hsp150Δ‐carrier confers secretion competence to the rat nerve growth factor receptor ectodomain in Saccharomyces cerevisiae
When the extracellular domain of rat low‐affinity nerve growth factor receptor (NGFRe) was synthesized in Saccharomyces cerevisiae with the signal peptide of invertase, NGFRe was translocated to the endoplasmic reticulum (ER) and retained there. However, when NGFRe was fused to the C‐terminus of the...
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| Veröffentlicht in: | Yeast (Chichester, England) England), 1996-04, Vol.12 (5), p.457-466 |
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| creator | Simonen, Marjo Vihinen, Helena Jämsä, Eija Arumäe, Urmas Kalkkinen, Nisse Makarow, Marja |
| description | When the extracellular domain of rat low‐affinity nerve growth factor receptor (NGFRe) was synthesized in Saccharomyces cerevisiae with the signal peptide of invertase, NGFRe was translocated to the endoplasmic reticulum (ER) and retained there. However, when NGFRe was fused to the C‐terminus of the hsp150Δ‐carrier, the hsp150Δ-NGFRe fusion protein was efficiently secreted to the growth medium with no apparent retention in the ER. The NGFRe portion was disulphide‐bonded and its single N‐glycosylation site was occupied. The hsp150Δ‐carrier is an N‐terminal signal peptide‐containing fragment of a yeast secretory glycoprotein. Hsp150Δ-NGFRe, harvested from the culture medium, inhibited the cross‐linking of [¹²⁵I]NGF to authentic NGFR on the surface of human melanoma cells. Moreover, [¹²⁵I]NGF could be chemically cross‐linked to secretory hsp150Δ-NGFRe, suggesting that the NGFRe portion had adopted a ligand‐binding conformation. However, inhibition of the cross‐linking by unlabelled NGF was less effective than in the case of the authentic receptor. The hsp150Δ‐carrier may have potential in the production of mammalian proteins, which require elaborate folding and disulphide formation in the ER. |
| doi_str_mv | 10.1002/(SICI)1097-0061(199604)12:5<457::AID-YEA930>3.0.CO;2-D |
| format | Article |
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However, when NGFRe was fused to the C‐terminus of the hsp150Δ‐carrier, the hsp150Δ-NGFRe fusion protein was efficiently secreted to the growth medium with no apparent retention in the ER. The NGFRe portion was disulphide‐bonded and its single N‐glycosylation site was occupied. The hsp150Δ‐carrier is an N‐terminal signal peptide‐containing fragment of a yeast secretory glycoprotein. Hsp150Δ-NGFRe, harvested from the culture medium, inhibited the cross‐linking of [¹²⁵I]NGF to authentic NGFR on the surface of human melanoma cells. Moreover, [¹²⁵I]NGF could be chemically cross‐linked to secretory hsp150Δ-NGFRe, suggesting that the NGFRe portion had adopted a ligand‐binding conformation. However, inhibition of the cross‐linking by unlabelled NGF was less effective than in the case of the authentic receptor. The hsp150Δ‐carrier may have potential in the production of mammalian proteins, which require elaborate folding and disulphide formation in the ER.</description><identifier>ISSN: 0749-503X</identifier><identifier>EISSN: 1097-0061</identifier><identifier>DOI: 10.1002/(SICI)1097-0061(199604)12:5<457::AID-YEA930>3.0.CO;2-D</identifier><identifier>PMID: 8740419</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; Base Sequence ; beta-Fructofuranosidase ; Biological Transport ; Disulfides ; Endoplasmic Reticulum - metabolism ; Glycoproteins ; Glycoside Hydrolases - genetics ; Glycosylation ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - metabolism ; hsp150 protein ; Humans ; Melanoma ; Molecular Sequence Data ; Nerve Growth Factors - metabolism ; NGFR ; Peptide Fragments - metabolism ; protein production ; Protein Sorting Signals - genetics ; Rats ; Receptor, Nerve Growth Factor ; Receptors, Nerve Growth Factor - genetics ; Receptors, Nerve Growth Factor - metabolism ; Recombinant Fusion Proteins - isolation & purification ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins ; secretion ; Tumor Cells, Cultured ; yeast</subject><ispartof>Yeast (Chichester, England), 1996-04, Vol.12 (5), p.457-466</ispartof><rights>Copyright © 1996 John Wiley & Sons Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4210-32f36719502c2261741f1cb6972640700c76e6e1b21226f461fa5bd1c56dfc133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F%28SICI%291097-0061%28199604%2912%3A5%3C457%3A%3AAID-YEA930%3E3.0.CO%3B2-D$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F%28SICI%291097-0061%28199604%2912%3A5%3C457%3A%3AAID-YEA930%3E3.0.CO%3B2-D$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8740419$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Simonen, Marjo</creatorcontrib><creatorcontrib>Vihinen, Helena</creatorcontrib><creatorcontrib>Jämsä, Eija</creatorcontrib><creatorcontrib>Arumäe, Urmas</creatorcontrib><creatorcontrib>Kalkkinen, Nisse</creatorcontrib><creatorcontrib>Makarow, Marja</creatorcontrib><title>hsp150Δ‐carrier confers secretion competence to the rat nerve growth factor receptor ectodomain in Saccharomyces cerevisiae</title><title>Yeast (Chichester, England)</title><addtitle>Yeast</addtitle><description>When the extracellular domain of rat low‐affinity nerve growth factor receptor (NGFRe) was synthesized in Saccharomyces cerevisiae with the signal peptide of invertase, NGFRe was translocated to the endoplasmic reticulum (ER) and retained there. However, when NGFRe was fused to the C‐terminus of the hsp150Δ‐carrier, the hsp150Δ-NGFRe fusion protein was efficiently secreted to the growth medium with no apparent retention in the ER. The NGFRe portion was disulphide‐bonded and its single N‐glycosylation site was occupied. The hsp150Δ‐carrier is an N‐terminal signal peptide‐containing fragment of a yeast secretory glycoprotein. Hsp150Δ-NGFRe, harvested from the culture medium, inhibited the cross‐linking of [¹²⁵I]NGF to authentic NGFR on the surface of human melanoma cells. Moreover, [¹²⁵I]NGF could be chemically cross‐linked to secretory hsp150Δ-NGFRe, suggesting that the NGFRe portion had adopted a ligand‐binding conformation. However, inhibition of the cross‐linking by unlabelled NGF was less effective than in the case of the authentic receptor. The hsp150Δ‐carrier may have potential in the production of mammalian proteins, which require elaborate folding and disulphide formation in the ER.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>beta-Fructofuranosidase</subject><subject>Biological Transport</subject><subject>Disulfides</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Glycoproteins</subject><subject>Glycoside Hydrolases - genetics</subject><subject>Glycosylation</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>hsp150 protein</subject><subject>Humans</subject><subject>Melanoma</subject><subject>Molecular Sequence Data</subject><subject>Nerve Growth Factors - metabolism</subject><subject>NGFR</subject><subject>Peptide Fragments - metabolism</subject><subject>protein production</subject><subject>Protein Sorting Signals - genetics</subject><subject>Rats</subject><subject>Receptor, Nerve Growth Factor</subject><subject>Receptors, Nerve Growth Factor - genetics</subject><subject>Receptors, Nerve Growth Factor - metabolism</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>secretion</subject><subject>Tumor Cells, Cultured</subject><subject>yeast</subject><issn>0749-503X</issn><issn>1097-0061</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdFu0zAUhiMEGmXwCAhfoe0i5Rw7cZKBJlXtgEqTelGGxtWR656sQU1c7HRTbxCPwAXPxUPwJKRKtRuQJlmyff7f_2_pi6JzhCECyDcn8-l4eopQZDGAxhMsCg3JKcqz9F2SZmdno-kk_nIxKhScqyEMx7O3Mp48igb3Tx5HA8iSIk5BXT-NnoXwFQAxlflRdJRnCSRYDKLvq7DBFH7_-vPjpzXeV-yFdU3JPojA1nNbuaab1BtuubEsWifaFQtvWtGwv2Vx491duxKlsa3zwrPlzf7A3XXpalM1oltzY-3KeFfvLAdh2fNtFSrDz6MnpVkHfnHYj6Or9xefxh_jy9mH6Xh0GdtEIsRKlkpnWKQgrZQaswRLtAtdZFInkAHYTLNmXEjs5DLRWJp0sUSb6mVpUanj6HWfu_Hu25ZDS3UVLK_XpmG3DZTlmOdKyQeNmOYFYKI74-feaL0LwXNJG1_Vxu8IgfYEifYEaY-D9jioJ0goKaWOIFFHkHqCpAhoPCNJky745eEH20XNy_vYA7JOv-71u2rNu39aHyj9b-dh0kW_6qNL48jc-CrQ1VwCKsACk1yD-gv-a8IS</recordid><startdate>199604</startdate><enddate>199604</enddate><creator>Simonen, Marjo</creator><creator>Vihinen, Helena</creator><creator>Jämsä, Eija</creator><creator>Arumäe, Urmas</creator><creator>Kalkkinen, Nisse</creator><creator>Makarow, Marja</creator><general>John Wiley & Sons, Ltd</general><scope>FBQ</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>199604</creationdate><title>hsp150Δ‐carrier confers secretion competence to the rat nerve growth factor receptor ectodomain in Saccharomyces cerevisiae</title><author>Simonen, Marjo ; Vihinen, Helena ; Jämsä, Eija ; Arumäe, Urmas ; Kalkkinen, Nisse ; Makarow, Marja</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4210-32f36719502c2261741f1cb6972640700c76e6e1b21226f461fa5bd1c56dfc133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>beta-Fructofuranosidase</topic><topic>Biological