Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells
Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells. Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kD...
Gespeichert in:
| Veröffentlicht in: | Biochemistry (Easton) 1987-06, Vol.26 (12), p.3297-3303 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3303 |
|---|---|
| container_issue | 12 |
| container_start_page | 3297 |
| container_title | Biochemistry (Easton) |
| container_volume | 26 |
| creator | Collard, Michael W Griswold, Michael D |
| description | Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells. Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kDa subunits. A plasmid cDNA library was constructed from immunopurified mRNA, and a recombinant clone containing the entire protein coding sequence of SGP-2 was isolated. The 1857-nucleotide cDNA consists of a 297-nucleotide 5' noncoding segment, a 1341-nucleotide coding segment, and a 219-nucleotide 3' noncoding sequence. The 5' noncoding region contains five ATG codons followed by four short open reading frames. The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites. Proteolytic processing sites for the preproprotein were determined by amino-terminal sequencing of the isolated SGP-2 subunits. Northern blots show a wide tissue distribution for the 2.0-kb SGP-2 message, and computer sequence analysis indicates a significant relationship between SGP-2 and human apolipoprotein A-I. |
| doi_str_mv | 10.1021/bi00386a008 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_81000374</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>81000374</sourcerecordid><originalsourceid>FETCH-LOGICAL-a449t-3c5bf79690ea098f2dc5f33241f370e5957f99b4b1b62721a082fcf64099999a3</originalsourceid><addsrcrecordid>eNptkM2LFDEQxYMo67h68izkIHqQ1spXp3NcB1fFFYUdL3oI6UyyZs101lQ3OP-93cwweLAuRdX7Ubx6hDxl8JoBZ2_6BCC61gF098iKKQ6NNEbdJysAaBtuWnhIHiHezqMELc_ImWgVE51ckR9vU8H9MP4MmJC6YUt3JQc_ZVepz2VIww0tkeKUoxvDlt7kvS93tYwhDZRTDL6GZd_vaXUjvQ51LDlRH3LGx-RBdBnDk2M_J98u323WH5qrL-8_ri-uGielGRvhVR-1aQ0EB6aLfOtVFIJLFoWGoIzS0Zhe9qxvuebMQcejj60Es5QT5-TF4e7s6_cUcLS7hIsDN4Qyoe3Y_LjQcgZfHUBfC2IN0d7VtHN1bxnYJUr7T5Qz_ex4dup3YXtij9nN-vOj7tC7HKsbfMITplWnDV-w5oAlHMOfk-zqL9tqoZXdfL22n77L9eYzXFoz8y8PvPNob8tUhzm7_xr8C3gElmw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>81000374</pqid></control><display><type>article</type><title>Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells</title><source>ACS Publications</source><source>MEDLINE</source><creator>Collard, Michael W ; Griswold, Michael D</creator><creatorcontrib>Collard, Michael W ; Griswold, Michael D</creatorcontrib><description>Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells. Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kDa subunits. A plasmid cDNA library was constructed from immunopurified mRNA, and a recombinant clone containing the entire protein coding sequence of SGP-2 was isolated. The 1857-nucleotide cDNA consists of a 297-nucleotide 5' noncoding segment, a 1341-nucleotide coding segment, and a 219-nucleotide 3' noncoding sequence. The 5' noncoding region contains five ATG codons followed by four short open reading frames. The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites. Proteolytic processing sites for the preproprotein were determined by amino-terminal sequencing of the isolated SGP-2 subunits. Northern blots show a wide tissue distribution for the 2.0-kb SGP-2 message, and computer sequence analysis indicates a significant relationship between SGP-2 and human apolipoprotein A-I.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00386a008</identifier><identifier>PMID: 3651384</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Cells, Cultured ; Cloning, Molecular ; Clusterin ; DNA - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - biosynthesis ; Glycoproteins - genetics ; Glycoproteins - metabolism ; Male ; Molecular and cellular biology ; Molecular Chaperones ; Molecular genetics ; Plasmids ; Polyribosomes ; Rats ; RNA, Messenger - genetics ; RNA, Messenger - isolation & purification ; Sertoli Cells - metabolism ; Transcription, Genetic ; Translation. Translation factors. Protein processing</subject><ispartof>Biochemistry (Easton), 1987-06, Vol.26 (12), p.3297-3303</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a449t-3c5bf79690ea098f2dc5f33241f370e5957f99b4b1b62721a082fcf64099999a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00386a008$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00386a008$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7587924$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3651384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Collard, Michael W</creatorcontrib><creatorcontrib>Griswold, Michael D</creatorcontrib><title>Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells. Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kDa subunits. A plasmid cDNA library was constructed from immunopurified mRNA, and a recombinant clone containing the entire protein coding sequence of SGP-2 was isolated. The 1857-nucleotide cDNA consists of a 297-nucleotide 5' noncoding segment, a 1341-nucleotide coding segment, and a 219-nucleotide 3' noncoding sequence. The 5' noncoding region contains five ATG codons followed by four short open reading frames. The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites. Proteolytic processing sites for the preproprotein were determined by amino-terminal sequencing of the isolated SGP-2 subunits. Northern blots show a wide tissue distribution for the 2.0-kb SGP-2 message, and computer sequence analysis indicates a significant relationship between SGP-2 and human apolipoprotein A-I.