Isoenzyme pattern of enolase in the diagnosis of neuroendocrine bronchopulmonary tumors
Electrophoretic separation of enolase isoenzymes and the measurement of enolase activity were performed in 25 lung tumor extracts. In 13 neuroendocrine (NE) tumors (nine small cell lung carcinoma [SCLC], three atypical NE tumors, and one carcinoid tumor), the NE differentiation was assessed by ultra...
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| Veröffentlicht in: | Cancer 1987-08, Vol.60 (4), p.838-843 |
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| creator | Batandier, C. Brambilla, E. Jacrot, M. Morel, F. Beriel, H. Paramelle, B. Brambilla, C. |
| description | Electrophoretic separation of enolase isoenzymes and the measurement of enolase activity were performed in 25 lung tumor extracts. In 13 neuroendocrine (NE) tumors (nine small cell lung carcinoma [SCLC], three atypical NE tumors, and one carcinoid tumor), the NE differentiation was assessed by ultrastructural determination of neurosecretory granule (NSG) density. Twelve non‐NE lung tumors also were studied (three adenocarcinomas, four epidermoid, two composite, two large cell undifferentiated carcinomas, and one lymphoma). Four normal lung tissues and 1 human brain were used as controls. The γγ isoenzyme was present at a high level (mean ± SE, 12 ± 3%) in all NE carcinomas and consistently absent in all non‐NE tumors as well as in normal lung. The αγ isoenzyme was found in significantly higher proportion in NE carcinomas (mean ± SE, 29 ± 2%) than in non‐NE tumors (mean ± SE, 8 ± 1%) (P |
| doi_str_mv | 10.1002/1097-0142(19870815)60:4<838::AID-CNCR2820600420>3.0.CO;2-W |
| format | Article |
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In 13 neuroendocrine (NE) tumors (nine small cell lung carcinoma [SCLC], three atypical NE tumors, and one carcinoid tumor), the NE differentiation was assessed by ultrastructural determination of neurosecretory granule (NSG) density. Twelve non‐NE lung tumors also were studied (three adenocarcinomas, four epidermoid, two composite, two large cell undifferentiated carcinomas, and one lymphoma). Four normal lung tissues and 1 human brain were used as controls. The γγ isoenzyme was present at a high level (mean ± SE, 12 ± 3%) in all NE carcinomas and consistently absent in all non‐NE tumors as well as in normal lung. The αγ isoenzyme was found in significantly higher proportion in NE carcinomas (mean ± SE, 29 ± 2%) than in non‐NE tumors (mean ± SE, 8 ± 1%) (P <0.0001), despite an equally high level of total enolase activity in both groups of tumor. The separation of αm̀ and γγ isoenzymes of enolase allows for the accurate diagnosis of NE tumors and NE components of atypical NE carcinomas, and the γγ isoenzyme, in contrast to γ chain detection by immunoassay, can be considered to be a specific marker in itself of NE differentiation in lung neoplasms.</description><identifier>ISSN: 0008-543X</identifier><identifier>EISSN: 1097-0142</identifier><identifier>DOI: 10.1002/1097-0142(19870815)60:4<838::AID-CNCR2820600420>3.0.CO;2-W</identifier><identifier>PMID: 3036337</identifier><identifier>CODEN: CANCAR</identifier><language>eng</language><publisher>New York: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Adenocarcinoma - enzymology ; Biological and medical sciences ; Carcinoid Tumor - enzymology ; Carcinoma, Small Cell - enzymology ; Carcinoma, Squamous Cell - enzymology ; Cytoplasmic Granules - ultrastructure ; Electrophoresis, Cellulose Acetate ; Humans ; Lung Neoplasms - diagnosis ; Lung Neoplasms - enzymology ; Lung Neoplasms - ultrastructure ; Lymphoma - enzymology ; Medical sciences ; Phosphopyruvate Hydratase - analysis ; Pneumology ; Tumors of the respiratory system and mediastinum</subject><ispartof>Cancer, 1987-08, Vol.60 (4), p.838-843</ispartof><rights>Copyright © 1987 American Cancer Society</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4950-9750afdb3bfbb4daa0c53c20e2733aac96899fc3f2f98f8a8b3ee8f15d078cb13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8299327$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3036337$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Batandier, C.