Vascular endothelial growth factor (VEGF) and its receptors in tumor-bearing dogs
The molecular biology of the angiogenic growth factor, vascular endothelial growth factor (VEGF), has been studied in the dog. All major isoforms of VEGF are present in the dog. The amino acid sequences are identical between human and dog in the loop regions that are responsible for receptor binding...
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| Veröffentlicht in: | Biological chemistry 1999-12, Vol.380 (12), p.1449-1454 |
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| creator | Scheidegger, P Weiglhofer, W Suarez, S Kaser-Hotz, B Steiner, R Ballmer-Hofer, K Jaussi, R |
| description | The molecular biology of the angiogenic growth factor, vascular endothelial growth factor (VEGF), has been studied in the dog. All major isoforms of VEGF are present in the dog. The amino acid sequences are identical between human and dog in the loop regions that are responsible for receptor binding. Accordingly, the VEGF receptors of dogs and humans are very similar and permit functional exchange of the growth factor. Here we show that canine VEGF activates human endothelial cells to the same extent as human VEGF. Similarly, the two proteins display identical cell binding properties. The VEGF receptor 1 (Flt-1) shows the same alternative splicing in humans and dogs and is overexpressed in the majority of tumors in both species. VEGF occurs also in canine tumors in similar relative quantities as in human malignancies. Based on the literature and our study we suggest that the molecular biology and the function of the VEGF signaling system are virtually identical in humans and canines and in healthy as well as in disease conditions. |
| doi_str_mv | 10.1515/BC.1999.187 |
| format | Article |
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All major isoforms of VEGF are present in the dog. The amino acid sequences are identical between human and dog in the loop regions that are responsible for receptor binding. Accordingly, the VEGF receptors of dogs and humans are very similar and permit functional exchange of the growth factor. Here we show that canine VEGF activates human endothelial cells to the same extent as human VEGF. Similarly, the two proteins display identical cell binding properties. The VEGF receptor 1 (Flt-1) shows the same alternative splicing in humans and dogs and is overexpressed in the majority of tumors in both species. VEGF occurs also in canine tumors in similar relative quantities as in human malignancies. 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All major isoforms of VEGF are present in the dog. The amino acid sequences are identical between human and dog in the loop regions that are responsible for receptor binding. Accordingly, the VEGF receptors of dogs and humans are very similar and permit functional exchange of the growth factor. Here we show that canine VEGF activates human endothelial cells to the same extent as human VEGF. Similarly, the two proteins display identical cell binding properties. The VEGF receptor 1 (Flt-1) shows the same alternative splicing in humans and dogs and is overexpressed in the majority of tumors in both species. VEGF occurs also in canine tumors in similar relative quantities as in human malignancies. Based on the literature and our study we suggest that the molecular biology and the function of the VEGF signaling system are virtually identical in humans and canines and in healthy as well as in disease conditions.</description><subject>Alternative Splicing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>disease models</subject><subject>DNA, Complementary</subject><subject>Dogs</subject><subject>Endothelial Growth Factors - metabolism</subject><subject>Endothelial Growth Factors - physiology</subject><subject>growth factors</subject><subject>Humans</subject><subject>Lymphokines - metabolism</subject><subject>Lymphokines - physiology</subject><subject>Molecular Sequence Data</subject><subject>Neoplasms, Experimental - blood supply</subject><subject>Neoplasms, Experimental - metabolism</subject><subject>Neovascularization, Pathologic</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Receptor Protein-Tyrosine Kinases - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vascular Endothelial Growth Factor A</subject><subject>Vascular Endothelial Growth Factor Receptor-1</subject><subject>Vascular Endothelial Growth Factors</subject><issn>1431-6730</issn><issn>1437-4315</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpN0EFv0zAUwHELgbYxduK--YRAKOU9O47rI4vWgbRpqii9Wo5jdxlpXOxEwLfHI9PEyU9-P73Dn5C3CAsUKD5d1gtUSi1wKV-QEyy5LEqO4uW_GYtKcjgmr1N6AIAllPyIHCNUVeblCVlvTbJTbyJ1QxvGe9d3pqe7GH6N99QbO4ZI32-vrlcfqBla2o2JRmfdIf8n2g10nPYhFo0zsRt2tA279Ia88qZP7uzpPSWb1dWm_lLc3F1_rT_fFLYUMBYtrxi3xlrWNAyYBQsVazzaNs-tdEvWWCWxKp0XlWpB-SWglIJ79NwJfkrezWcPMfycXBr1vkvW9b0ZXJiSrlTJEATP8OMMbQwpRef1IXZ7E_9oBP0YUF_W-jGgzkWyPn86OzV71_5n52IZFDPo0uh-P-9N_KFzaSn0elPq9fqWC7mt9Sr7i9l7E7TZxS7p798YIAemOEdQ_C_TG4Kx</recordid><startdate>19991201</startdate><enddate>19991201</enddate><creator>Scheidegger, P</creator><creator>Weiglhofer, W</creator><creator>Suarez, S</creator><creator>Kaser-Hotz, B</creator><creator>Steiner, R</creator><creator>Ballmer-Hofer, K</creator><creator>Jaussi, R</creator><general>Walter