The expression of Cox17p in rodent tissues and cells
Previous works have reported the isolation of a novel polypeptide from porcine heart. Structural analysis has shown that it is a mammalian homologue of Cox17p, believed essential for the assembly of functional cytochrome c oxidase and delivery of copper ions to the mitochondrion for insertion into t...
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Veröffentlicht in: | European journal of biochemistry 2000-11, Vol.267 (22), p.6699-6707 |
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description | Previous works have reported the isolation of a novel polypeptide from porcine heart. Structural analysis has shown that it is a mammalian homologue of Cox17p, believed essential for the assembly of functional cytochrome c oxidase and delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast. Although the human, mouse and porcine homologs of this small protein have already been cloned or purified, the function of Cox17p in the mammalian system has not yet been elucidated. To investigate the physiological function of Cox17p in mammals, we performed Northern blot analysis using probes containing the mouse and rat sequences obtained by RT‐PCR. The hybridization signals were detected in all mouse tissues, but notably intense signals were observed in heart, brain and kidney RNA samples. Some of the neuroendocrine and endocrine cell lines showed higher expression levels than fibroblasts. The highest expression level of Cox17p mRNA in mouse brain was observed in the pituitary sample. While in rat heart, Cox17p mRNA expression was detected from early development, in rat brain, embryonic and postnatal changes in the expression were observed. Immunocytochemical analysis showed that Cox17p immunoreactivity was strong in the pituitary cell line, AtT‐20. These findings suggested that Cox17p is not only part of the respiratory chain but also involved in brain and endocrine functions. |
doi_str_mv | 10.1046/j.1432-1327.2000.01771.x |
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Structural analysis has shown that it is a mammalian homologue of Cox17p, believed essential for the assembly of functional cytochrome c oxidase and delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast. Although the human, mouse and porcine homologs of this small protein have already been cloned or purified, the function of Cox17p in the mammalian system has not yet been elucidated. To investigate the physiological function of Cox17p in mammals, we performed Northern blot analysis using probes containing the mouse and rat sequences obtained by RT‐PCR. The hybridization signals were detected in all mouse tissues, but notably intense signals were observed in heart, brain and kidney RNA samples. Some of the neuroendocrine and endocrine cell lines showed higher expression levels than fibroblasts. The highest expression level of Cox17p mRNA in mouse brain was observed in the pituitary sample. While in rat heart, Cox17p mRNA expression was detected from early development, in rat brain, embryonic and postnatal changes in the expression were observed. Immunocytochemical analysis showed that Cox17p immunoreactivity was strong in the pituitary cell line, AtT‐20. These findings suggested that Cox17p is not only part of the respiratory chain but also involved in brain and endocrine functions.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1046/j.1432-1327.2000.01771.x</identifier><identifier>PMID: 11054125</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>3T3 Cells ; Aging ; Amino Acid Sequence ; Animals ; Brain - enzymology ; Carrier Proteins ; Cation Transport Proteins ; Cell Line ; copper recruitment ; Cox17p ; Electron Transport Complex IV - genetics ; Embryonic and Fetal Development ; endocrine cells ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Humans ; Kidney - enzymology ; L Cells (Cell Line) ; Male ; Mice ; Mice, Inbred ICR ; Molecular Chaperones ; Molecular Sequence Data ; Myocardium - enzymology ; PC12 Cells ; pituitary ; Proteins - genetics ; Rats ; Rats, Wistar ; Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Sequence Homology, Nucleic Acid ; Swine ; tissue distribution ; Tumor Cells, Cultured</subject><ispartof>European journal of biochemistry, 2000-11, Vol.267 (22), p.6699-6707</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4821-51792d8b71d65a553841a2f91f63e7d92ab7394e515b4627c5ad9ff347f967e83</citedby><cites>FETCH-LOGICAL-c4821-51792d8b71d65a553841a2f91f63e7d92ab7394e515b4627c5ad9ff347f967e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1432-1327.2000.01771.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1432-1327.2000.01771.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27907,27908,45557,45558</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11054125$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kako, Koichiro</creatorcontrib><creatorcontrib>Tsumori, Keiko</creatorcontrib><creatorcontrib>Ohmasa, Yoshitaka</creatorcontrib><creatorcontrib>Takahashi, Yoshinori</creatorcontrib><creatorcontrib>Munekata, Eisuke</creatorcontrib><title>The expression of Cox17p in rodent tissues and cells</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Previous works have reported the isolation of a novel polypeptide from porcine heart. Structural analysis has shown that it is a mammalian homologue of Cox17p, believed essential for the assembly of functional cytochrome c oxidase and delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast. Although the human, mouse and porcine homologs of this small protein have already been cloned or purified, the function of Cox17p in the mammalian system has not yet been elucidated. To investigate the physiological function of Cox17p in mammals, we performed Northern blot analysis using probes containing the mouse and rat sequences obtained by RT‐PCR. The hybridization signals were detected in all mouse tissues, but notably intense signals were observed in heart, brain and kidney RNA samples. Some of the neuroendocrine and endocrine cell lines showed higher expression levels than fibroblasts. The highest expression level of Cox17p mRNA in mouse brain was observed in the pituitary sample. While in rat heart, Cox17p mRNA expression was detected from early development, in rat brain, embryonic and postnatal changes in the expression were observed. Immunocytochemical analysis showed that Cox17p immunoreactivity was strong in the pituitary cell line, AtT‐20. These findings suggested that Cox17p is not only part of the respiratory chain but also involved in brain and endocrine functions.