterase may represent an altered form of this enzyme.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/0304-3940(90)90119-T</identifier><identifier>PMID: 2290622</identifier><identifier>CODEN: NELED5</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Acetylcholinesterase - metabolism ; Adult ; Aged ; Aged, 80 and over ; Alzheimer Disease - enzymology ; Alzheimer Disease - pathology ; Alzheimer's disease ; Binding, Competitive ; Biological and medical sciences ; Brain - enzymology ; Brain - pathology ; Butyrylcholinesterase - metabolism ; Cholinesterase histochemistry ; Cholinesterase Inhibitors - metabolism ; Competitive substrate inhibition ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; Female ; Humans ; Hydrogen-Ion Concentration ; Medical sciences ; Neurology ; Plaque ; Reference Values ; Tangle</subject><ispartof>Neuroscience letters, 1990-09, Vol.117 (1), p.56-61</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-c82419833dfd71ef3bab72f6a9f5b2a5cec23552624a41c0bbdfea357b7602303</citedby><cites>FETCH-LOGICAL-c418t-c82419833dfd71ef3bab72f6a9f5b2a5cec23552624a41c0bbdfea357b7602303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/030439409090119T$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19302700$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2290622$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schätz, Christoph R.</creatorcontrib><creatorcontrib>Geula, Changiz</creatorcontrib><creatorcontrib>Mesulam, Marsel</creatorcontrib><title>Competitive substrate inhibition in the histochemistry of cholinesterase activity in Alzheimer's disease</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>We used acetylcholine and butyrylcholine to competitively inhibit the cleavage of acetylthiocholine or butyrylthiocholine in plaques and tangles of Alzheimer's disease. Butyrylcholine was much more effective than acetylcholine in reducing the histochemical reaction for acetylcholinesterase not only in neuronal fibers, but also in plaques and tangles. This is in keeping with biochemical data on acetylcholinesterase and supports the existence of true acetylcholinesterase activity within plaques and tangles. However, 2–4 times higher acetylcholine and buturylcholine concentrations were necessary to inhibit the plaque and tangle bound enzyme. Together with the previously reported different pH optima, this suggests that the plaque- and tangle-bound acetylcholinesterase may represent an altered form of this enzyme.</description><subject>Acetylcholinesterase - metabolism</subject><subject>Adult</subject><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Alzheimer Disease - enzymology</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>Brain - pathology</subject><subject>Butyrylcholinesterase - metabolism</subject><subject>Cholinesterase histochemistry</subject><subject>Cholinesterase Inhibitors - metabolism</subject><subject>Competitive substrate inhibition</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>Female</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Medical sciences</subject><subject>Neurology</subject><subject>Plaque</subject><subject>Reference Values</subject><subject>Tangle</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV2L1DAUDaKs4-o_UOiLH_tQvUmatnlZWAZ1Fxb2ZXwOSXpDI20zJpmF8debMsP6phC4IeeDk3MJeUvhMwXafgEOTc1lA58kXEmgVNa7Z2RD-47VnezYc7J5orwkr1L6CQCCiuaCXDAmoWVsQ8ZtmPeYffaPWKWDSTnqjJVfRm_KY1jKtcojVqNPOdgR5zLjsQqusmOY_IIpY9QJK22Lh8_HVXAz_R7Rzxg_pmrwCQv-mrxwekr45jwvyY9vX3fb2_r-4fvd9ua-tg3tc2171lDZcz64oaPouNGmY67V0gnDtLBoGReCtazRDbVgzOBQc9GZrgXGgV-SDyfffQy_DiWdKoktTpNeMByS6oG1nFHxXyIVkvWSr8TmRLQxpBTRqX30s45HRUGtm1BrzWqtWcn1lE2oXZG9O_sfzIzDk-hcfcHfn3GdrJ5c1Iv16a-35MA6WD90feJhae3RY1TJelwsDj6izWoI_t9B_gDGsabB</recordid><startdate>19900904</startdate><enddate>19900904</enddate><creator>Schätz, Christoph R.</creator><creator>Geula, Changiz</creator><creator>Mesulam, Marsel</creator><general>Elsevier Ireland Ltd</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19900904</creationdate><title>Competitive substrate inhibition in the histochemistry of cholinesterase activity in Alzheimer's disease</title><author>Schätz, Christoph R. ; Geula, Changiz ; Mesulam, Marsel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-c82419833dfd71ef3bab72f6a9f5b2a5cec23552624a41c0bbdfea357b7602303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Acetylcholinesterase - metabolism</topic><topic>Adult</topic><topic>Aged</topic><topic>Aged, 80 and over</topic><topic>Alzheimer Disease - enzymology</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer's disease</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>Brain - pathology</topic><topic>Butyrylcholinesterase - metabolism</topic><topic>Cholinesterase histochemistry</topic><topic>Cholinesterase Inhibitors - metabolism</topic><topic>Competitive substrate inhibition</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>Female</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Medical sciences</topic><topic>Neurology</topic><topic>Plaque</topic><topic>Reference Values</topic><topic>Tangle</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schätz, Christoph R.</creatorcontrib><creatorcontrib>Geula, Changiz</creatorcontrib><creatorcontrib>Mesulam, Marsel</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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schätz, Christoph R.</au><au>Geula, Changiz</au><au>Mesulam, Marsel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Competitive substrate inhibition in the histochemistry of cholinesterase activity in Alzheimer's disease</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>1990-09-04</date><risdate>1990</risdate><volume>117</volume><issue>1</issue><spage>56</spage><epage>61</epage><pages>56-61</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><coden>NELED5</coden><abstract>We used acetylcholine and butyrylcholine to competitively inhibit the cleavage of acetylthiocholine or butyrylthiocholine in plaques and tangles of Alzheimer's disease. Butyrylcholine was much more effective than acetylcholine in reducing the histochemical reaction for acetylcholinesterase not only in neuronal fibers, but also in plaques and tangles. This is in keeping with biochemical data on acetylcholinesterase and supports the existence of true acetylcholinesterase activity within plaques and tangles. However, 2–4 times higher acetylcholine and buturylcholine concentrations were necessary to inhibit the plaque and tangle bound enzyme. Together with the previously reported different pH optima, this suggests that the plaque- and tangle-bound acetylcholinesterase may represent an altered form of this enzyme.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>2290622</pmid><doi>10.1016/0304-3940(90)90119-T</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0304-3940 |
| ispartof | Neuroscience letters, 1990-09, Vol.117 (1), p.56-61 |
| issn | 0304-3940 1872-7972 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acetylcholinesterase - metabolism Adult Aged Aged, 80 and over Alzheimer Disease - enzymology Alzheimer Disease - pathology Alzheimer's disease Binding, Competitive Biological and medical sciences Brain - enzymology Brain - pathology Butyrylcholinesterase - metabolism Cholinesterase histochemistry Cholinesterase Inhibitors - metabolism Competitive substrate inhibition Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Female Humans Hydrogen-Ion Concentration Medical sciences Neurology Plaque Reference Values Tangle |
| title | Competitive substrate inhibition in the histochemistry of cholinesterase activity in Alzheimer's disease |
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