Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fc gamma-IIA receptor
Activation of human platelets by cross-linking of the platelet low-affinity IgG receptor, the Fc gamma receptor IIA (Fc gamma-RIIA), or by collagen is associated with rapid phosphorylation on tyrosine of the non-receptor tyrosine kinase syk. Phosphorylation is still observed, albeit sometimes reduce...
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| Veröffentlicht in: | Biochemical journal 1995-10, Vol.311 ( Pt 2) (2), p.471-478 |
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| creator | Yanaga, F Poole, A Asselin, J Blake, R Schieven, G L Clark, E A Law, C L Watson, S P |
| description | Activation of human platelets by cross-linking of the platelet low-affinity IgG receptor, the Fc gamma receptor IIA (Fc gamma-RIIA), or by collagen is associated with rapid phosphorylation on tyrosine of the non-receptor tyrosine kinase syk. Phosphorylation is still observed, albeit sometimes reduced, in the presence of a combination of a protein kinase C inhibitor, Ro 31-8220, and the intracellular calcium chelator, BAPTA-AM, demonstrating independence from phosphoinositide-specific phospholipase C (PLC) activity. In contrast, the combination of Ro 31-8220 and BAPTA-AM completely inhibits phosphorylation of syk in thrombin-stimulated platelets. Phosphorylation of syk increases its autophosphorylation activity measured in a kinase assay performed on syk immunoprecipitates. Fc gamma-RIIA also undergoes phosphorylation in syk immunoprecipitates from platelets activated by cross-linking of Fc gamma-RIIA but not by collagen, suggesting that it associates with the kinase. Consistent with this, tyrosine-phosphorylated Fc gamma-RIIA is precipitated by a glutathione S-transferase (GST) fusion protein containing the tandem src homology (SH2) domains of syk from Fc gamma-RIIA- but not collagen-activated cells. Two uncharacterized tyrosine-phosphorylated proteins of 40 and 65 kDa are uniquely precipitated by a GST fusion protein containing the tandem syk-SH2 domains in collagen-stimulated platelets. A peptide based on the antigen recognition activation motif (ARAM) of Fc gamma-RIIA, and phosphorylated on the two tyrosine residues found within this region, selectively binds syk from lysates of resting platelets; this interaction is not seen with a non-phosphorylated peptide. Kinase assays on Fc gamma-RIIA immunoprecipitates reveal the constitutive association of an unidentified kinase activity in resting cells which phosphorylates a 67 kDa protein. Syk is not detected in Fc gamma-RIIA immunoprecipitates from resting cells but associates with the receptor following activation and, together with Fc gamma-RIIA, is phosphorylated in the kinase assay in vitro. These results demonstrate that syk is activated by Fc gamma-RIIA cross-linking and collagen, independent of PLC, suggesting that it may have an important role in the early events associated with platelet activation. The association of syk with Fc gamma-RIIA appears to be mediated through the tandem SH2 domains in syk and the ARAM motif of Fc gamma-RIIA. A similar interaction may underlie the response to collagen, sug |
| doi_str_mv | 10.1042/bj3110471 |
| format | Article |
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Phosphorylation is still observed, albeit sometimes reduced, in the presence of a combination of a protein kinase C inhibitor, Ro 31-8220, and the intracellular calcium chelator, BAPTA-AM, demonstrating independence from phosphoinositide-specific phospholipase C (PLC) activity. In contrast, the combination of Ro 31-8220 and BAPTA-AM completely inhibits phosphorylation of syk in thrombin-stimulated platelets. Phosphorylation of syk increases its autophosphorylation activity measured in a kinase assay performed on syk immunoprecipitates. Fc gamma-RIIA also undergoes phosphorylation in syk immunoprecipitates from platelets activated by cross-linking of Fc gamma-RIIA but not by collagen, suggesting that it associates with the kinase. Consistent with this, tyrosine-phosphorylated Fc gamma-RIIA is precipitated by a glutathione S-transferase (GST) fusion protein containing the tandem src homology (SH2) domains of syk from Fc gamma-RIIA- but not collagen-activated cells. Two uncharacterized tyrosine-phosphorylated proteins of 40 and 65 kDa are uniquely precipitated by a GST fusion protein containing the tandem syk-SH2 