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Identification of a peptide antagonist for platelet-derived growth factor
A series of peptides derived from the primary sequence of the B-chain of platelet-derived growth factor (PDGF) was analyzed for their ability to inhibit the binding of 125I-PDGF-AA and 125I-PDGF-BB to PDGF alpha-receptors and PDGF beta-receptors, respectively. A 13-amino acid peptide (ANFLVWEIVRKKP)...
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| Published in: | The Journal of biological chemistry 1992-08, Vol.267 (23), p.16581-16587 |
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| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c506t-92d33ef42b7a3969e2b9ff409b8bb1381a27e2151d5bb58c661cbb0f6b05534b3 |
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| cites | cdi_FETCH-LOGICAL-c506t-92d33ef42b7a3969e2b9ff409b8bb1381a27e2151d5bb58c661cbb0f6b05534b3 |
| container_end_page | 16587 |
| container_issue | 23 |
| container_start_page | 16581 |
| container_title | The Journal of biological chemistry |
| container_volume | 267 |
| creator | Engström, U Engström, A Ernlund, A Westermark, B Heldin, C H |
| description | A series of peptides derived from the primary sequence of the B-chain of platelet-derived growth factor (PDGF) was analyzed
for their ability to inhibit the binding of 125I-PDGF-AA and 125I-PDGF-BB to PDGF alpha-receptors and PDGF beta-receptors,
respectively. A 13-amino acid peptide (ANFLVWEIVRKKP), corresponding to amino acids 116-121 and 157-163 in PDGF B-chain, was
found to compete with binding to both alpha- and beta-receptors. Modification of this peptide on the tryptophan residue increased
its receptor competing activity. The peptide was found to be a receptor antagonist, since it inhibited dimerization and autophosphorylation
of PDGF receptors. When analyzed on intact cells, the peptide was found to have, in addition to the specific inhibitory effect
at the receptor level, a nonspecific inhibitory effect on [3H]thymidine incorporation. Our study has identified two regions
in PDGF that are of importance for receptor interaction. |
| doi_str_mv | 10.1016/s0021-9258(18)42042-x |
| format | article |
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for their ability to inhibit the binding of 125I-PDGF-AA and 125I-PDGF-BB to PDGF alpha-receptors and PDGF beta-receptors,
respectively. A 13-amino acid peptide (ANFLVWEIVRKKP), corresponding to amino acids 116-121 and 157-163 in PDGF B-chain, was
found to compete with binding to both alpha- and beta-receptors. Modification of this peptide on the tryptophan residue increased
its receptor competing activity. The peptide was found to be a receptor antagonist, since it inhibited dimerization and autophosphorylation
of PDGF receptors. When analyzed on intact cells, the peptide was found to have, in addition to the specific inhibitory effect
at the receptor level, a nonspecific inhibitory effect on [3H]thymidine incorporation. Our study has identified two regions
in PDGF that are of importance for receptor interaction.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)42042-x</identifier><identifier>PMID: 1322909</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 ; antagonists ; Biological and medical sciences ; Cell Line ; Chromatography, High Pressure Liquid ; Fundamental and applied biological sciences. Psychology ; Humans ; Kinetics ; man ; Molecular Sequence Data ; peptides ; Peptides - chemical synthesis ; Peptides - pharmacology ; platelet-derived growth factor ; Platelet-Derived Growth Factor - metabolism ; Platelet-Derived Growth Factor - pharmacology ; Protein hormones. Growth factors. Cytokines ; Proteins ; Receptors, Cell Surface - antagonists & inhibitors ; Receptors, Cell Surface - metabolism ; Receptors, Platelet-Derived Growth Factor ; Recombinant Proteins - metabolism ; Skin</subject><ispartof>The Journal of biological chemistry, 1992-08, Vol.267 (23), p.16581-16587</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-92d33ef42b7a3969e2b9ff409b8bb1381a27e2151d5bb58c661cbb0f6b05534b3</citedby><cites>FETCH-LOGICAL-c506t-92d33ef42b7a3969e2b9ff409b8bb1381a27e2151d5bb58c661cbb0f6b05534b3</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=5566428$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1322909$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Engström, U</creatorcontrib><creatorcontrib>Engström, A</creatorcontrib><creatorcontrib>Ernlund, A</creatorcontrib><creatorcontrib>Westermark, B</creatorcontrib><creatorcontrib>Heldin, C H</creatorcontrib><title>Identification of a peptide antagonist for platelet-derived growth factor</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A series of peptides derived from the primary sequence of the B-chain of platelet-derived growth factor (PDGF) was analyzed
for their ability to inhibit the binding of 125I-PDGF-AA and 125I-PDGF-BB to PDGF alpha-receptors and PDGF beta-receptors,
respectively. A 13-amino acid peptide (ANFLVWEIVRKKP), corresponding to amino acids 116-121 and 157-163 in PDGF B-chain, was
found to compete with binding to both alpha- and beta-receptors. Modification of this peptide on the tryptophan residue increased
its receptor competing activity. The peptide was found to be a receptor antagonist, since it inhibited dimerization and autophosphorylation
of PDGF receptors. When analyzed on intact cells, the peptide was found to have, in addition to the specific inhibitory effect
