The complete primary structure for a novel laminin chain, the laminin B1k chain
We have isolated overlapping cDNA clones encoding the entire kalinin B1 chain. The predicted sequences are consistent with the models proposed for the structure of this chain as a truncated homologue of the B1 chain of laminin. The percent sequence homology with other laminin B1 chains is relatively...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1994-04, Vol.269 (15), p.11073-11080 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 11080 |
|---|---|
| container_issue | 15 |
| container_start_page | 11073 |
| container_title | The Journal of biological chemistry |
| container_volume | 269 |
| creator | GERECKE, D. R WAGMAN, D. W CHAMPLIAUD, M.-F BURGESON, R. E |
| description | We have isolated overlapping cDNA clones encoding the entire kalinin B1 chain. The predicted sequences are consistent with
the models proposed for the structure of this chain as a truncated homologue of the B1 chain of laminin. The percent sequence
homology with other laminin B1 chains is relatively low, suggesting that this chain is functionally different. The sequence
of the VI domain of this chain is consistent with the possibility that it serves to bind specifically the kalinin A chain
and subsequently covalently binds to it. In keeping with the accepted nomenclature for the laminin chains we name this novel
polypeptide the laminin B1k chain. |
| doi_str_mv | 10.1016/s0021-9258(19)78093-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76441222</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76441222</sourcerecordid><originalsourceid>FETCH-LOGICAL-c506t-61ee4249db397d4b03f5d3edee2d3daa81da1476ef5eb80034f08227cf071a423</originalsourceid><addsrcrecordid>eNqFkEtP3TAQRi3Uil4ePwHJi6pqpaZ4_EjsJaBSKiGxKEjsLMeZEEMet3ZC1X9PLje9XTKbkWbONyMdQk6AfQMG-WlijENmuNKfwXwpNDMik3tkBUyLTCi4f0dWO-QDOUjpkc0lDeyT_UIBV0qvyM1tg9QP3brFEek6hs7FvzSNcfLjFJHWQ6SO9sMztrR1XehDT33jQv-VjnPy3-gcnrbjI_K-dm3C46UfkrvL77cXV9n1zY-fF2fXmVcsH7McECWXpiqFKSpZMlGrSmCFyCtROaehciCLHGuFpWZMyJppzgtfswKc5OKQfNreXcfh94RptF1IHtvW9ThMyRa5lMD52yDkWiol9QyqLejjkFLE2i42LDC7MW5_bXTajU4Lxr4at3LOnSwPprLDapdaFM_7j8veJe_aOrreh7TDJGhuQPzHmvDQ_AkRbRkG32BneW4sKAvACiFeAHELk90</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16845548</pqid></control><display><type>article</type><title>The complete primary structure for a novel laminin chain, the laminin B1k chain</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>GERECKE, D. R ; WAGMAN, D. W ; CHAMPLIAUD, M.-F ; BURGESON, R. E</creator><creatorcontrib>GERECKE, D. R ; WAGMAN, D. W ; CHAMPLIAUD, M.-F ; BURGESON, R. E</creatorcontrib><description>We have isolated overlapping cDNA clones encoding the entire kalinin B1 chain. The predicted sequences are consistent with
the models proposed for the structure of this chain as a truncated homologue of the B1 chain of laminin. The percent sequence
homology with other laminin B1 chains is relatively low, suggesting that this chain is functionally different. The sequence
of the VI domain of this chain is consistent with the possibility that it serves to bind specifically the kalinin A chain
and subsequently covalently binds to it. In keeping with the accepted nomenclature for the laminin chains we name this novel
polypeptide the laminin B1k chain.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)78093-4</identifier><identifier>PMID: 7512558</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; B1k chain ; Base Sequence ; Biological and medical sciences ; carcinoma ; Carcinoma, Squamous Cell ; cDNA ; Cell Adhesion Molecules - chemistry ; Cell Adhesion Molecules - metabolism ; Cell Line ; Cloning, Molecular ; DNA, Complementary - isolation & purification ; DNA, Complementary - metabolism ; Epitopes - analysis ; Fundamental and applied biological sciences. Psychology ; genes ; Glycoproteins ; Humans ; Kalinin ; laminin ; Laminin - biosynthesis ; Laminin - chemistry ; Laminin - isolation & purification ; Macromolecular Substances ; man ; Molecular Sequence Data ; nucleotide sequence ; Peptide Fragments - biosynthesis ; Peptide Fragments - chemistry ; Peptide Fragments - isolation & purification ; predictions ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Restriction Mapping ; Sequence Homology, Amino Acid ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1994-04, Vol.269 (15), p.11073-11080</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-61ee4249db397d4b03f5d3edee2d3daa81da1476ef5eb80034f08227cf071a423</citedby><cites>FETCH-LOGICAL-c506t-61ee4249db397d4b03f5d3edee2d3daa81da1476ef5eb80034f08227cf071a423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4182913$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7512558$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GERECKE, D. R</creatorcontrib><creatorcontrib>WAGMAN, D. W</creatorcontrib><creatorcontrib>CHAMPLIAUD, M.-F</creatorcontrib><creatorcontrib>BURGESON, R. E</creatorcontrib><title>The complete primary structure for a novel laminin chain, the laminin B1k chain</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have isolated overlapping cDNA clones encoding the entire kalinin B1 chain. The predicted sequences are consistent with
the models proposed for the structure of this chain as a truncated homologue of the B1 chain of laminin. The percent sequence
homology with other laminin B1 chains is relatively low, suggesting that this chain is functionally different. The sequence
of the VI domain of this chain is consistent with the possibility that it serves to bind specifically the kalinin A chain
and subsequently covalently binds to it. In keeping with the accepted nomenclature for the laminin chains we name this novel
