Echistatin inhibits pp72syk and pp125FAK phosphorylation in fibrinogen-adherent platelets
The adhesion of ADP-stimulated platelets to immobilized fibrinogen induces the tyrosine phosphorylation of multiple proteins which include pp72syk and pp125FAK. The phosphorylation of these two proteins increases as function of time of platelet adhesion to fibrinogen; however, pp72syk results strong...
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Veröffentlicht in: | Biochimie 1997-12, Vol.79 (12), p.769-773 |
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creator | Staiano, N Della Morte, R Di Domenico, C Tafuri, S Squillacioti, C Belisario, M A Di Natale, P |
description | The adhesion of ADP-stimulated platelets to immobilized fibrinogen induces the tyrosine phosphorylation of multiple proteins which include pp72syk and pp125FAK. The phosphorylation of these two proteins increases as function of time of platelet adhesion to fibrinogen; however, pp72syk results strongly phosphorylated already after 15 min, whereas pp125FAK reaches high levels of phosphorylation after 1 h of platelet adhesion. Phosphorylation of both proteins is only slightly detectable when platelets are held in suspension or when platelets are allowed to adhere to bovine serum albumin, a non-specific substrate. Echistatin, an Arg-Gly-Asp (RGD)-containing snake-venom protein, affects protein tyrosine phosphorylation promoted by platelet adhesion to fibrinogen, by causing an approximately 44% and 39% decrease of pp72syk and pp125FAK phosphorylation, respectively. The interaction of echistatin with fibrinogen receptor glycoprotein IIb-IIIa on platelet surface might be responsible for the block of integrin-mediated signaling cascade, including pp72syk and pp125FAK inactivation. |
doi_str_mv | 10.1016/s0300-9084(97)86935-0 |
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The phosphorylation of these two proteins increases as function of time of platelet adhesion to fibrinogen; however, pp72syk results strongly phosphorylated already after 15 min, whereas pp125FAK reaches high levels of phosphorylation after 1 h of platelet adhesion. Phosphorylation of both proteins is only slightly detectable when platelets are held in suspension or when platelets are allowed to adhere to bovine serum albumin, a non-specific substrate. Echistatin, an Arg-Gly-Asp (RGD)-containing snake-venom protein, affects protein tyrosine phosphorylation promoted by platelet adhesion to fibrinogen, by causing an approximately 44% and 39% decrease of pp72syk and pp125FAK phosphorylation, respectively. The interaction of echistatin with fibrinogen receptor glycoprotein IIb-IIIa on platelet surface might be responsible for the block of integrin-mediated signaling cascade, including pp72syk and pp125FAK inactivation.</description><identifier>ISSN: 0300-9084</identifier><identifier>DOI: 10.1016/s0300-9084(97)86935-0</identifier><identifier>PMID: 9523019</identifier><language>eng</language><publisher>France</publisher><subject>Blood Platelets - enzymology ; Blotting, Western ; Cell Adhesion Molecules - blood ; Cell Adhesion Molecules - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Enzyme Precursors - antagonists & inhibitors ; Enzyme Precursors - blood ; Fibrinogen - metabolism ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Intracellular Signaling Peptides and Proteins ; Peptides - pharmacology ; Phosphorylation - drug effects ; Platelet Adhesiveness - drug effects ; Platelet Aggregation Inhibitors - pharmacology ; Precipitin Tests ; Protein-Tyrosine Kinases - antagonists & inhibitors ; Protein-Tyrosine Kinases - blood ; Protein-Tyrosine Kinases - pharmacology ; Syk Kinase</subject><ispartof>Biochimie, 1997-12, Vol.79 (12), p.769-773</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2469-cff34aa575961a1e9d136ba5ec18af9e78ad1586a68b2c0882ad7f3f9b0247693</citedby><cites>FETCH-LOGICAL-c2469-cff34aa575961a1e9d136ba5ec18af9e78ad1586a68b2c0882ad7f3f9b0247693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9523019$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Staiano, N</creatorcontrib><creatorcontrib>Della Morte, R</creatorcontrib><creatorcontrib>Di Domenico, C</creatorcontrib><creatorcontrib>Tafuri, S</creatorcontrib><creatorcontrib>Squillacioti, C</creatorcontrib><creatorcontrib>Belisario, M A</creatorcontrib><creatorcontrib>Di Natale, P</creatorcontrib><title>Echistatin inhibits pp72syk and pp125FAK phosphorylation in fibrinogen-adherent platelets</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>The adhesion of ADP-stimulated platelets to immobilized fibrinogen induces the tyrosine phosphorylation of multiple proteins which include pp72syk and pp125FAK. The phosphorylation of these two proteins increases as function of time of platelet adhesion to fibrinogen; however, pp72syk results strongly phosphorylated already after 15 min, whereas pp125FAK reaches high levels of phosphorylation after 1 h of platelet adhesion. Phosphorylation of both proteins is only slightly detectable when platelets are held in suspension or when platelets are allowed to adhere to bovine serum albumin, a non-specific substrate. Echistatin, an Arg-Gly-Asp (RGD)-containing snake-venom protein, affects protein tyrosine phosphorylation promoted by platelet adhesion to fibrinogen, by causing an approximately 44% and 39% decrease of pp72syk and pp125FAK phosphorylation, respectively. The interaction of echistatin with fibrinogen receptor glycoprotein IIb-IIIa on platelet surface might be responsible for the block of integrin-mediated signaling cascade, including pp72syk and pp125FAK inactivation.</description><subject>Blood Platelets - enzymology</subject><subject>Blotting, Western</subject><subject>Cell Adhesion Molecules - blood</subject><subject>Cell Adhesion Molecules - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Precursors - antagonists & inhibitors</subject><subject>Enzyme Precursors - blood</subject><subject>Fibrinogen - metabolism</subject><subject>Focal Adhesion Kinase 1</subject><subject>Focal Adhesion Protein-Tyrosine Kinases</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Peptides - pharmacology</subject><subject>Phosphorylation - drug effects</subject><subject>Platelet Adhesiveness - drug effects</subject><subject>Platelet Aggregation Inhibitors - pharmacology</subject><subject>Precipitin Tests</subject><subject>Protein-Tyrosine Kinases - antagonists & inhibitors</subject><subject>Protein-Tyrosine Kinases - blood</subject><subject>Protein-Tyrosine Kinases - pharmacology</subject><subject>Syk Kinase</subject><issn>0300-9084</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1PwzAMhnMAjTH4CZN6QnAoOEnzdZymDRCTOAAHTlHaJjTQtSXpDvv3tGzawbJlv68tPwjNMdxjwPwhAgVIFcjsVok7yRVlKZyh6al9gS5j_AYABkRN0EQxQgGrKfpcFZWPvel9k_im8rnvY9J1gsT9T2KacqgxYevFS9JVbRwi7OtB3I7qxPk8-Kb9sk1qysoG2_RJN4xtbft4hc6dqaO9PuYZ-liv3pdP6eb18Xm52KQFybhKC-doZgwTTHFssFUlpjw3zBZYGqeskKbETHLDZU4KkJKYUjjqVA4kE8OnM3Rz2NuF9ndnY6-3Pha2rk1j213UQjGJBYdByA7CIrQxBut0F_zWhL3GoEeM-m3kpUdeWgn9j1GPvvnxwC7f2vLkOjKkfy9kcJA</recordid><startdate>199712</startdate><enddate>199712</enddate><creator>Staiano, N</creator><creator>Della Morte, R</creator><creator>Di Domenico, C</creator><creator>Tafuri, S</creator><creator>Squillacioti, C</creator><creator>Belisario, M A</creator><creator>Di Natale, 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>7X8</scope></search><sort><creationdate>199712</creationdate><title>Echistatin inhibits pp72syk and pp125FAK phosphorylation in fibrinogen-adherent platelets</title><author>Staiano, N ; Della Morte, R ; Di Domenico, C ; Tafuri, S ; Squillacioti, C ; Belisario, M A ; Di Natale, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2469-cff34aa575961a1e9d136ba5ec18af9e78ad1586a68b2c0882ad7f3f9b0247693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Blood