Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat
We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues poss...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1987-11, Vol.84 (21), p.7749-7752 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Koelle, G.B Massoulie, J Eugene, D Melone, M.A.B Boulla, G |
| description | We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues possess very different levels of enzymic activities. The proportions of the α α , α γ , and γ γ enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical findings. The results are consistent with the premise that the G1 (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites. |
| doi_str_mv | 10.1073/pnas.84.21.7749 |
| format | Article |
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The proportions of the α α , α γ , and γ γ enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical findings. The results are consistent with the premise that the G1 (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.84.21.7749</identifier><identifier>PMID: 3478723</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>ACETILCOLINESTERASA ; ACETYLCHOLINESTERASE ; Acetylcholinesterase - isolation & purification ; Acetylcholinesterase - metabolism ; Animals ; BIOLOGIA MOLECULAR ; Biological and medical sciences ; BIOLOGIE MOLECULAIRE ; Butyrylcholinesterase - isolation & purification ; Butyrylcholinesterase - metabolism ; CATS ; Caudate Nucleus - enzymology ; Cell membranes ; Cell physiology ; CHAT ; CHEMISTRY ; CHIMIE ; CHOLINESTERASE ; Cholinesterases - metabolism ; COLINESTERASA ; Cytoplasm ; Denervation ; Dimers ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Ganglia ; Ganglia, Spinal - enzymology ; Ganglia, Sympathetic - enzymology ; GATO ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; L-Lactate Dehydrogenase - metabolism ; Molecular and cellular biology ; MOLECULAR BIOLOGY ; Nerve tissue ; NERVOUS SYSTEM ; Neurons ; Neurotransmission ; Organ Specificity ; Phosphopyruvate Hydratase - metabolism ; QUIMICA ; SISTEMA NERVIOSO ; Stellate Ganglion - enzymology ; Superior cervical ganglion ; Synapses ; SYSTEME NERVEUX</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1987-11, Vol.84 (21), p.7749-7752</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c542t-d1a71331178dfaa760104dc23e3bd7654fb5ac491d7d1318c940449418e1fe33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/84/21.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30902$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30902$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7419934$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3478723$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koelle, G.B</creatorcontrib><creatorcontrib>Massoulie, J</creatorcontrib><creatorcontrib>Eugene, D</creatorcontrib><creatorcontrib>Melone, M.A.B</creatorcontrib><creatorcontrib>Boulla, G</creatorcontrib><title>Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues possess very different levels of enzymic activities. The proportions of the α α , α γ , and γ γ enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical findings. The results are consistent with the premise that the G1 (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites.</description><subject>ACETILCOLINESTERASA</subject><subject>ACETYLCHOLINESTERASE</subject><subject>Acetylcholinesterase - isolation & purification</subject><subject>Acetylcholinesterase - metabolism</subject><subject>Animals</subject><subject>BIOLOGIA MOLECULAR</subject><subject>Biological and medical sciences</subject><subject>BIOLOGIE MOLECULAIRE</subject><subject>Butyrylcholinesterase - isolation & purification</subject><subject>Butyrylcholinesterase - metabolism</subject><subject>CATS</subject><subject>Caudate Nucleus - enzymology</subject><subject>Cell membranes</subject><subject>Cell physiology</subject><subject>CHAT</subject><subject>CHEMISTRY</subject><subject>CHIMIE</subject><subject>CHOLINESTERASE</subject><subject>Cholinesterases - metabolism</subject><subject>COLINESTERASA</subject><subject>Cytoplasm</subject><subject>Denervation</subject><subject>Dimers</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Ganglia</subject><subject>Ganglia, Spinal - enzymology</subject><subject>Ganglia, Sympathetic - enzymology</subject><subject>GATO</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>L-Lactate Dehydrogenase - metabolism</subject><subject>Molecular and cellular biology</subject><subject>MOLECULAR BIOLOGY</subject><subject>Nerve tissue</subject><subject>NERVOUS SYSTEM</subject><subject>Neurons</subject><subject>Neurotransmission</subject><subject>Organ Specificity</subject><subject>Phosphopyruvate Hydratase - metabolism</subject><subject>QUIMICA</subject><subject>SISTEMA NERVIOSO</subject><subject>Stellate Ganglion - enzymology</subject><subject>Superior cervical ganglion</subject><subject>Synapses</subject><subject>SYSTEME