domains in collagen-stimulated platelets. A peptide based on the antigen recognition activation motif (ARAM) of Fc gamma-RIIA, and phosphorylated on the two tyrosine residues found within this region, selectively binds syk from lysates of resting platelets; this interaction is not seen with a non-phosphorylated peptide. Kinase assays on Fc gamma-RIIA immunoprecipitates reveal the constitutive association of an unidentified kinase activity in resting cells which phosphorylates a 67 kDa protein. Syk is not detected in Fc gamma-RIIA immunoprecipitates from resting cells but associates with the receptor following activation and, together with Fc gamma-RIIA, is phosphorylated in the kinase assay in vitro. These results demonstrate that syk is activated by Fc gamma-RIIA cross-linking and collagen, independent of PLC, suggesting that it may have an important role in the early events associated with platelet activation. The association of syk with Fc gamma-RIIA appears to be mediated through the tandem SH2 domains in syk and the ARAM motif of Fc gamma-RIIA. A similar interaction may underlie the response to collagen, suggesting that its signalling receptor contains an ARAM motif.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj3110471</identifier><identifier>PMID: 7487883</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Blood Platelets - metabolism ; Chelating Agents - pharmacology ; Collagen - pharmacology ; DNA Primers - chemistry ; Egtazic Acid - analogs & derivatives ; Egtazic Acid - pharmacology ; Enzyme Inhibitors - pharmacology ; Enzyme Precursors - chemistry ; Enzyme Precursors - metabolism ; Humans ; Indoles - pharmacology ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; Molecular Weight ; Peptide Fragments - chemistry ; Phosphorylation ; Platelet Activation - drug effects ; Protein Kinase C - antagonists & inhibitors ; Protein-Tyrosine Kinases - chemistry ; Protein-Tyrosine Kinases - metabolism ; Rabbits ; Receptors, IgG - chemistry ; Receptors, IgG - metabolism ; Syk Kinase ; Type C Phospholipases - metabolism ; Tyrosine - metabolism</subject><ispartof>Biochemical journal, 1995-10, Vol.311 ( Pt 2) (2), p.471-478</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-977291acc8822c0eba8d506968f0a3dd85c162ab1439addb219c80f593dce0c83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1136023/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1136023/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7487883$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yanaga, F</creatorcontrib><creatorcontrib>Poole, A</creatorcontrib><creatorcontrib>Asselin, J</creatorcontrib><creatorcontrib>Blake, R</creatorcontrib><creatorcontrib>Schieven, G L</creatorcontrib><creatorcontrib>Clark, E A</creatorcontrib><creatorcontrib>Law, C L</creatorcontrib><creatorcontrib>Watson, S P</creatorcontrib><title>Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fc gamma-IIA receptor</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Activation of human platelets by cross-linking of the platelet low-affinity IgG receptor, the Fc gamma receptor IIA (Fc gamma-RIIA), or by collagen is associated with rapid phosphorylation on tyrosine of the non-receptor tyrosine kinase syk. Phosphorylation is still observed, albeit sometimes reduced, in the presence of a combination of a protein kinase C inhibitor, Ro 31-8220, and the intracellular calcium chelator, BAPTA-AM, demonstrating independence from phosphoinositide-specific phospholipase C (PLC) activity. In contrast, the combination of Ro 31-8220 and BAPTA-AM completely inhibits phosphorylation of syk in thrombin-stimulated platelets. Phosphorylation of syk increases its autophosphorylation activity measured in a kinase assay performed on syk immunoprecipitates. Fc gamma-RIIA also undergoes phosphorylation in syk immunoprecipitates from platelets activated by cross-linking of Fc gamma-RIIA but not by collagen, suggesting that it associates with the kinase. Consistent with this, tyrosine-phosphorylated Fc gamma-RIIA is precipitated by a glutathione S-transferase (GST) fusion protein containing the tandem src homology (SH2) domains of syk from Fc gamma-RIIA- but not collagen-activated cells. Two uncharacterized tyrosine-phosphorylated proteins of 40 and 65 kDa are uniquely precipitated by a GST fusion protein containing the tandem syk-SH2 domains in collagen-stimulated platelets. A peptide based on the antigen