Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets
Trigramin, a naturally occurring peptide purified from Trimeresurus gramineus (T. stejnegeri formosensis) snake venom, inhibits platelet aggregation and the binding of 125I-fibrinogen to ADP-stimulated platelets (Ki = 2 X 10(-8) M) without affecting the platelet-release reaction. 125I-trigramin bind...
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| Veröffentlicht in: | Biochemistry (Easton) 1989-01, Vol.28 (2), p.661-666 |
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| creator | Huang, Tur Fu Holt, John C Kirby, Edward P Niewiarowski, Stefan |
| description | Trigramin, a naturally occurring peptide purified from Trimeresurus gramineus (T. stejnegeri formosensis) snake venom, inhibits platelet aggregation and the binding of 125I-fibrinogen to ADP-stimulated platelets (Ki = 2 X 10(-8) M) without affecting the platelet-release reaction. 125I-trigramin binds to ADP-stimulated and to chymotrypsin-treated normal platelets but not to thrombasthenic platelets. 125I-trigramin binding to platelets is blocked by monoclonal antibodies directed against the glycoprotein IIb/IIIa complex and by Arg-Gly-Asp-Ser (RGDS) [Huang et al. (1987) J. Biol. Chem. 262, 161]. We determined the primary structure of trigramin, which is composed of a single polypeptide chain of 72 amino acid residues and six disulfide bridges. The molecular weight of trigramin calculated on the basis of amino acid sequence was 7500, and the average pI was 5.61. An RGD sequence appeared in the carboxy-terminal domain of trigramin. An amino-terminal fragment (7-33) of trigramin showed 39% homology with a region (1555-1581) of von Willebrand factor (vWF). Trigramin also showed 36% identity in a 42 amino acid overlap and 53% identity in a 15 amino acid overlap when compared with two adhesive proteins, collagen alpha 1 (I) and laminin B1, respectively. Trigramin blocked binding of human vWF to the glycoprotein IIb/IIIa complex in thrombin-activated platelets in a dose-dependent manner. Reduction of trigramin resulted in a marked decrease in its ability to block vWF binding to human platelets. |
| doi_str_mv | 10.1021/bi00428a037 |
| format | Article |
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(1987) J. Biol. Chem. 262, 161]. We determined the primary structure of trigramin, which is composed of a single polypeptide chain of 72 amino acid residues and six disulfide bridges. The molecular weight of trigramin calculated on the basis of amino acid sequence was 7500, and the average pI was 5.61. An RGD sequence appeared in the carboxy-terminal domain of trigramin. An amino-terminal fragment (7-33) of trigramin showed 39% homology with a region (1555-1581) of von Willebrand factor (vWF). Trigramin also showed 36% identity in a 42 amino acid overlap and 53% identity in a 15 amino acid overlap when compared with two adhesive proteins, collagen alpha 1 (I) and laminin B1, respectively. Trigramin blocked binding of human vWF to the glycoprotein IIb/IIIa complex in thrombin-activated platelets in a dose-dependent manner. Reduction of trigramin resulted in a marked decrease in its ability to block vWF binding to human platelets.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00428a037</identifier><identifier>PMID: 2653425</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>550201 - Biochemistry- Tracer Techniques ; AMINO ACID SEQUENCE ; AMINO ACIDS ; ANIMALS ; ANTIBODIES ; ARGININE ; ASPARTIC ACID ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BIOLOGICAL MATERIALS ; BLOOD ; BLOOD CELLS ; BLOOD COAGULATION ; BLOOD PLATELETS ; BODY FLUIDS ; CARBOHYDRATES ; CARBOXYLIC ACIDS ; CHEMICAL REACTIONS ; CROSS-LINKING ; Crotalid Venoms - chemistry ; DAYS LIVING RADIOISOTOPES ; ELECTRON CAPTURE RADIOISOTOPES ; Fibrinogen - antagonists & inhibitors ; GLUCOPROTEINS ; GLYCINE ; GLYCOPROTEINS ; Humans ; HYDROXY ACIDS ; INHIBITION ; INTERMEDIATE MASS NUCLEI ; IODINE 125 ; IODINE ISOTOPES ; ISOTOPES ; MATERIALS ; MEMBRANE PROTEINS ; Molecular Sequence Data ; MOLECULAR STRUCTURE ; MONOCLONAL ANTIBODIES ; NUCLEI ; ODD-EVEN NUCLEI ; ORGANIC ACIDS ; ORGANIC COMPOUNDS ; Peptide Hydrolases ; PEPTIDES ; Peptides - isolation & purification ; Peptides - pharmacology ; Platelet Membrane Glycoproteins - metabolism ; POLYMERIZATION ; PROTEINS ; RADIOISOTOPES ; RECEPTORS ; REPTILES ; SACCHARIDES ; Sequence Homology, Nucleic Acid ; SERINE ; SNAKES ; trigramin ; Trimeresurus gramineus ; venom ; VENOMS ; VERTEBRATES ; von Willebrand factor ; von Willebrand Factor - metabolism</subject><ispartof>Biochemistry (Easton), 1989-01, Vol.28 (2), p.661-666</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a327t-6bdb80ced5bb38a9c5d00d5a182ad17ea9b2161e02d8b33a275fb4c289f0c30e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00428a037$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00428a037$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2653425$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/5405722$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, Tur Fu</creatorcontrib><creatorcontrib>Holt, John C</creatorcontrib><creatorcontrib>Kirby, Edward P</creatorcontrib><creatorcontrib>Niewiarowski, Stefan</creatorcontrib><title>Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Trigramin, a naturally occurring peptide purified from Trimeresurus gramineus (T. stejnegeri formosensis) snake venom, inhibits platelet aggregation and the binding of 125I-fibrinogen to ADP-stimulated platelets (Ki = 2 X 10(-8) M) without affecting the platelet-release reaction. 125I-trigramin binds to ADP-stimulated and to chymotrypsin-treated normal platelets but not to thrombasthenic platelets. 125I-trigramin binding to platelets is blocked by monoclonal antibodies directed against the glycoprotein IIb/IIIa complex and by Arg-Gly-Asp-Ser (RGDS) [Huang et al. (1987) J. Biol. Chem. 262, 161]. We determined the primary structure of trigramin, which is composed of a single polypeptide chain of 72 amino acid residues and six disulfide bridges. The molecular weight of trigramin calculated on the basis of amino acid sequence was 7500, and the average pI was 5.61. An RGD sequence appeared in the carboxy-terminal domain of trigramin. An amino-terminal fragment (7-33) of trigramin showed 39% homology with a region (1555-1581) of von Willebrand factor (vWF). Trigramin also showed 36% identity in a 42 amino acid overlap and 53% identity in a 15 amino acid overlap when compared with two adhesive proteins, collagen alpha 1 (I) and laminin B1, respectively. Trigramin blocked binding of human vWF to the glycoprotein IIb/IIIa complex in thrombin-activated platelets in a dose-dependent manner. Reduction of trigramin resulted in a marked decrease in its ability to block vWF binding to human platelets.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>AMINO ACID SEQUENCE</subject><subject>AMINO ACIDS</subject><subject>ANIMALS</subject><subject>ANTIBODIES</subject><subject>ARGININE</subject><subject>ASPARTIC ACID</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>BLOOD COAGULATION</subject><subject>BLOOD PLATELETS</subject><subject>BODY FLUIDS</subject><subject>CARBOHYDRATES</subject><subject>CARBOXYLIC ACIDS</subject><subject>CHEMICAL REACTIONS</subject><subject>CROSS-LINKING</subject><subject>Crotalid Venoms - chemistry</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>Fibrinogen - antagonists & inhibitors</subject><subject>GLUCOPROTEINS</subject><subject>GLYCINE</subject><subject>GLYCOPROTEINS</subject><subject>Humans</subject><subject>HYDROXY ACIDS</subject><subject>INHIBITION</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>ISOTOPES</subject><subject>MATERIALS</subject><subject>MEMBRANE