Transport</topic><topic>Disulfides</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Glycoproteins</topic><topic>Glycoside Hydrolases - genetics</topic><topic>Glycosylation</topic><topic>Heat-Shock Proteins - genetics</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>hsp150 protein</topic><topic>Humans</topic><topic>Melanoma</topic><topic>Molecular Sequence Data</topic><topic>Nerve Growth Factors - metabolism</topic><topic>NGFR</topic><topic>Peptide Fragments - metabolism</topic><topic>protein production</topic><topic>Protein Sorting Signals - genetics</topic><topic>Rats</topic><topic>Receptor, Nerve Growth Factor</topic><topic>Receptors, Nerve Growth Factor - genetics</topic><topic>Receptors, Nerve Growth Factor - metabolism</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>secretion</topic><topic>Tumor Cells, Cultured</topic><topic>yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Simonen, Marjo</creatorcontrib><creatorcontrib>Vihinen, Helena</creatorcontrib><creatorcontrib>Jämsä, Eija</creatorcontrib><creatorcontrib>Arumäe, Urmas</creatorcontrib><creatorcontrib>Kalkkinen, Nisse</creatorcontrib><creatorcontrib>Makarow, Marja</creatorcontrib><collection>AGRIS</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Yeast (Chichester, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simonen, Marjo</au><au>Vihinen, Helena</au><au>Jämsä, Eija</au><au>Arumäe, Urmas</au><au>Kalkkinen, Nisse</au><au>Makarow, Marja</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>hsp150Δ‐carrier confers secretion competence to the rat nerve growth factor receptor ectodomain in Saccharomyces cerevisiae</atitle><jtitle>Yeast (Chichester, England)</jtitle><addtitle>Yeast</addtitle><date>1996-04</date><risdate>1996</risdate><volume>12</volume><issue>5</issue><spage>457</spage><epage>466</epage><pages>457-466</pages><issn>0749-503X</issn><eissn>1097-0061</eissn><abstract>When the extracellular domain of rat low‐affinity nerve growth factor receptor (NGFRe) was synthesized in Saccharomyces cerevisiae with the signal peptide of invertase, NGFRe was translocated to the endoplasmic reticulum (ER) and retained there. However, when NGFRe was fused to the C‐terminus of the hsp150Δ‐carrier, the hsp150Δ-NGFRe fusion protein was efficiently secreted to the growth medium with no apparent retention in the ER. The NGFRe portion was disulphide‐bonded and its single N‐glycosylation site was occupied. The hsp150Δ‐carrier is an N‐terminal signal peptide‐containing fragment of a yeast secretory glycoprotein. Hsp150Δ-NGFRe, harvested from the culture medium, inhibited the cross‐linking of [¹²⁵I]NGF to authentic NGFR on the surface of human melanoma cells. Moreover, [¹²⁵I]NGF could be chemically cross‐linked to secretory hsp150Δ-NGFRe, suggesting that the NGFRe portion had adopted a ligand‐binding conformation. However, inhibition of the cross‐linking by unlabelled NGF was less effective than in the case of the authentic receptor. The hsp150Δ‐carrier may have potential in the production of mammalian proteins, which require elaborate folding and disulphide formation in the ER.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>8740419</pmid><doi>10.1002/(SICI)1097-0061(199604)12:5<457::AID-YEA930>3.0.CO;2-D</doi><tpages>10</tpages></addata></record> |
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| identifier | ISSN: 0749-503X |
| ispartof | Yeast (Chichester, England), 1996-04, Vol.12 (5), p.457-466 |
| issn | 0749-503X 1097-0061 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; Wiley Free Content |
| subjects | Animals Base Sequence beta-Fructofuranosidase Biological Transport Disulfides Endoplasmic Reticulum - metabolism Glycoproteins Glycoside Hydrolases - genetics Glycosylation Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism hsp150 protein Humans Melanoma Molecular Sequence Data Nerve Growth Factors - metabolism NGFR Peptide Fragments - metabolism protein production Protein Sorting Signals - genetics Rats Receptor, Nerve Growth Factor Receptors, Nerve Growth Factor - genetics Receptors, Nerve Growth Factor - metabolism Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins secretion Tumor Cells, Cultured yeast |
| title | hsp150Δ‐carrier confers secretion competence to the rat nerve growth factor receptor ectodomain in Saccharomyces cerevisiae |
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