Secretion of glycosylated human recombinant haptoglobin in baculovirus-infected insect cells
Human haptoglobin (Hp alpha 2 beta) was synthesized in insect cells using the baculovirus Autographa californica nuclear polyhedrosis virus (AcNPV) as an expression vector. Viruses carrying the proHp alpha 2 beta cDNA, either fused or non fused to viral polyhedrin DNA sequences, expressed intracellu...
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| Veröffentlicht in: | Molecular biology reports 1989-01, Vol.13 (4), p.225-232 |
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| creator | Heinderyckx, M Jacobs, P Bollen, A |
| description | Human haptoglobin (Hp alpha 2 beta) was synthesized in insect cells using the baculovirus Autographa californica nuclear polyhedrosis virus (AcNPV) as an expression vector. Viruses carrying the proHp alpha 2 beta cDNA, either fused or non fused to viral polyhedrin DNA sequences, expressed intracellularly low levels of unglycosylated and non maturated haptoglobin. On the contrary, recombinant viruses containing the preproHp alpha 2 beta cDNA directed the expression of high levels of prohaptoglobin. To a large extent, the uncleaved product was found in the culture medium as a glycosylated molecule. Despite the lack of maturation into subunits, the secreted recombinant prohaptoglobin was able to bind hemoglobin in vitro, although less efficiently than plasma-derived haptoglobin. |
| doi_str_mv | 10.1007/BF00788175 |
| format | Article |
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Viruses carrying the proHp alpha 2 beta cDNA, either fused or non fused to viral polyhedrin DNA sequences, expressed intracellularly low levels of unglycosylated and non maturated haptoglobin. On the contrary, recombinant viruses containing the preproHp alpha 2 beta cDNA directed the expression of high levels of prohaptoglobin. To a large extent, the uncleaved product was found in the culture medium as a glycosylated molecule. Despite the lack of maturation into subunits, the secreted recombinant prohaptoglobin was able to bind hemoglobin in vitro, although less efficiently than plasma-derived haptoglobin.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/BF00788175</identifier><identifier>PMID: 3078448</identifier><language>eng</language><publisher>Netherlands</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; DNA - genetics ; Glycosylation ; Haptoglobins - genetics ; Haptoglobins - metabolism ; Humans ; In Vitro Techniques ; Insect Viruses - genetics ; Insect Viruses - isolation & purification ; Insecta - genetics ; Insecta - microbiology ; Molecular Sequence Data ; Recombinant Proteins - analysis ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - genetics</subject><ispartof>Molecular biology reports, 1989-01, Vol.13 (4), p.225-232</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c282t-8ddda8ce804e60fc1056836f7b6759f33ef57eda8651028e56f4772be3c0418e3</citedby><cites>FETCH-LOGICAL-c282t-8ddda8ce804e60fc1056836f7b6759f33ef57eda8651028e56f4772be3c0418e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3078448$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heinderyckx, M</creatorcontrib><creatorcontrib>Jacobs, P</creatorcontrib><creatorcontrib>Bollen, A</creatorcontrib><title>Secretion of glycosylated human recombinant haptoglobin in baculovirus-infected insect cells</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><description>Human haptoglobin (Hp alpha 2 beta) was synthesized in insect cells using the baculovirus Autographa californica nuclear polyhedrosis virus (AcNPV) as an expression vector. 