Platelets - enzymology</topic><topic>Blotting, Western</topic><topic>Cell Adhesion Molecules - blood</topic><topic>Cell Adhesion Molecules - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Precursors - antagonists & inhibitors</topic><topic>Enzyme Precursors - blood</topic><topic>Fibrinogen - metabolism</topic><topic>Focal Adhesion Kinase 1</topic><topic>Focal Adhesion Protein-Tyrosine Kinases</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Peptides - pharmacology</topic><topic>Phosphorylation - drug effects</topic><topic>Platelet Adhesiveness - drug effects</topic><topic>Platelet Aggregation Inhibitors - pharmacology</topic><topic>Precipitin Tests</topic><topic>Protein-Tyrosine Kinases - antagonists & inhibitors</topic><topic>Protein-Tyrosine Kinases - blood</topic><topic>Protein-Tyrosine Kinases - pharmacology</topic><topic>Syk Kinase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Staiano, N</creatorcontrib><creatorcontrib>Della Morte, R</creatorcontrib><creatorcontrib>Di Domenico, C</creatorcontrib><creatorcontrib>Tafuri, S</creatorcontrib><creatorcontrib>Squillacioti, C</creatorcontrib><creatorcontrib>Belisario, M A</creatorcontrib><creatorcontrib>Di Natale, 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>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Staiano, N</au><au>Della Morte, R</au><au>Di Domenico, C</au><au>Tafuri, S</au><au>Squillacioti, C</au><au>Belisario, M A</au><au>Di Natale, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Echistatin inhibits pp72syk and pp125FAK phosphorylation in fibrinogen-adherent platelets</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>1997-12</date><risdate>1997</risdate><volume>79</volume><issue>12</issue><spage>769</spage><epage>773</epage><pages>769-773</pages><issn>0300-9084</issn><abstract>The adhesion of ADP-stimulated platelets to immobilized fibrinogen induces the tyrosine phosphorylation of multiple proteins which include pp72syk and pp125FAK. The phosphorylation of these two proteins increases as function of time of platelet adhesion to fibrinogen; however, pp72syk results strongly phosphorylated already after 15 min, whereas pp125FAK reaches high levels of phosphorylation after 1 h of platelet adhesion. Phosphorylation of both proteins is only slightly detectable when platelets are held in suspension or when platelets are allowed to adhere to bovine serum albumin, a non-specific substrate. Echistatin, an Arg-Gly-Asp (RGD)-containing snake-venom protein, affects protein tyrosine phosphorylation promoted by platelet adhesion to fibrinogen, by causing an approximately 44% and 39% decrease of pp72syk and pp125FAK phosphorylation, respectively. The interaction of echistatin with fibrinogen receptor glycoprotein IIb-IIIa on platelet surface might be responsible for the block of integrin-mediated signaling cascade, including pp72syk and pp125FAK inactivation.</abstract><cop>France</cop><pmid>9523019</pmid><doi>10.1016/s0300-9084(97)86935-0</doi><tpages>5</tpages></addata></record> |
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subjects | Blood Platelets - enzymology Blotting, Western Cell Adhesion Molecules - blood Cell Adhesion Molecules - pharmacology Electrophoresis, Polyacrylamide Gel Enzyme Precursors - antagonists & inhibitors Enzyme Precursors - blood Fibrinogen - metabolism Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Humans Intracellular Signaling Peptides and Proteins Peptides - pharmacology Phosphorylation - drug effects Platelet Adhesiveness - drug effects Platelet Aggregation Inhibitors - pharmacology Precipitin Tests Protein-Tyrosine Kinases - antagonists & inhibitors Protein-Tyrosine Kinases - blood Protein-Tyrosine Kinases - pharmacology Syk Kinase |
title | Echistatin inhibits pp72syk and pp125FAK phosphorylation in fibrinogen-adherent platelets |
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