at the receptor level, a nonspecific inhibitory effect on [3H]thymidine incorporation. Our study has identified two regions
in PDGF that are of importance for receptor interaction.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>antagonists</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>man</subject><subject>Molecular Sequence Data</subject><subject>peptides</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - pharmacology</subject><subject>platelet-derived growth factor</subject><subject>Platelet-Derived Growth Factor - metabolism</subject><subject>Platelet-Derived Growth Factor - pharmacology</subject><subject>Protein hormones. Growth factors. Cytokines</subject><subject>Proteins</subject><subject>Receptors, Cell Surface - antagonists & inhibitors</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Platelet-Derived Growth Factor</subject><subject>Recombinant Proteins - metabolism</subject><subject>Skin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNqFkE1vEzEQhi0EKmnhJ1TaA0L0sNTjr3iPVQUlUiUOUKk3y_aOE6PNems7FP49myZqj8xlDvPMzKuHkHOgn4GCuiyUMmg7JvUn0BeCUcHaP6_IAqjmLZdw_5osnpG35LSUX3Qu0cEJOQHOWEe7BVmtehxrDNHbGtPYpNDYZsKpxh4bO1a7TmMstQkpN9NgKw5Y2x5z_I19s87psW6aYH1N-R15E-xQ8P2xn5G7r19-Xn9rb7_frK6vblsvqapzmp5zDIK5peWd6pC5LgRBO6edA67BsiUykNBL56T2SoF3jgblqJRcOH5GPh7uTjk97LBUs43F4zDYEdOumCUHJgSX_wVBCao424PyAPqcSskYzJTj1ua_BqjZuzY_9iLNXqQBbZ5cm_t57_z4YOe22L9sHeTO8w_HuS3eDiHb0cfyjEmplGD6BdvE9eYxZjQuJr_BrWFqaRifg0oN_B_j9ZKr</recordid><startdate>19920815</startdate><enddate>19920815</enddate><creator>Engström, U</creator><creator>Engström, A</creator><creator>Ernlund, A</creator><creator>Westermark, B</creator><creator>Heldin, C H</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920815</creationdate><title>Identification of a peptide antagonist for platelet-derived growth factor</title><author>Engström, U ; Engström, A ; Ernlund, A ; Westermark, B ; Heldin, C H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-92d33ef42b7a3969e2b9ff409b8bb1381a27e2151d5bb58c661cbb0f6b05534b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>antagonists</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>peptides</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - pharmacology</topic><topic>platelet-derived growth factor</topic><topic>Platelet-Derived Growth Factor - metabolism</topic><topic>Platelet-Derived Growth Factor - pharmacology</topic><topic>Protein hormones. Growth factors. Cytokines</topic><topic>Proteins</topic><topic>Receptors, Cell Surface - antagonists & inhibitors</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Platelet-Derived Growth Factor</topic><topic>Recombinant Proteins - metabolism</topic><topic>Skin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Engström, U</creatorcontrib><creatorcontrib>Engström, A</creatorcontrib><creatorcontrib>Ernlund, A</creatorcontrib><creatorcontrib>Westermark, B</creatorcontrib><creatorcontrib>Heldin, C H</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering 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>Engström, U</au><au>Engström, A</au><au>Ernlund, A</au><au>Westermark, B</au><au>Heldin, C H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a peptide antagonist for platelet-derived growth factor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-08-15</date><risdate>1992</risdate><volume>267</volume><issue>23</issue><spage>16581</spage><epage>16587</epage><pages>16581-16587</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>A series of peptides derived from the primary sequence of the B-chain of platelet-derived growth factor (PDGF) was analyzed
for their ability to inhibit the binding of 125I-PDGF-AA and 125I-PDGF-BB to PDGF alpha-receptors and PDGF beta-receptors,
respectively. A 13-amino acid peptide (ANFLVWEIVRKKP), corresponding to amino acids 116-121 and 157-163 in PDGF B-chain, was
found to compete with binding to both alpha- and beta-receptors. Modification of this peptide on the tryptophan residue increased
its receptor competing activity. The peptide was found to be a receptor antagonist, since it inhibited dimerization and autophosphorylation
of PDGF receptors. When analyzed on intact cells, the peptide was found to have, in addition to the specific inhibitory effect
at the receptor level, a nonspecific inhibitory effect on [3H]thymidine incorporation. Our study has identified two regions
in PDGF that are of importance for receptor interaction.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1322909</pmid><doi>10.1016/s0021-9258(18)42042-x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1992-08, Vol.267 (23), p.16581-16587 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73124435 |
| source | Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry antagonists Biological and medical sciences Cell Line Chromatography, High Pressure Liquid Fundamental and applied biological sciences. Psychology Humans Kinetics man Molecular Sequence Data peptides Peptides - chemical synthesis Peptides - pharmacology platelet-derived growth factor Platelet-Derived Growth Factor - metabolism Platelet-Derived Growth Factor - pharmacology Protein hormones. Growth factors. Cytokines Proteins Receptors, Cell Surface - antagonists & inhibitors Receptors, Cell Surface - metabolism Receptors, Platelet-Derived Growth Factor Recombinant Proteins - metabolism Skin |
| title | Identification of a peptide antagonist for platelet-derived growth factor |
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