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Despite the lack of maturation into subunits, the secreted recombinant prohaptoglobin was able to bind hemoglobin in vitro, although less efficiently than plasma-derived haptoglobin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>DNA - genetics</subject><subject>Glycosylation</subject><subject>Haptoglobins - genetics</subject><subject>Haptoglobins - metabolism</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Insect Viruses - genetics</subject><subject>Insect Viruses - isolation & purification</subject><subject>Insecta - genetics</subject><subject>Insecta - microbiology</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Proteins - analysis</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM9LwzAUx4Moc04v3oWcPAjVpEma7KjDqTDwoN6EkqYvW6VNZtIK_e_N2FB4vB_weV_e-yJ0ScktJUTePSxTVopKcYSmVEiW8blUx2hKGKEZV4KeorMYvwghPEETNGGJ51xN0ecbmAB94x32Fq_b0fg4trqHGm-GTjscwPiuapx2Pd7obe_XrU8jTlFpM7T-pwlDzBpnwey2GhdTgw20bTxHJ1a3ES4OdYY-lo_vi-ds9fr0srhfZSZXeZ-puq61MqAIh4JYQ4koFCusrAop5pYxsEJCQgpBSa5AFJZLmVfATPpHAZuh673uNvjvAWJfdk3cXaAd-CGWyRuSBHkCb_agCT7GALbchqbTYSwpKXdWlv9WJvjqoDpUHdR_6ME79gvDXW97</recordid><startdate>19890101</startdate><enddate>19890101</enddate><creator>Heinderyckx, M</creator><creator>Jacobs, P</creator><creator>Bollen, A</creator><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>19890101</creationdate><title>Secretion of glycosylated human recombinant haptoglobin in baculovirus-infected insect cells</title><author>Heinderyckx, M ; Jacobs, P ; Bollen, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c282t-8ddda8ce804e60fc1056836f7b6759f33ef57eda8651028e56f4772be3c0418e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>DNA - genetics</topic><topic>Glycosylation</topic><topic>Haptoglobins - genetics</topic><topic>Haptoglobins - metabolism</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Insect Viruses - genetics</topic><topic>Insect Viruses - isolation & purification</topic><topic>Insecta - genetics</topic><topic>Insecta - microbiology</topic><topic>Molecular Sequence Data</topic><topic>Recombinant Proteins - analysis</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heinderyckx, M</creatorcontrib><creatorcontrib>Jacobs, P</creatorcontrib><creatorcontrib>Bollen, A</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>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heinderyckx, M</au><au>Jacobs, P</au><au>Bollen, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Secretion of glycosylated human recombinant haptoglobin in baculovirus-infected insect cells</atitle><jtitle>Molecular biology reports</jtitle><addtitle>Mol Biol Rep</addtitle><date>1989-01-01</date><risdate>1989</risdate><volume>13</volume><issue>4</issue><spage>225</spage><epage>232</epage><pages>225-232</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>Human haptoglobin (Hp alpha 2 beta) was synthesized in insect cells using the baculovirus Autographa californica nuclear polyhedrosis virus (AcNPV) as an expression vector. Viruses carrying the proHp alpha 2 beta cDNA, either fused or non fused to viral polyhedrin DNA sequences, expressed intracellularly low levels of unglycosylated and non maturated haptoglobin. On the contrary, recombinant viruses containing the preproHp alpha 2 beta cDNA directed the expression of high levels of prohaptoglobin. To a large extent, the uncleaved product was found in the culture medium as a glycosylated molecule. Despite the lack of maturation into subunits, the secreted recombinant prohaptoglobin was able to bind hemoglobin in vitro, although less efficiently than plasma-derived haptoglobin.</abstract><cop>Netherlands</cop><pmid>3078448</pmid><doi>10.1007/BF00788175</doi><tpages>8</tpages></addata></record> |
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| ispartof | Molecular biology reports, 1989-01, Vol.13 (4), p.225-232 |
| issn | 0301-4851 1573-4978 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Animals Base Sequence DNA - genetics Glycosylation Haptoglobins - genetics Haptoglobins - metabolism Humans In Vitro Techniques Insect Viruses - genetics Insect Viruses - isolation & purification Insecta - genetics Insecta - microbiology Molecular Sequence Data Recombinant Proteins - analysis Recombinant Proteins - biosynthesis Recombinant Proteins - genetics |
| title | Secretion of glycosylated human recombinant haptoglobin in baculovirus-infected insect cells |
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