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Cloning, Molecular</subject><subject>Clusterin</subject><subject>DNA - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - biosynthesis</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>Male</subject><subject>Molecular and cellular biology</subject><subject>Molecular Chaperones</subject><subject>Molecular genetics</subject><subject>Plasmids</subject><subject>Polyribosomes</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - isolation & purification</subject><subject>Sertoli Cells - metabolism</subject><subject>Transcription, Genetic</subject><subject>Translation. Translation factors. Protein processing</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM2LFDEQxYMo67h68izkIHqQ1spXp3NcB1fFFYUdL3oI6UyyZs101lQ3OP-93cwweLAuRdX7Ubx6hDxl8JoBZ2_6BCC61gF098iKKQ6NNEbdJysAaBtuWnhIHiHezqMELc_ImWgVE51ckR9vU8H9MP4MmJC6YUt3JQc_ZVepz2VIww0tkeKUoxvDlt7kvS93tYwhDZRTDL6GZd_vaXUjvQ51LDlRH3LGx-RBdBnDk2M_J98u323WH5qrL-8_ri-uGielGRvhVR-1aQ0EB6aLfOtVFIJLFoWGoIzS0Zhe9qxvuebMQcejj60Es5QT5-TF4e7s6_cUcLS7hIsDN4Qyoe3Y_LjQcgZfHUBfC2IN0d7VtHN1bxnYJUr7T5Qz_ex4dup3YXtij9nN-vOj7tC7HKsbfMITplWnDV-w5oAlHMOfk-zqL9tqoZXdfL22n77L9eYzXFoz8y8PvPNob8tUhzm7_xr8C3gElmw</recordid><startdate>19870616</startdate><enddate>19870616</enddate><creator>Collard, Michael W</creator><creator>Griswold, Michael D</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>19870616</creationdate><title>Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells</title><author>Collard, Michael W ; Griswold, Michael D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a449t-3c5bf79690ea098f2dc5f33241f370e5957f99b4b1b62721a082fcf64099999a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Cloning, Molecular</topic><topic>Clusterin</topic><topic>DNA - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - biosynthesis</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - metabolism</topic><topic>Male</topic><topic>Molecular and cellular biology</topic><topic>Molecular Chaperones</topic><topic>Molecular genetics</topic><topic>Plasmids</topic><topic>Polyribosomes</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - isolation & purification</topic><topic>Sertoli Cells - metabolism</topic><topic>Transcription, Genetic</topic><topic>Translation. Translation factors. Protein processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Collard, Michael W</creatorcontrib><creatorcontrib>Griswold, Michael D</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Collard, Michael W</au><au>Griswold, Michael D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1987-06-16</date><risdate>1987</risdate><volume>26</volume><issue>12</issue><spage>3297</spage><epage>3303</epage><pages>3297-3303</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Sulfated glycoprotein 2 (SGP-2) is the major protein secreted by rat Sertoli cells. Pulse-chase labeling shows that SGP-2 is synthesized as a cotranslationally glycosylated 64-kDa precursor that is modified to a negatively charged 73-kDa form before intracellular cleavage to the mature 47- and 34-kDa subunits. A plasmid cDNA library was constructed from immunopurified mRNA, and a recombinant clone containing the entire protein coding sequence of SGP-2 was isolated. The 1857-nucleotide cDNA consists of a 297-nucleotide 5' noncoding segment, a 1341-nucleotide coding segment, and a 219-nucleotide 3' noncoding sequence. The 5' noncoding region contains five ATG codons followed by four short open reading frames. The derived SGP-2 sequence has a molecular weight of 51,379 and contains six potential N-glycosylation sites. Proteolytic processing sites for the preproprotein were determined by amino-terminal sequencing of the isolated SGP-2 subunits. Northern blots show a wide tissue distribution for the 2.0-kb SGP-2 message, and computer sequence analysis indicates a significant relationship between SGP-2 and human apolipoprotein A-I.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>3651384</pmid><doi>10.1021/bi00386a008</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1987-06, Vol.26 (12), p.3297-3303 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81000374 |
| source | ACS Publications; MEDLINE |
| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Cells, Cultured Cloning, Molecular Clusterin DNA - metabolism Fundamental and applied biological sciences. Psychology Glycoproteins - biosynthesis Glycoproteins - genetics Glycoproteins - metabolism Male Molecular and cellular biology Molecular Chaperones Molecular genetics Plasmids Polyribosomes Rats RNA, Messenger - genetics RNA, Messenger - isolation & purification Sertoli Cells - metabolism Transcription, Genetic Translation. Translation factors. Protein processing |
| title | Biosynthesis and molecular cloning of sulfated glycoprotein 2 secreted by rat Sertoli cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T05%3A13%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biosynthesis%20and%20molecular%20cloning%20of%20sulfated%20glycoprotein%202%20secreted%20by%20rat%20Sertoli%20cells&rft.jtitle=Biochemistry%20(Easton)&rft.au=Collard,%20Michael%20W&rft.date=1987-06-16&rft.volume=26&rft.issue=12&rft.spage=3297&rft.epage=3303&rft.pages=3297-3303&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00386a008&rft_dat=%3Cproquest_cross%3E81000374%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=81000374&rft_id=info:pmid/3651384&rfr_iscdi=true |