Different transforming growth factor-α species are derived from a glycosylated and palmitoylated transmembrane precursor
cDNA analysis has revealed that the 50 amino acid transforming growth factor-α (TGF-α) is derived from a 160 amino acid precursor. Antibodies to TGF-α and to a C-terminal portion of the precursor were used to study the biosynthesis and processing of the precursor. CHO cells transfected with a TGF-α...
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| Veröffentlicht in: | Cell 1987-02, Vol.48 (3), p.429-440 |
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| creator | Bringman, Timothy S. Lindquist, Patricia B. Derynck, Rik |
| description | cDNA analysis has revealed that the 50 amino acid transforming growth factor-α (TGF-α) is derived from a 160 amino acid precursor. Antibodies to TGF-α and to a C-terminal portion of the precursor were used to study the biosynthesis and processing of the precursor. CHO cells transfected with a TGF-α expression vector secrete high levels of TGF-α; a mixture of species of about 18 kd is secreted in addition to the 50 amino acid form. These larger species are N-glycosylated and are derived from the same precursor as the smaller form. The C-terminal segment of the precursor remains anchored in the membrane and has covalently attached palmitate. The newly synthesized TGF-α precursor is thus a transmembrane protein that subsequently undergoes external proteolytic cleavages, releasing several TGF-α species. |
| doi_str_mv | 10.1016/0092-8674(87)90194-2 |
| format | Article |
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Antibodies to TGF-α and to a C-terminal portion of the precursor were used to study the biosynthesis and processing of the precursor. CHO cells transfected with a TGF-α expression vector secrete high levels of TGF-α; a mixture of species of about 18 kd is secreted in addition to the 50 amino acid form. These larger species are N-glycosylated and are derived from the same precursor as the smaller form. The C-terminal segment of the precursor remains anchored in the membrane and has covalently attached palmitate. The newly synthesized TGF-α precursor is thus a transmembrane protein that subsequently undergoes external proteolytic cleavages, releasing several TGF-α species.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(87)90194-2</identifier><identifier>PMID: 3467848</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antibodies ; Cell Line ; Cell Membrane - metabolism ; Cricetinae ; Glycosylation ; Membrane Proteins - metabolism ; Palmitates - metabolism ; Peptides - immunology ; Peptides - metabolism ; Protein Precursors - immunology ; Protein Precursors - metabolism ; Protein Processing, Post-Translational ; Transforming Growth Factors</subject><ispartof>Cell, 1987-02, Vol.48 (3), p.429-440</ispartof><rights>1987</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-38d856a98e7c84948996ac5f65d1cb36e463fd80e4465b585da26ebfdb611c573</citedby><cites>FETCH-LOGICAL-c357t-38d856a98e7c84948996ac5f65d1cb36e463fd80e4465b585da26ebfdb611c573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0092-8674(87)90194-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3467848$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bringman, Timothy S.</creatorcontrib><creatorcontrib>Lindquist, Patricia B.</creatorcontrib><creatorcontrib>Derynck, Rik</creatorcontrib><title>Different transforming growth factor-α species are derived from a glycosylated and palmitoylated transmembrane precursor</title><title>Cell</title><addtitle>Cell</addtitle><description>cDNA analysis has revealed that the 50 amino acid transforming growth factor-α (TGF-α) is derived from a 160 amino acid precursor. 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The newly synthesized TGF-α precursor is thus a transmembrane protein that subsequently undergoes external proteolytic cleavages, releasing several TGF-α species.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cricetinae</subject><subject>Glycosylation</subject><subject>Membrane Proteins - metabolism</subject><subject>Palmitates - metabolism</subject><subject>Peptides - immunology</subject><subject>Peptides - metabolism</subject><subject>Protein Precursors - immunology</subject><subject>Protein Precursors - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Transforming Growth Factors</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1uFDEQhS1ElAyBG4DkVQSLTuxu_24iRUkgkSKxgbXltsuDUXe7Y3uC5lhcJGeiJzPKklVJr169qvoQ-kjJOSVUXBCi20YJyT4r-UUTqlnTvkErSrRsGJXtW7R6tZygd6X8JoQozvkxOu6YkIqpFdrexBAgw1RxzXYqIeUxTmu8zulP_YWDdTXl5vkvLjO4CAXbDNhDjk_gcchpxBavh61LZTvYumh28ni2wxhrOigvuSOM_VIBzxncJpeU36OjYIcCHw71FP38evvj-q55-P7t_vrqoXEdl7XplFdcWK1AOsU0U1oL63gQ3FPXdwKY6IJXBBgTvOeKe9sK6IPvBaWOy-4Une1z55weN1CqGWNxMAzLNWlTjJSd0KrbGdne6HIqJUMwc46jzVtDidkRNzucZofTKGleiJt2Gft0yN_0I_jXoQPipX-578Py5FOEbMoCcnLg44KiGp_i_xf8A2rWk9A</recordid><startdate>19870213</startdate><enddate>19870213</enddate><creator>Bringman, Timothy S.</creator><creator>Lindquist, Patricia B.</creator><creator>Derynck, Rik</creator><general>Elsevier Inc</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>19870213</creationdate><title>Different transforming growth factor-α species are derived from a glycosylated and palmitoylated transmembrane precursor</title><author>Bringman, Timothy S. ; Lindquist, Patricia B. ; Derynck, Rik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-38d856a98e7c84948996ac5f65d1cb36e463fd80e4465b585da26ebfdb611c573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Cricetinae</topic><topic>Glycosylation</topic><topic>Membrane Proteins - metabolism</topic><topic>Palmitates - metabolism</topic><topic>Peptides - immunology</topic><topic>Peptides - metabolism</topic><topic>Protein Precursors - immunology</topic><topic>Protein Precursors - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Transforming Growth Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bringman, Timothy S.</creatorcontrib><creatorcontrib>Lindquist, Patricia B.</creatorcontrib><creatorcontrib>Derynck, Rik</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>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bringman, Timothy S.</au><au>Lindquist, Patricia B.</au><au>Derynck, Rik</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Different transforming growth factor-α species are derived from a glycosylated and palmitoylated transmembrane precursor</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1987-02-13</date><risdate>1987</risdate><volume>48</volume><issue>3</issue><spage>429</spage><epage>440</epage><pages>429-440</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>cDNA analysis has revealed that the 50 amino acid transforming growth factor-α (TGF-α) is derived from a 160 amino acid precursor. Antibodies to TGF-α and to a C-terminal portion of the precursor were used to study the biosynthesis and processing of the precursor. CHO cells transfected with a TGF-α expression vector secrete high levels of TGF-α; a mixture of species of about 18 kd is secreted in addition to the 50 amino acid form. These larger species are N-glycosylated and are derived from the same precursor as the smaller form. The C-terminal segment of the precursor remains anchored in the membrane and has covalently attached palmitate. The newly synthesized TGF-α precursor is thus a transmembrane protein that subsequently undergoes external proteolytic cleavages, releasing several TGF-α species.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>3467848</pmid><doi>10.1016/0092-8674(87)90194-2</doi><tpages>12</tpages></addata></record> |
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| identifier | ISSN: 0092-8674 |
| ispartof | Cell, 1987-02, Vol.48 (3), p.429-440 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77369837 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Antibodies Cell Line Cell Membrane - metabolism Cricetinae Glycosylation Membrane Proteins - metabolism Palmitates - metabolism Peptides - immunology Peptides - metabolism Protein Precursors - immunology Protein Precursors - metabolism Protein Processing, Post-Translational Transforming Growth Factors |
| title | Different transforming growth factor-α species are derived from a glycosylated and palmitoylated transmembrane precursor |
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