PROTEINS</subject><subject>Molecular Sequence Data</subject><subject>MOLECULAR STRUCTURE</subject><subject>MONOCLONAL ANTIBODIES</subject><subject>NUCLEI</subject><subject>ODD-EVEN NUCLEI</subject><subject>ORGANIC ACIDS</subject><subject>ORGANIC COMPOUNDS</subject><subject>Peptide Hydrolases</subject><subject>PEPTIDES</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - pharmacology</subject><subject>Platelet Membrane Glycoproteins - metabolism</subject><subject>POLYMERIZATION</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>RECEPTORS</subject><subject>REPTILES</subject><subject>SACCHARIDES</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>SERINE</subject><subject>SNAKES</subject><subject>trigramin</subject><subject>Trimeresurus gramineus</subject><subject>venom</subject><subject>VENOMS</subject><subject>VERTEBRATES</subject><subject>von Willebrand factor</subject><subject>von Willebrand Factor - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcGL1DAUxoMo6-zqybMQPLgHqfuSNE27Nx10LSwoOKJ4CUmazmRtkzFJZffuH26HDosHwdPj8f3yPfJ9CD0j8JoAJRfaAZS0VsDEA7QinEJRNg1_iFYAUBW0qeAxOk3pZl5LEOUJOqEVZyXlK_R7E902qtH5S7yPblTxDqccJ5OnaLHyHXY5Yed3Trvsgsehx7_m8dUNg9XxAPTK5BCxdr5zfotzwNvhzoR9DNk6j9tWX7Rtq7AJ436wt3h-vZtG5fF-UNkONqcn6FGvhmSfHucZ-vL-3Wb9obj-eNWu31wXilGRi0p3ugZjO641q1VjeAfQcUVqqjoirGo0JRWxQLtaM6ao4L0uDa2bHgwDy87Qi8U3pOxkMi5bszPBe2uy5CVwQekMvVyg-QM_J5uyHF0ydhiUt2FKUtSNgDnF_4KEE8FIeXB8tYAmhpSi7eUxaUlAHhqUfzU408-PtpMebXfPHiub9WLRXcr29l5W8YesBBNcbj59ls1V-Xb9rf4uD_z5wiuT5E2Yop8j_uflP4Djsy8</recordid><startdate>19890124</startdate><enddate>19890124</enddate><creator>Huang, Tur Fu</creator><creator>Holt, John C</creator><creator>Kirby, Edward P</creator><creator>Niewiarowski, Stefan</creator><general>American Chemical Society</general><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19890124</creationdate><title>Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets</title><author>Huang, Tur Fu ; Holt, John C ; Kirby, Edward P ; Niewiarowski, Stefan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a327t-6bdb80ced5bb38a9c5d00d5a182ad17ea9b2161e02d8b33a275fb4c289f0c30e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>AMINO ACID SEQUENCE</topic><topic>AMINO ACIDS</topic><topic>ANIMALS</topic><topic>ANTIBODIES</topic><topic>ARGININE</topic><topic>ASPARTIC ACID</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BIOLOGICAL MATERIALS</topic><topic>BLOOD</topic><topic>BLOOD CELLS</topic><topic>BLOOD COAGULATION</topic><topic>BLOOD PLATELETS</topic><topic>BODY FLUIDS</topic><topic>CARBOHYDRATES</topic><topic>CARBOXYLIC ACIDS</topic><topic>CHEMICAL REACTIONS</topic><topic>CROSS-LINKING</topic><topic>Crotalid Venoms - chemistry</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>Fibrinogen - antagonists & inhibitors</topic><topic>GLUCOPROTEINS</topic><topic>GLYCINE</topic><topic>GLYCOPROTEINS</topic><topic>Humans</topic><topic>HYDROXY ACIDS</topic><topic>INHIBITION</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>ISOTOPES</topic><topic>MATERIALS</topic><topic>MEMBRANE PROTEINS</topic><topic>Molecular Sequence Data</topic><topic>MOLECULAR STRUCTURE</topic><topic>MONOCLONAL ANTIBODIES</topic><topic>NUCLEI</topic><topic>ODD-EVEN NUCLEI</topic><topic>ORGANIC ACIDS</topic><topic>ORGANIC COMPOUNDS</topic><topic>Peptide Hydrolases</topic><topic>PEPTIDES</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - pharmacology</topic><topic>Platelet Membrane Glycoproteins - metabolism</topic><topic>POLYMERIZATION</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>RECEPTORS</topic><topic>REPTILES</topic><topic>SACCHARIDES</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>SERINE</topic><topic>SNAKES</topic><topic>trigramin</topic><topic>Trimeresurus gramineus</topic><topic>venom</topic><topic>VENOMS</topic><topic>VERTEBRATES</topic><topic>von