</creatorcontrib><creatorcontrib>Brambilla, E.</creatorcontrib><creatorcontrib>Jacrot, M.</creatorcontrib><creatorcontrib>Morel, F.</creatorcontrib><creatorcontrib>Beriel, H.</creatorcontrib><creatorcontrib>Paramelle, B.</creatorcontrib><creatorcontrib>Brambilla, C.</creatorcontrib><title>Isoenzyme pattern of enolase in the diagnosis of neuroendocrine bronchopulmonary tumors</title><title>Cancer</title><addtitle>Cancer</addtitle><description>Electrophoretic separation of enolase isoenzymes and the measurement of enolase activity were performed in 25 lung tumor extracts. In 13 neuroendocrine (NE) tumors (nine small cell lung carcinoma [SCLC], three atypical NE tumors, and one carcinoid tumor), the NE differentiation was assessed by ultrastructural determination of neurosecretory granule (NSG) density. Twelve non‐NE lung tumors also were studied (three adenocarcinomas, four epidermoid, two composite, two large cell undifferentiated carcinomas, and one lymphoma). Four normal lung tissues and 1 human brain were used as controls. The γγ isoenzyme was present at a high level (mean ± SE, 12 ± 3%) in all NE carcinomas and consistently absent in all non‐NE tumors as well as in normal lung. The αγ isoenzyme was found in significantly higher proportion in NE carcinomas (mean ± SE, 29 ± 2%) than in non‐NE tumors (mean ± SE, 8 ± 1%) (P <0.0001), despite an equally high level of total enolase activity in both groups of tumor. The separation of αm̀ and γγ isoenzymes of enolase allows for the accurate diagnosis of NE tumors and NE components of atypical NE carcinomas, and the γγ isoenzyme, in contrast to γ chain detection by immunoassay, can be considered to be a specific marker in itself of NE differentiation in lung neoplasms.</description><subject>Adenocarcinoma - enzymology</subject><subject>Biological and medical sciences</subject><subject>Carcinoid Tumor - enzymology</subject><subject>Carcinoma, Small Cell - enzymology</subject><subject>Carcinoma, Squamous Cell - enzymology</subject><subject>Cytoplasmic Granules - ultrastructure</subject><subject>Electrophoresis, Cellulose Acetate</subject><subject>Humans</subject><subject>Lung Neoplasms - diagnosis</subject><subject>Lung Neoplasms - enzymology</subject><subject>Lung Neoplasms - ultrastructure</subject><subject>Lymphoma - enzymology</subject><subject>Medical sciences</subject><subject>Phosphopyruvate Hydratase - analysis</subject><subject>Pneumology</subject><subject>Tumors of the respiratory system and mediastinum</subject><issn>0008-543X</issn><issn>1097-0142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF2L1DAYhYMo6-zqTxB6IeJedHyTNE0yK8JavwYWB0QZ8SakaeJW2mRMWmT89bbMOKAXglchnOc9HB6EXmJYYgDyDIPkOeCCPMVScBCYXZawKp4LKlar6_WrvHpffSCCQAlQEHhBl7CsNlck395Bi9PxXbQAAJGzgn6-j85T-jZ9OWH0DJ1RoCWlfIG26xSs_7nvbbbTw2Cjz4LLrA-dTjZrfTbc2qxp9VcfUpvmzNsxTidNMLH1Nqtj8OY27MauD17HfTaMfYjpAbrndJfsw-N7gT69ef2xepffbN6uq-ub3BSSQS45A-2amtaurotGazCMGgKWcEq1NrIUUjpDHXFSOKFFTa0VDrMGuDA1phfoyaF3F8P30aZB9W0ytuu0t2FMinPGMKdyAr8cQBNDStE6tYttPw1WGNRsXc3i1CxO_bauSlCFmqwrNVlXf1pXVIGqNoqo7VT-6LhirHvbnKqPmqf88THXyejORe1Nm06YIFJSMmP2gP1oO7v_r4H_3PdXQn8B2rCuVQ</recordid><startdate>19870815</startdate><enddate>19870815</enddate><creator>Batandier, C.</creator><creator>Brambilla, E.</creator><creator>Jacrot, M.</creator><creator>Morel, F.</creator><creator>Beriel, H.</creator><creator>Paramelle, B.</creator><creator>Brambilla, C.