</description><subject>3T3 Cells</subject><subject>Aging</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Brain - enzymology</subject><subject>Carrier Proteins</subject><subject>Cation Transport Proteins</subject><subject>Cell Line</subject><subject>copper recruitment</subject><subject>Cox17p</subject><subject>Electron Transport Complex IV - genetics</subject><subject>Embryonic and Fetal Development</subject><subject>endocrine cells</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Humans</subject><subject>Kidney - enzymology</subject><subject>L Cells (Cell Line)</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Molecular Chaperones</subject><subject>Molecular Sequence Data</subject><subject>Myocardium - enzymology</subject><subject>PC12 Cells</subject><subject>pituitary</subject><subject>Proteins - genetics</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Swine</subject><subject>tissue distribution</subject><subject>Tumor Cells, Cultured</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1Lw0AQhhdRbK3-BdmTt8Sd_cxeBC2tCgUP1vOySXYxJU1itsH035uYgldPMzDPzLw8CGEgMRAu73cxcEYjYFTFlBASE1AK4v4MzacBYewczQkBHlEt5AxdhbAbQKmlukQzACI4UDFHfPvpsOub1oVQ1BWuPV7WPagGFxVu69xVB3woQuhcwLbKcebKMlyjC2_L4G5OdYE-1qvt8iXavD2_Lh83UcYTCpEApWmepApyKawQLOFgqdfgJXMq19SmimnuBIiUS6oyYXPtPePKDzFdwhbobrrbtPXXkOBg9kUYE9jK1V0wijIpNVUDmExg1tYhtM6bpi32tj0aIGY0ZnZmFGNGY2Y0Zn6NmX5YvT396NK9y_8WT4oG4GECvovSHf992KxXT-9jy34AjQl3kA</recordid><startdate>200011</startdate><enddate>200011</enddate><creator>Kako, Koichiro</creator><creator>Tsumori, Keiko</creator><creator>Ohmasa, Yoshitaka</creator><creator>Takahashi, Yoshinori</creator><creator>Munekata, Eisuke</creator><general>Blackwell Science Ltd</general><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>200011</creationdate><title>The expression of Cox17p in rodent tissues and cells</title><author>Kako, Koichiro ; Tsumori, Keiko ; Ohmasa, Yoshitaka ; Takahashi, Yoshinori ; Munekata, Eisuke</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4821-51792d8b71d65a553841a2f91f63e7d92ab7394e515b4627c5ad9ff347f967e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>3T3 Cells</topic><topic>Aging</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Brain - enzymology</topic><topic>Carrier Proteins</topic><topic>Cation Transport Proteins</topic><topic>Cell Line</topic><topic>copper recruitment</topic><topic>Cox17p</topic><topic>Electron Transport Complex IV - genetics</topic><topic>Embryonic and Fetal Development</topic><topic>endocrine cells</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Humans</topic><topic>Kidney - enzymology</topic><topic>L Cells (Cell Line)</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Molecular Chaperones</topic><topic>Molecular Sequence Data</topic><topic>Myocardium - enzymology</topic><topic>PC12 Cells</topic><topic>pituitary</topic><topic>Proteins - genetics</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Swine</topic><topic>tissue distribution</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kako, Koichiro</creatorcontrib><creatorcontrib>Tsumori, Keiko</creatorcontrib><creatorcontrib>Ohmasa, Yoshitaka</creatorcontrib><creatorcontrib>Takahashi, Yoshinori</creatorcontrib><creatorcontrib>Munekata, Eisuke</creatorcontrib><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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kako, Koichiro</au><au>Tsumori, Keiko</au><au>Ohmasa, Yoshitaka</au><au>Takahashi, Yoshinori</au><au>Munekata, Eisuke</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The expression of Cox17p in rodent tissues and cells</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2000-11</date><risdate>2000</risdate><volume>267</volume><issue>22</issue><spage>6699</spage><epage>6707</epage><pages>6699-6707</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Previous works have reported the isolation of a novel polypeptide from porcine heart. Structural analysis has shown that it is a mammalian homologue of Cox17p, believed essential for the assembly of functional cytochrome c oxidase and delivery of copper ions to the mitochondrion for insertion into the enzyme in yeast. Although the human, mouse and porcine homologs of this small protein have already been cloned or purified, the function of Cox17p in the mammalian system has not yet been elucidated. To investigate the physiological function of Cox17p in mammals, we performed Northern blot analysis using probes containing the mouse and rat sequences obtained by RT‐PCR. The hybridization signals were detected in all mouse tissues, but notably intense signals were observed in heart, brain and kidney RNA samples. Some of the neuroendocrine and endocrine cell lines showed higher expression levels than fibroblasts. The highest expression level of Cox17p mRNA in mouse brain was observed in the pituitary sample. While in rat heart, Cox17p mRNA expression was detected from early development, in rat brain, embryonic and postnatal changes in the expression were observed. Immunocytochemical analysis showed that Cox17p immunoreactivity was strong in the pituitary cell line, AtT‐20. These findings suggested that Cox17p is not only part of the respiratory chain but also involved in brain and endocrine functions.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>11054125</pmid><doi>10.1046/j.1432-1327.2000.01771.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 3T3 Cells Aging Amino Acid Sequence Animals Brain - enzymology Carrier Proteins Cation Transport Proteins Cell Line copper recruitment Cox17p Electron Transport Complex IV - genetics Embryonic and Fetal Development endocrine cells Gene Expression Regulation, Developmental Gene Expression Regulation, Enzymologic Humans Kidney - enzymology L Cells (Cell Line) Male Mice Mice, Inbred ICR Molecular Chaperones Molecular Sequence Data Myocardium - enzymology PC12 Cells pituitary Proteins - genetics Rats Rats, Wistar Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Homology, Nucleic Acid Swine tissue distribution Tumor Cells, Cultured |
title | The expression of Cox17p in rodent tissues and cells |
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