Cancer Isoform of a Tumor-Associated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion
We have described a drug-responsive form of a cell surface NADH oxidase (hydroquinone oxidase) of cancer cells (tNOX) that exhibits unusual characteristics including resistance to proteases, resistance to cyanogen bromide digestion, and an ability to form amyloid filaments closely resembling those o...
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| Veröffentlicht in: | Biochemistry (Easton) 2001-06, Vol.40 (25), p.7351-7354 |
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| container_title | Biochemistry (Easton) |
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| creator | Kelker, Matthew Kim, Chinpal Chueh, Pin-Ju Guimont, Rodney Morré, Dorothy M Morré, D. James |
| description | We have described a drug-responsive form of a cell surface NADH oxidase (hydroquinone oxidase) of cancer cells (tNOX) that exhibits unusual characteristics including resistance to proteases, resistance to cyanogen bromide digestion, and an ability to form amyloid filaments closely resembling those of spongiform encephalopathies and all of which are characteristics of PrPsc (PrPres), the presumed infective and proteinase K resistant particle of the scrapie prion. The tNOX protein from the HeLa cell surface copurified with authentic glyceraldehyde-3-phosphate dehydrogenase (muscle form) (GAPDH). Surprisingly, the tNOX-associated muscle GAPDH also was proteinase K resistant. In this paper, we show that combination of authentic rabbit muscle GAPDH with tNOX renders the GAPDH resistant to proteinase K digestion. This property, that of converting the normal form of a protein into a likeness of itself, is one of the defining characteristics of the group of proteins designated as prions. |
| doi_str_mv | 10.1021/bi010596i |
| format | Article |
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James</creatorcontrib><title>Cancer Isoform of a Tumor-Associated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>We have described a drug-responsive form of a cell surface NADH oxidase (hydroquinone oxidase) of cancer cells (tNOX) that exhibits unusual characteristics including resistance to proteases, resistance to cyanogen bromide digestion, and an ability to form amyloid filaments closely resembling those of spongiform encephalopathies and all of which are characteristics of PrPsc (PrPres), the presumed infective and proteinase K resistant particle of the scrapie prion. The tNOX protein from the HeLa cell surface copurified with authentic glyceraldehyde-3-phosphate dehydrogenase (muscle form) (GAPDH). Surprisingly, the tNOX-associated muscle GAPDH also was proteinase K resistant. In this paper, we show that combination of authentic rabbit muscle GAPDH with tNOX renders the GAPDH resistant to proteinase K digestion. This property, that of converting the normal form of a protein into a likeness of itself, is one of the defining characteristics of the group of proteins designated as prions.</description><subject>Animals</subject><subject>Endopeptidase K - metabolism</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>NADH, NADPH Oxidoreductases - chemistry</subject><subject>NADH, NADPH Oxidoreductases - genetics</subject><subject>NADH, NADPH Oxidoreductases - metabolism</subject><subject>Neoplasm Proteins - chemistry</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Peptide Fragments - biosynthesis</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - metabolism</subject><subject>Prions - chemistry</subject><subject>Prions - genetics</subject><subject>Prions - metabolism</subject><subject>PrPSc Proteins - chemistry</subject><subject>PrPSc Proteins - metabolism</subject><subject>Rabbits</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMFqGzEQhkVJqZ2kh7xA0CWlPmwrraSVdXS3SW0wtoMXmpuQtbOgxGs50i6kb1-FNe6lp2GYj39-PoRuKPlGSU6_7xyhRKjCfUBjKnKScaXEBRoTQoosVwUZocsYn9PKieSf0IhSTnMyVWOkS3OwEPAi-saHFvsGG1z1rQ_ZLEZvnemgxiXs93jbh8ZYwKvZzzlev7naRMBfu9X6aYLnJuJN8EcInYM4pGyC84dr9LEx-wifT_MKVQ_3VTnPlutfi3K2zAzjqsuKXBgKuVWq5oal2kbuCICVggEwWijJprzmokgF7E6CzHltLcsNa6aWWHaFvgyxx-Bfe4idbl20qbU5gO-jlkQxKsQ0gZMBtMHHGKDRx-BaE_5oSvS7TH2WmdjbU2i_a6H-R57sJSAbABc7eDvfTXjRhWRS6Gqz1avHakXJ71L_SPzdwBsb9bPvwyEp-c_jvytniI8</recordid><startdate>20010626</startdate><enddate>20010626</enddate><creator>Kelker, Matthew</creator><creator>Kim, Chinpal</creator><creator>Chueh, Pin-Ju</creator><creator>Guimont, Rodney</creator><creator>Morré, Dorothy