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</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>19870815</creationdate><title>Isoenzyme pattern of enolase in the diagnosis of neuroendocrine bronchopulmonary tumors</title><author>Batandier, C. ; Brambilla, E. ; Jacrot, M. ; Morel, F. ; Beriel, H. ; Paramelle, B. ; Brambilla, C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4950-9750afdb3bfbb4daa0c53c20e2733aac96899fc3f2f98f8a8b3ee8f15d078cb13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Adenocarcinoma - enzymology</topic><topic>Biological and medical sciences</topic><topic>Carcinoid Tumor - enzymology</topic><topic>Carcinoma, Small Cell - enzymology</topic><topic>Carcinoma, Squamous Cell - enzymology</topic><topic>Cytoplasmic Granules - ultrastructure</topic><topic>Electrophoresis, Cellulose Acetate</topic><topic>Humans</topic><topic>Lung Neoplasms - diagnosis</topic><topic>Lung Neoplasms - enzymology</topic><topic>Lung Neoplasms - ultrastructure</topic><topic>Lymphoma - enzymology</topic><topic>Medical sciences</topic><topic>Phosphopyruvate Hydratase - analysis</topic><topic>Pneumology</topic><topic>Tumors of the respiratory system and mediastinum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Batandier, C.</creatorcontrib><creatorcontrib>Brambilla, E.</creatorcontrib><creatorcontrib>Jacrot, M.</creatorcontrib><creatorcontrib>Morel, F.</creatorcontrib><creatorcontrib>Beriel, H.</creatorcontrib><creatorcontrib>Paramelle, B.</creatorcontrib><creatorcontrib>Brambilla, C.</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>Cancer</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Batandier, C.</au><au>Brambilla, E.</au><au>Jacrot, M.</au><au>Morel, F.</au><au>Beriel, H.</au><au>Paramelle, B.</au><au>Brambilla, C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isoenzyme pattern of enolase in the diagnosis of neuroendocrine bronchopulmonary tumors</atitle><jtitle>Cancer</jtitle><addtitle>Cancer</addtitle><date>1987-08-15</date><risdate>1987</risdate><volume>60</volume><issue>4</issue><spage>838</spage><epage>843</epage><pages>838-843</pages><issn>0008-543X</issn><eissn>1097-0142</eissn><coden>CANCAR</coden><abstract>Electrophoretic separation of enolase isoenzymes and the measurement of enolase activity were performed in 25 lung tumor extracts. In 13 neuroendocrine (NE) tumors (nine small cell lung carcinoma [SCLC], three atypical NE tumors, and one carcinoid tumor), the NE differentiation was assessed by ultrastructural determination of neurosecretory granule (NSG) density. Twelve non‐NE lung tumors also were studied (three adenocarcinomas, four epidermoid, two composite, two large cell undifferentiated carcinomas, and one lymphoma). Four normal lung tissues and 1 human brain were used as controls. The γγ isoenzyme was present at a high level (mean ± SE, 12 ± 3%) in all NE carcinomas and consistently absent in all non‐NE tumors as well as in normal lung. The αγ isoenzyme was found in significantly higher proportion in NE carcinomas (mean ± SE, 29 ± 2%) than in non‐NE tumors (mean ± SE, 8 ± 1%) (P <0.0001), despite an equally high level of total enolase activity in both groups of tumor. The separation of αm̀ and γγ isoenzymes of enolase allows for the accurate diagnosis of NE tumors and NE components of atypical NE carcinomas, and the γγ isoenzyme, in contrast to γ chain detection by immunoassay, can be considered to be a specific marker in itself of NE differentiation in lung neoplasms.</abstract><cop>New York</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>3036337</pmid><doi>10.1002/1097-0142(19870815)60:4<838::AID-CNCR2820600420>3.0.CO;2-W</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenocarcinoma - enzymology Biological and medical sciences Carcinoid Tumor - enzymology Carcinoma, Small Cell - enzymology Carcinoma, Squamous Cell - enzymology Cytoplasmic Granules - ultrastructure Electrophoresis, Cellulose Acetate Humans Lung Neoplasms - diagnosis Lung Neoplasms - enzymology Lung Neoplasms - ultrastructure Lymphoma - enzymology Medical sciences Phosphopyruvate Hydratase - analysis Pneumology Tumors of the respiratory system and mediastinum |
| title | Isoenzyme pattern of enolase in the diagnosis of neuroendocrine bronchopulmonary tumors |
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