de Gruyter</general><scope>FBQ</scope><scope>BSCLL</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>19991201</creationdate><title>Vascular endothelial growth factor (VEGF) and its receptors in tumor-bearing dogs</title><author>Scheidegger, P ; Weiglhofer, W ; Suarez, S ; Kaser-Hotz, B ; Steiner, R ; Ballmer-Hofer, K ; Jaussi, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-d3623cacc2bb202c0c062bf1cd2c0d7e82bc97164ef569d09f8017753f1f3e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Alternative Splicing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>disease models</topic><topic>DNA, Complementary</topic><topic>Dogs</topic><topic>Endothelial Growth Factors - metabolism</topic><topic>Endothelial Growth Factors - physiology</topic><topic>growth factors</topic><topic>Humans</topic><topic>Lymphokines - metabolism</topic><topic>Lymphokines - physiology</topic><topic>Molecular Sequence Data</topic><topic>Neoplasms, Experimental - blood supply</topic><topic>Neoplasms, Experimental - metabolism</topic><topic>Neovascularization, Pathologic</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Receptor Protein-Tyrosine Kinases - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vascular Endothelial Growth Factor A</topic><topic>Vascular Endothelial Growth Factor Receptor-1</topic><topic>Vascular Endothelial Growth Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scheidegger, P</creatorcontrib><creatorcontrib>Weiglhofer, W</creatorcontrib><creatorcontrib>Suarez, S</creatorcontrib><creatorcontrib>Kaser-Hotz, B</creatorcontrib><creatorcontrib>Steiner, R</creatorcontrib><creatorcontrib>Ballmer-Hofer, K</creatorcontrib><creatorcontrib>Jaussi, R</creatorcontrib><collection>AGRIS</collection><collection>Istex</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>Biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scheidegger, P</au><au>Weiglhofer, W</au><au>Suarez, S</au><au>Kaser-Hotz, B</au><au>Steiner, R</au><au>Ballmer-Hofer, K</au><au>Jaussi, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vascular endothelial growth factor (VEGF) and its receptors in tumor-bearing dogs</atitle><jtitle>Biological chemistry</jtitle><addtitle>Biological Chemistry</addtitle><date>1999-12-01</date><risdate>1999</risdate><volume>380</volume><issue>12</issue><spage>1449</spage><epage>1454</epage><pages>1449-1454</pages><issn>1431-6730</issn><eissn>1437-4315</eissn><abstract>The molecular biology of the angiogenic growth factor, vascular endothelial growth factor (VEGF), has been studied in the dog. All major isoforms of VEGF are present in the dog. The amino acid sequences are identical between human and dog in the loop regions that are responsible for receptor binding. Accordingly, the VEGF receptors of dogs and humans are very similar and permit functional exchange of the growth factor. Here we show that canine VEGF activates human endothelial cells to the same extent as human VEGF. Similarly, the two proteins display identical cell binding properties. The VEGF receptor 1 (Flt-1) shows the same alternative splicing in humans and dogs and is overexpressed in the majority of tumors in both species. VEGF occurs also in canine tumors in similar relative quantities as in human malignancies. Based on the literature and our study we suggest that the molecular biology and the function of the VEGF signaling system are virtually identical in humans and canines and in healthy as well as in disease conditions.</abstract><cop>Germany</cop><pub>Walter de Gruyter</pub><pmid>10661874</pmid><doi>10.1515/BC.1999.187</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biological chemistry, 1999-12, Vol.380 (12), p.1449-1454 |
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| language | eng |
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| source | MEDLINE; De Gruyter journals |
| subjects | Alternative Splicing Amino Acid Sequence Animals Base Sequence disease models DNA, Complementary Dogs Endothelial Growth Factors - metabolism Endothelial Growth Factors - physiology growth factors Humans Lymphokines - metabolism Lymphokines - physiology Molecular Sequence Data Neoplasms, Experimental - blood supply Neoplasms, Experimental - metabolism Neovascularization, Pathologic Proto-Oncogene Proteins - metabolism Receptor Protein-Tyrosine Kinases - metabolism RNA, Messenger - genetics Sequence Homology, Amino Acid Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factor Receptor-1 Vascular Endothelial Growth Factors |
| title | Vascular endothelial growth factor (VEGF) and its receptors in tumor-bearing dogs |
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