cDNA sequence of the human integrin beta 5 subunit
A novel integrin receptor involved in cell adhesion to the matrix protein vitronectin has recently been described from a human lung epithelial-derived cell line (Cheresh, D. A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69). This receptor has an alpha subunit that appears iden...
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| Veröffentlicht in: | The Journal of biological chemistry 1990-10, Vol.265 (28), p.17126-17131 |
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| container_issue | 28 |
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| container_title | The Journal of biological chemistry |
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| creator | McLean, J W Vestal, D J Cheresh, D A Bodary, S C |
| description | A novel integrin receptor involved in cell adhesion to the matrix protein vitronectin has recently been described from a human lung epithelial-derived cell line (Cheresh, D. A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69). This receptor has an alpha subunit that appears identical to the alpha v of the vitronectin receptor alpha v beta 3 expressed in melanoma and endothelial cells, but is complexed with a distinct beta subunit, beta 5. cDNA clones coding for beta 5 have been isolated and used to determine the mRNA and amino acid sequence of this new subunit. A 3.3-kilobase mRNA was found to code for a mature protein of 775 amino acid residues with a hydrophobic leader sequence of 24 amino acids. A 56% identity was found between the beta 5 and beta 3 protein sequences, making them the most closely related of the integrin beta subunits. Polymerase chain reaction abundance analysis revealed that alpha v and beta 5 mRNAs were found in seven very different cell lines, compared with beta 3 mRNA which was found in only three of the them, indicating that this new integrin receptor may be widely distributed. |
| doi_str_mv | 10.1016/S0021-9258(17)44878-2 |
| format | Article |
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A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69). This receptor has an alpha subunit that appears identical to the alpha v of the vitronectin receptor alpha v beta 3 expressed in melanoma and endothelial cells, but is complexed with a distinct beta subunit, beta 5. cDNA clones coding for beta 5 have been isolated and used to determine the mRNA and amino acid sequence of this new subunit. A 3.3-kilobase mRNA was found to code for a mature protein of 775 amino acid residues with a hydrophobic leader sequence of 24 amino acids. A 56% identity was found between the beta 5 and beta 3 protein sequences, making them the most closely related of the integrin beta subunits. 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A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69). This receptor has an alpha subunit that appears identical to the alpha v of the vitronectin receptor alpha v beta 3 expressed in melanoma and endothelial cells, but is complexed with a distinct beta subunit, beta 5. cDNA clones coding for beta 5 have been isolated and used to determine the mRNA and amino acid sequence of this new subunit. A 3.3-kilobase mRNA was found to code for a mature protein of 775 amino acid residues with a hydrophobic leader sequence of 24 amino acids. A 56% identity was found between the beta 5 and beta 3 protein sequences, making them the most closely related of the integrin beta subunits. Polymerase chain reaction abundance analysis revealed that alpha v and beta 5 mRNAs were found in seven very different cell lines, compared with beta 3 mRNA which was found in only three of the them, indicating that this new integrin receptor may be widely distributed.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>DNA, Neoplasm - genetics</subject><subject>DNA, Neoplasm - isolation & purification</subject><subject>Humans</subject><subject>Integrins - genetics</subject><subject>Integrins - isolation & purification</subject><subject>Macromolecular Substances</subject><subject>Molecular Sequence Data</subject><subject>Neoplasms</subject><subject>Oligonucleotide Probes</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - isolation & purification</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EKuXxCZWyQAgWAY-dpM4KVeUpVbAAJHZWYk8aoyYpdgLi73Gaqlu8mcWcO746hEyAXgGF5PqVUgZhymJxAdPLKBJTEbI9MgYqeMhj-Ngn4x1ySI6c-6T-RSmMyIgxgATiMWHq9nkWOPzqsFYYNEXQlhiUXZXVgalbXFpTBzm2WRAHrsu72rQn5KDIVg5Pt_OYvN_fvc0fw8XLw9N8tggVT0QbogJMIU1oTDFXNI0ipnydQnOmkeupUjqiohCcp2mhilznKsdCCBQxZ1QrfkzOh7tr2_h6rpWVcQpXq6zGpnNSUMqZ4ODBeACVbZyzWMi1NVVmfyVQ2buSG1eyFyFhKjeuJPO5yfaDLq9Q71JbOX5_NuxLsyx_jEWZm0aVWEmWxJL1t4AlHrsZMPQyvg1a6ZTpbWofUa3UjfmnyB_pjYOJ</recordid><startdate>19901005</startdate><enddate>19901005</enddate><creator>McLean, J W</creator><creator>Vestal, D J</creator><creator>Cheresh, D A</creator><creator>Bodary, S C</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>19901005</creationdate><title>cDNA sequence of the human integrin beta 5 subunit</title><author>McLean, J W ; Vestal, D J ; Cheresh, D A ; Bodary, S C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-ec1e9196050ebc09442c021fd32de3d7ccd408f83399fcfbdbcbef88e85320dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>DNA, Neoplasm - genetics</topic><topic>DNA, Neoplasm - isolation & purification</topic><topic>Humans</topic><topic>Integrins - genetics</topic><topic>Integrins - isolation & purification</topic><topic>Macromolecular Substances</topic><topic>Molecular Sequence Data</topic><topic>Neoplasms</topic><topic>Oligonucleotide Probes</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - isolation & purification</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McLean, J W</creatorcontrib><creatorcontrib>Vestal, D J</creatorcontrib><creatorcontrib>Cheresh, D A</creatorcontrib><creatorcontrib>Bodary, S C</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McLean, J W</au><au>Vestal, D J</au><au>Cheresh, D A</au><au>Bodary, S C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cDNA sequence of the human integrin beta 5 subunit</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-10-05</date><risdate>1990</risdate><volume>265</volume><issue>28</issue><spage>17126</spage><epage>17131</epage><pages>17126-17131</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A novel integrin receptor involved in cell adhesion to the matrix protein vitronectin has recently been described from a human lung epithelial-derived cell line (Cheresh, D. A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69). This receptor has an alpha subunit that appears identical to the alpha v of the vitronectin receptor alpha v beta 3 expressed in melanoma and endothelial cells, but is complexed with a distinct beta subunit, beta 5. cDNA clones coding for beta 5 have been isolated and used to determine the mRNA and amino acid sequence of this new subunit. A 3.3-kilobase mRNA was found to code for a mature protein of 775 amino acid residues with a hydrophobic leader sequence of 24 amino acids. A 56% identity was found between the beta 5 and beta 3 protein sequences, making them the most closely related of the integrin beta subunits. 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| ispartof | The Journal of biological chemistry, 1990-10, Vol.265 (28), p.17126-17131 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Base Sequence Blotting, Northern Cell Line Cloning, Molecular DNA, Neoplasm - genetics DNA, Neoplasm - isolation & purification Humans Integrins - genetics Integrins - isolation & purification Macromolecular Substances Molecular Sequence Data Neoplasms Oligonucleotide Probes RNA, Messenger - genetics RNA, Messenger - isolation & purification Sequence Homology, Nucleic Acid |
| title | cDNA sequence of the human integrin beta 5 subunit |
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