recognition activation motif (ARAM) of Fc gamma-RIIA, and phosphorylated on the two tyrosine residues found within this region, selectively binds syk from lysates of resting platelets; this interaction is not seen with a non-phosphorylated peptide. Kinase assays on Fc gamma-RIIA immunoprecipitates reveal the constitutive association of an unidentified kinase activity in resting cells which phosphorylates a 67 kDa protein. Syk is not detected in Fc gamma-RIIA immunoprecipitates from resting cells but associates with the receptor following activation and, together with Fc gamma-RIIA, is phosphorylated in the kinase assay in vitro. These results demonstrate that syk is activated by Fc gamma-RIIA cross-linking and collagen, independent of PLC, suggesting that it may have an important role in the early events associated with platelet activation. The association of syk with Fc gamma-RIIA appears to be mediated through the tandem SH2 domains in syk and the ARAM motif of Fc gamma-RIIA. A similar interaction may underlie the response to collagen, suggesting that its signalling receptor contains an ARAM motif.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blood Platelets - metabolism</subject><subject>Chelating Agents - pharmacology</subject><subject>Collagen - pharmacology</subject><subject>DNA Primers - chemistry</subject><subject>Egtazic Acid - analogs & derivatives</subject><subject>Egtazic Acid - pharmacology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Precursors - chemistry</subject><subject>Enzyme Precursors - metabolism</subject><subject>Humans</subject><subject>Indoles - pharmacology</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - chemistry</subject><subject>Phosphorylation</subject><subject>Platelet Activation - drug effects</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein-Tyrosine Kinases - chemistry</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Rabbits</subject><subject>Receptors, IgG - chemistry</subject><subject>Receptors, IgG - metabolism</subject><subject>Syk Kinase</subject><subject>Type C Phospholipases - metabolism</subject><subject>Tyrosine - metabolism</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUctOwzAQtBColMKBD0DylUPAjzRxLkhVRaESEgfgHDm2k7hNnMh2i_IN_DTuQxUcVrvanZnV7gBwi9EDRjF5LFYUhyLFZ2CM4xRFLCXsHIwRSeIoQQRfgivnVgjhGMVoBEZpzFLG6Bj8fAxrqI1Xlgvv4Lf2NfSD7Zw2KurrzoWwQ8O9krC3nVfauICH9ablBva7QaMCMbD1do8qBii6puGVMpAbCUUQc1GjzVqbCnYl9LWCCwEr3rY8Wi5n0Cqhet_Za3BR8sapm2OegK_F8-f8NXp7f1nOZ2-RoDTzUZamJMNcCMYIEUgVnMkpSrKElYhTKdlU4ITwAsc041IWBGeCoXKaUSkUEoxOwNNBt98UrQpN4y1v8t7qltsh77jO_0-MrvOq2-YY0_BMGgTuDwL726wqT1yM8p0h-cmQgL37u-yEPDpAfwHgd4p6</recordid><startdate>19951015</startdate><enddate>19951015</enddate><creator>Yanaga, F</creator><creator>Poole, A</creator><creator>Asselin, J</creator><creator>Blake, R</creator><creator>Schieven, G L</creator><creator>Clark, E A</creator><creator>Law, C L</creator><creator>Watson, S P</creator><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>5PM</scope></search><sort><creationdate>19951015</creationdate><title>Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fc gamma-IIA receptor</title><author>Yanaga, F ; Poole, A ; Asselin, J ; Blake, R ; Schieven, G L ; Clark, E A ; Law, C L ; Watson, S P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-977291acc8822c0eba8d506968f0a3dd85c162ab1439addb219c80f593dce0c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blood Platelets - metabolism</topic><topic>Chelating Agents - pharmacology</topic><topic>Collagen - pharmacology</topic><topic>DNA Primers - chemistry</topic><topic>Egtazic Acid - analogs & derivatives</topic><topic>Egtazic Acid - pharmacology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme Precursors - chemistry</topic><topic>Enzyme Precursors - metabolism</topic><topic>Humans</topic><topic>Indoles - pharmacology</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - chemistry</topic><topic>Phosphorylation</topic><topic>Platelet Activation - drug effects</topic><topic>Protein Kinase C - antagonists & inhibitors</topic><topic>Protein-Tyrosine Kinases - chemistry</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Rabbits</topic><topic>Receptors, IgG - chemistry</topic><topic>Receptors, IgG - metabolism</topic><topic>Syk Kinase</topic><topic>Type C Phospholipases - metabolism</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yanaga, F</creatorcontrib><creatorcontrib>Poole, A</creatorcontrib><creatorcontrib>Asselin, J</creatorcontrib><creatorcontrib>Blake, R</creatorcontrib><creatorcontrib>Schieven, G