Willebrand factor</topic><topic>von Willebrand Factor - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, Tur Fu</creatorcontrib><creatorcontrib>Holt, John C</creatorcontrib><creatorcontrib>Kirby, Edward P</creatorcontrib><creatorcontrib>Niewiarowski, Stefan</creatorcontrib><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>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><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Tur Fu</au><au>Holt, John C</au><au>Kirby, Edward P</au><au>Niewiarowski, Stefan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1989-01-24</date><risdate>1989</risdate><volume>28</volume><issue>2</issue><spage>661</spage><epage>666</epage><pages>661-666</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Trigramin, a naturally occurring peptide purified from Trimeresurus gramineus (T. stejnegeri formosensis) snake venom, inhibits platelet aggregation and the binding of 125I-fibrinogen to ADP-stimulated platelets (Ki = 2 X 10(-8) M) without affecting the platelet-release reaction. 125I-trigramin binds to ADP-stimulated and to chymotrypsin-treated normal platelets but not to thrombasthenic platelets. 125I-trigramin binding to platelets is blocked by monoclonal antibodies directed against the glycoprotein IIb/IIIa complex and by Arg-Gly-Asp-Ser (RGDS) [Huang et al. (1987) J. Biol. Chem. 262, 161]. We determined the primary structure of trigramin, which is composed of a single polypeptide chain of 72 amino acid residues and six disulfide bridges. The molecular weight of trigramin calculated on the basis of amino acid sequence was 7500, and the average pI was 5.61. An RGD sequence appeared in the carboxy-terminal domain of trigramin. An amino-terminal fragment (7-33) of trigramin showed 39% homology with a region (1555-1581) of von Willebrand factor (vWF). Trigramin also showed 36% identity in a 42 amino acid overlap and 53% identity in a 15 amino acid overlap when compared with two adhesive proteins, collagen alpha 1 (I) and laminin B1, respectively. Trigramin blocked binding of human vWF to the glycoprotein IIb/IIIa complex in thrombin-activated platelets in a dose-dependent manner. Reduction of trigramin resulted in a marked decrease in its ability to block vWF binding to human platelets.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>2653425</pmid><doi>10.1021/bi00428a037</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemistry (Easton), 1989-01, Vol.28 (2), p.661-666 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_osti_scitechconnect_5405722 |
| source | ACS Publications; MEDLINE |
| subjects | 550201 - Biochemistry- Tracer Techniques AMINO ACID SEQUENCE AMINO ACIDS ANIMALS ANTIBODIES ARGININE ASPARTIC ACID BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BIOLOGICAL MATERIALS BLOOD BLOOD CELLS BLOOD COAGULATION BLOOD PLATELETS BODY FLUIDS CARBOHYDRATES CARBOXYLIC ACIDS CHEMICAL REACTIONS CROSS-LINKING Crotalid Venoms - chemistry DAYS LIVING RADIOISOTOPES ELECTRON CAPTURE RADIOISOTOPES Fibrinogen - antagonists & inhibitors GLUCOPROTEINS GLYCINE GLYCOPROTEINS Humans HYDROXY ACIDS INHIBITION INTERMEDIATE MASS NUCLEI IODINE 125 IODINE ISOTOPES ISOTOPES MATERIALS MEMBRANE PROTEINS Molecular Sequence Data MOLECULAR STRUCTURE MONOCLONAL ANTIBODIES NUCLEI ODD-EVEN NUCLEI ORGANIC ACIDS ORGANIC COMPOUNDS Peptide Hydrolases PEPTIDES Peptides - isolation & purification Peptides - pharmacology Platelet Membrane Glycoproteins - metabolism POLYMERIZATION PROTEINS RADIOISOTOPES RECEPTORS REPTILES SACCHARIDES Sequence Homology, Nucleic Acid SERINE SNAKES trigramin Trimeresurus gramineus venom VENOMS VERTEBRATES von Willebrand factor von Willebrand Factor - metabolism |
| title | Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets |
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