NERVEUX</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2PFCEUxInRrOPq2cSo6YPRU8_ygBng4MGsn8kmHlzPhKFhhw3djEBvnP9e2mlHNyZ6IqF-9XhFIfQY8BIwp2e7QeelYEsCS86ZvIMWgCW0aybxXbTAmPBWMMLuowc5X2OM5UrgE3RCGRec0AWKb30uyW_G4uOQm-iaPgZrxqBT42Lqf15pY8s-mG0MfrC52KSzbfTQNdW2T38pfmgGm27imJvicx7tNKNsbWN0eYjuOR2yfTSfp-jy_bvL84_txecPn87fXLRmxUhpO9AcKAXgonNa8zUGzDpDqKWbjq9XzG1W2jAJHe-AgjCSYcYkA2HBWUpP0evD2N246W1n7FCSDmqXfK_TXkXt1W1l8Ft1FW8UkZJyUf0vZ3-K38aaTPU-GxuCHmzNpQRgITCw_4LAuKQEcAXPDqBJMedk3XEZwGqqUk1VKsEUATVVWR3P_sxw5Ofuqv5i1nU2OrikB-PzEeMMapZpw-czNs3_pd5659U_AeXGEIr9Xir55EBe5xLT74WwxKSKTw-i01Hpq1RX-fpF1I9i67UQ9Ae0vNQo</recordid><startdate>19871101</startdate><enddate>19871101</enddate><creator>Koelle, G.B</creator><creator>Massoulie, J</creator><creator>Eugene, D</creator><creator>Melone, M.A.B</creator><creator>Boulla, G</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</scope><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><scope>5PM</scope></search><sort><creationdate>19871101</creationdate><title>Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat</title><author>Koelle, G.B ; Massoulie, J ; Eugene, D ; Melone, M.A.B ; Boulla, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c542t-d1a71331178dfaa760104dc23e3bd7654fb5ac491d7d1318c940449418e1fe33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>ACETILCOLINESTERASA</topic><topic>ACETYLCHOLINESTERASE</topic><topic>Acetylcholinesterase - isolation & purification</topic><topic>Acetylcholinesterase - metabolism</topic><topic>Animals</topic><topic>BIOLOGIA MOLECULAR</topic><topic>Biological and medical sciences</topic><topic>BIOLOGIE MOLECULAIRE</topic><topic>Butyrylcholinesterase - isolation & purification</topic><topic>Butyrylcholinesterase - metabolism</topic><topic>CATS</topic><topic>Caudate Nucleus - enzymology</topic><topic>Cell membranes</topic><topic>Cell physiology</topic><topic>CHAT</topic><topic>CHEMISTRY</topic><topic>CHIMIE</topic><topic>CHOLINESTERASE</topic><topic>Cholinesterases - metabolism</topic><topic>COLINESTERASA</topic><topic>Cytoplasm</topic><topic>Denervation</topic><topic>Dimers</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Ganglia</topic><topic>Ganglia, Spinal - enzymology</topic><topic>Ganglia, Sympathetic - enzymology</topic><topic>GATO</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>L-Lactate Dehydrogenase - metabolism</topic><topic>Molecular and cellular biology</topic><topic>MOLECULAR BIOLOGY</topic><topic>Nerve tissue</topic><topic>NERVOUS SYSTEM</topic><topic>Neurons</topic><topic>Neurotransmission</topic><topic>Organ Specificity</topic><topic>Phosphopyruvate Hydratase - metabolism</topic><topic>QUIMICA</topic><topic>SISTEMA NERVIOSO</topic><topic>Stellate Ganglion - enzymology</topic><topic>Superior cervical ganglion</topic><topic>Synapses</topic><topic>SYSTEME NERVEUX</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koelle, G.B</creatorcontrib><creatorcontrib>Massoulie, J</creatorcontrib><creatorcontrib>Eugene, D</creatorcontrib><creatorcontrib>Melone, M.A.B</creatorcontrib><creatorcontrib>Boulla, G</creatorcontrib><collection>AGRIS</collection><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koelle, G.B</au><au>Massoulie, J</au><au>Eugene, D</au><au>Melone, M.A.B</au><au>Boulla, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1987-11-01</date><risdate>1987</risdate><volume>84</volume><issue>21</issue><spage>7749</spage><epage>7752</epage><pages>7749-7752</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues possess very different levels of enzymic activities. The proportions of the α α , α γ , and γ γ enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical findings. The results are consistent with the premise that the G1 (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3478723</pmid><doi>10.1073/pnas.84.21.7749</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0027-8424 1091-6490 |
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| subjects | ACETILCOLINESTERASA ACETYLCHOLINESTERASE Acetylcholinesterase - isolation & purification Acetylcholinesterase - metabolism Animals BIOLOGIA MOLECULAR Biological and medical sciences BIOLOGIE MOLECULAIRE Butyrylcholinesterase - isolation & purification Butyrylcholinesterase - metabolism CATS Caudate Nucleus - enzymology Cell membranes Cell physiology CHAT CHEMISTRY CHIMIE CHOLINESTERASE Cholinesterases - metabolism COLINESTERASA Cytoplasm Denervation Dimers Enzymes Fundamental and applied biological sciences. Psychology Ganglia Ganglia, Spinal - enzymology Ganglia, Sympathetic - enzymology GATO Isoenzymes - isolation & purification Isoenzymes - metabolism L-Lactate Dehydrogenase - metabolism Molecular and cellular biology MOLECULAR BIOLOGY Nerve tissue NERVOUS SYSTEM Neurons Neurotransmission Organ Specificity Phosphopyruvate Hydratase - metabolism QUIMICA SISTEMA NERVIOSO Stellate Ganglion - enzymology Superior cervical ganglion Synapses SYSTEME NERVEUX |
| title | Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat |
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