L</creatorcontrib><creatorcontrib>Clark, E A</creatorcontrib><creatorcontrib>Law, C L</creatorcontrib><creatorcontrib>Watson, S P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yanaga, F</au><au>Poole, A</au><au>Asselin, J</au><au>Blake, R</au><au>Schieven, G L</au><au>Clark, E A</au><au>Law, C L</au><au>Watson, S P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fc gamma-IIA receptor</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1995-10-15</date><risdate>1995</risdate><volume>311 ( Pt 2)</volume><issue>2</issue><spage>471</spage><epage>478</epage><pages>471-478</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Activation of human platelets by cross-linking of the platelet low-affinity IgG receptor, the Fc gamma receptor IIA (Fc gamma-RIIA), or by collagen is associated with rapid phosphorylation on tyrosine of the non-receptor tyrosine kinase syk. Phosphorylation is still observed, albeit sometimes reduced, in the presence of a combination of a protein kinase C inhibitor, Ro 31-8220, and the intracellular calcium chelator, BAPTA-AM, demonstrating independence from phosphoinositide-specific phospholipase C (PLC) activity. In contrast, the combination of Ro 31-8220 and BAPTA-AM completely inhibits phosphorylation of syk in thrombin-stimulated platelets. Phosphorylation of syk increases its autophosphorylation activity measured in a kinase assay performed on syk immunoprecipitates. Fc gamma-RIIA also undergoes phosphorylation in syk immunoprecipitates from platelets activated by cross-linking of Fc gamma-RIIA but not by collagen, suggesting that it associates with the kinase. Consistent with this, tyrosine-phosphorylated Fc gamma-RIIA is precipitated by a glutathione S-transferase (GST) fusion protein containing the tandem src homology (SH2) domains of syk from Fc gamma-RIIA- but not collagen-activated cells. Two uncharacterized tyrosine-phosphorylated proteins of 40 and 65 kDa are uniquely precipitated by a GST fusion protein containing the tandem syk-SH2 domains in collagen-stimulated platelets. A peptide based on the antigen recognition activation motif (ARAM) of Fc gamma-RIIA, and phosphorylated on the two tyrosine residues found within this region, selectively binds syk from lysates of resting platelets; this interaction is not seen with a non-phosphorylated peptide. Kinase assays on Fc gamma-RIIA immunoprecipitates reveal the constitutive association of an unidentified kinase activity in resting cells which phosphorylates a 67 kDa protein. Syk is not detected in Fc gamma-RIIA immunoprecipitates from resting cells but associates with the receptor following activation and, together with Fc gamma-RIIA, is phosphorylated in the kinase assay in vitro. These results demonstrate that syk is activated by Fc gamma-RIIA cross-linking and collagen, independent of PLC, suggesting that it may have an important role in the early events associated with platelet activation. The association of syk with Fc gamma-RIIA appears to be mediated through the tandem SH2 domains in syk and the ARAM motif of Fc gamma-RIIA. A similar interaction may underlie the response to collagen, suggesting that its signalling receptor contains an ARAM motif.</abstract><cop>England</cop><pmid>7487883</pmid><doi>10.1042/bj3110471</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1995-10, Vol.311 ( Pt 2) (2), p.471-478 |
| issn | 0264-6021 1470-8728 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Blood Platelets - metabolism Chelating Agents - pharmacology Collagen - pharmacology DNA Primers - chemistry Egtazic Acid - analogs & derivatives Egtazic Acid - pharmacology Enzyme Inhibitors - pharmacology Enzyme Precursors - chemistry Enzyme Precursors - metabolism Humans Indoles - pharmacology Intracellular Signaling Peptides and Proteins Molecular Sequence Data Molecular Weight Peptide Fragments - chemistry Phosphorylation Platelet Activation - drug effects Protein Kinase C - antagonists & inhibitors Protein-Tyrosine Kinases - chemistry Protein-Tyrosine Kinases - metabolism Rabbits Receptors, IgG - chemistry Receptors, IgG - metabolism Syk Kinase Type C Phospholipases - metabolism Tyrosine - metabolism |
| title | Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fc gamma-IIA receptor |
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