M</creator><creator>Morré, D. James</creator><general>American Chemical Society</general><scope>BSCLL</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>20010626</creationdate><title>Cancer Isoform of a Tumor-Associated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion</title><author>Kelker, Matthew ; Kim, Chinpal ; Chueh, Pin-Ju ; Guimont, Rodney ; Morré, Dorothy M ; Morré, D. James</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a349t-625a1e2c99d4a3006a7b0eec753ee31697384d456acecb7e724dcc32a3f8c0c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Endopeptidase K - metabolism</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>NADH, NADPH Oxidoreductases - chemistry</topic><topic>NADH, NADPH Oxidoreductases - genetics</topic><topic>NADH, NADPH Oxidoreductases - metabolism</topic><topic>Neoplasm Proteins - chemistry</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Peptide Fragments - biosynthesis</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - metabolism</topic><topic>Prions - chemistry</topic><topic>Prions - genetics</topic><topic>Prions - metabolism</topic><topic>PrPSc Proteins - chemistry</topic><topic>PrPSc Proteins - metabolism</topic><topic>Rabbits</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kelker, Matthew</creatorcontrib><creatorcontrib>Kim, Chinpal</creatorcontrib><creatorcontrib>Chueh, Pin-Ju</creatorcontrib><creatorcontrib>Guimont, Rodney</creatorcontrib><creatorcontrib>Morré, Dorothy M</creatorcontrib><creatorcontrib>Morré, D. 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James</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cancer Isoform of a Tumor-Associated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2001-06-26</date><risdate>2001</risdate><volume>40</volume><issue>25</issue><spage>7351</spage><epage>7354</epage><pages>7351-7354</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>We have described a drug-responsive form of a cell surface NADH oxidase (hydroquinone oxidase) of cancer cells (tNOX) that exhibits unusual characteristics including resistance to proteases, resistance to cyanogen bromide digestion, and an ability to form amyloid filaments closely resembling those of spongiform encephalopathies and all of which are characteristics of PrPsc (PrPres), the presumed infective and proteinase K resistant particle of the scrapie prion. The tNOX protein from the HeLa cell surface copurified with authentic glyceraldehyde-3-phosphate dehydrogenase (muscle form) (GAPDH). Surprisingly, the tNOX-associated muscle GAPDH also was proteinase K resistant. In this paper, we show that combination of authentic rabbit muscle GAPDH with tNOX renders the GAPDH resistant to proteinase K digestion. This property, that of converting the normal form of a protein into a likeness of itself, is one of the defining characteristics of the group of proteins designated as prions.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>11412089</pmid><doi>10.1021/bi010596i</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals Endopeptidase K - metabolism Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism HeLa Cells Humans Hydrolysis Isoenzymes - chemistry Isoenzymes - genetics Isoenzymes - metabolism NADH, NADPH Oxidoreductases - chemistry NADH, NADPH Oxidoreductases - genetics NADH, NADPH Oxidoreductases - metabolism Neoplasm Proteins - chemistry Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Peptide Fragments - biosynthesis Peptide Fragments - genetics Peptide Fragments - metabolism Prions - chemistry Prions - genetics Prions - metabolism PrPSc Proteins - chemistry PrPSc Proteins - metabolism Rabbits Recombinant Proteins - biosynthesis Recombinant Proteins - metabolism |
| title | Cancer Isoform of a Tumor-Associated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion |
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