polypeptide the laminin B1k chain.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>B1k chain</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>carcinoma</subject><subject>Carcinoma, Squamous Cell</subject><subject>cDNA</subject><subject>Cell Adhesion Molecules - chemistry</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - isolation & purification</subject><subject>DNA, Complementary - metabolism</subject><subject>Epitopes - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Glycoproteins</subject><subject>Humans</subject><subject>Kalinin</subject><subject>laminin</subject><subject>Laminin - biosynthesis</subject><subject>Laminin - chemistry</subject><subject>Laminin - isolation & purification</subject><subject>Macromolecular Substances</subject><subject>man</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Peptide Fragments - biosynthesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - isolation & purification</subject><subject>predictions</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtP3TAQRi3Uil4ePwHJi6pqpaZ4_EjsJaBSKiGxKEjsLMeZEEMet3ZC1X9PLje9XTKbkWbONyMdQk6AfQMG-WlijENmuNKfwXwpNDMik3tkBUyLTCi4f0dWO-QDOUjpkc0lDeyT_UIBV0qvyM1tg9QP3brFEek6hs7FvzSNcfLjFJHWQ6SO9sMztrR1XehDT33jQv-VjnPy3-gcnrbjI_K-dm3C46UfkrvL77cXV9n1zY-fF2fXmVcsH7McECWXpiqFKSpZMlGrSmCFyCtROaehciCLHGuFpWZMyJppzgtfswKc5OKQfNreXcfh94RptF1IHtvW9ThMyRa5lMD52yDkWiol9QyqLejjkFLE2i42LDC7MW5_bXTajU4Lxr4at3LOnSwPprLDapdaFM_7j8veJe_aOrreh7TDJGhuQPzHmvDQ_AkRbRkG32BneW4sKAvACiFeAHELk90</recordid><startdate>19940415</startdate><enddate>19940415</enddate><creator>GERECKE, D. R</creator><creator>WAGMAN, D. W</creator><creator>CHAMPLIAUD, M.-F</creator><creator>BURGESON, R. E</creator><general>American Society for Biochemistry and Molecular Biology</general><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>7T3</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19940415</creationdate><title>The complete primary structure for a novel laminin chain, the laminin B1k chain</title><author>GERECKE, D. R ; WAGMAN, D. W ; CHAMPLIAUD, M.-F ; BURGESON, R. E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-61ee4249db397d4b03f5d3edee2d3daa81da1476ef5eb80034f08227cf071a423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>B1k chain</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>carcinoma</topic><topic>Carcinoma, Squamous Cell</topic><topic>cDNA</topic><topic>Cell Adhesion Molecules - chemistry</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - isolation & purification</topic><topic>DNA, Complementary - metabolism</topic><topic>Epitopes - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>Kalinin</topic><topic>laminin</topic><topic>Laminin - biosynthesis</topic><topic>Laminin - chemistry</topic><topic>Laminin - isolation & purification</topic><topic>Macromolecular Substances</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Peptide Fragments - biosynthesis</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - isolation & purification</topic><topic>predictions</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Amino Acid</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GERECKE, D. R</creatorcontrib><creatorcontrib>WAGMAN, D. W</creatorcontrib><creatorcontrib>CHAMPLIAUD, M.-F</creatorcontrib><creatorcontrib>BURGESON, R. E</creatorcontrib><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>Human Genome Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GERECKE, D. R</au><au>WAGMAN, D. W</au><au>CHAMPLIAUD, M.-F</au><au>BURGESON, R. E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The complete primary structure for a novel laminin chain, the laminin B1k chain</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-04-15</date><risdate>1994</risdate><volume>269</volume><issue>15</issue><spage>11073</spage><epage>11080</epage><pages>11073-11080</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have isolated overlapping cDNA clones encoding the entire kalinin B1 chain. The predicted sequences are consistent with
the models proposed for the structure of this chain as a truncated homologue of the B1 chain of laminin. The percent sequence
homology with other laminin B1 chains is relatively low, suggesting that this chain is functionally different. The sequence
of the VI domain of this chain is consistent with the possibility that it serves to bind specifically the kalinin A chain
and subsequently covalently binds to it. In keeping with the accepted nomenclature for the laminin chains we name this novel
polypeptide the laminin B1k chain.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7512558</pmid><doi>10.1016/s0021-9258(19)78093-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1994-04, Vol.269 (15), p.11073-11080 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76441222 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry B1k chain Base Sequence Biological and medical sciences carcinoma Carcinoma, Squamous Cell cDNA Cell Adhesion Molecules - chemistry Cell Adhesion Molecules - metabolism Cell Line Cloning, Molecular DNA, Complementary - isolation & purification DNA, Complementary - metabolism Epitopes - analysis Fundamental and applied biological sciences. Psychology genes Glycoproteins Humans Kalinin laminin Laminin - biosynthesis Laminin - chemistry Laminin - isolation & purification Macromolecular Substances man Molecular Sequence Data nucleotide sequence Peptide Fragments - biosynthesis Peptide Fragments - chemistry Peptide Fragments - isolation & purification predictions Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Restriction Mapping Sequence Homology, Amino Acid Tumor Cells, Cultured |
| title | The complete primary structure for a novel laminin chain, the laminin B1k chain |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-19T15%3A32%3A07IST&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=The%20complete%20primary%20structure%20for%20a%20novel%20laminin%20chain,%20the%20laminin%20B1k%20chain&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=GERECKE,%20D.%20R&rft.date=1994-04-15&rft.volume=269&rft.issue=15&rft.spage=11073&rft.epage=11080&rft.pages=11073-11080&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/s0021-9258(19)78093-4&rft_dat=%3Cproquest_cross%3E76441222%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=16845548&rft_id=info:pmid/7512558&rfr_iscdi=true |