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Administration of γ′ peptides concomitantly with fibrinolytic agents such as t‐PA or during angioplasty has the potential to displace clot‐bound thrombin, thereby preventing restenosis.



The reaction of thrombin with fibrinogen‐like peptides containing 11, 14, and 16 residuesThe amino acid sequence in fibrin responsible for high affinity thrombin bindingγ and γ′ chains of human fibrinogen are produced by alternative mRNA processingStructure of the human γ‐fibrinogen gene.




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The carboxyl terminal sequences from amino acid 408 of the major form of the γ chain, γA (∼93%), and the minor form, γ′ (∼7%), are shown. A synthetic peptide corresponding to the carboxyl terminal 20 amino acids of the γ′ chain binds to thrombin with a Human γA/γA and γA/γ′ fibrinogen were purified from unfractionated plasminogen‐free fibrinogen (Calbiochem, La Jolla, CA, USA) using DEAE/cellulose chromatography as described previously [Recombinant fibrinogen molecules were expressed with tyrosine to phenylalanine mutations in the γ′ chain at positions γ′ 418 and/or γ′ 422. Fluorescein‐labeled VRPEHPAETE‐Y(POOne prediction of the concept that the γ′ peptide binds exosite II rather than exosite I is that the γ′ peptide should bind to γ‐thrombin, a proteolyzed product of α‐thrombin in which exosite I fails to bind fibrinogen or hirudin [Clot‐entrapped thrombin plays a significant role in thrombus growth and in restenosis following thrombolytic therapy, even when therapeutic levels of heparin are administered [The data presented herein which show that γ′ chain carboxyl terminal peptides bind to thrombin exosite II must be reconciled with reports that hirudin peptide binding to exosite I can displace fibrin‐bound thrombin [These data extend previous observations that the low‐affinity interaction of thrombin with fibrin is mediated by exosite I [Model of thrombin/γ′ chain interactions during coagulation and fibrinolysis. Future studies The authors wish to thank Dr Jeffrey I. Weitz for DNA aptamers to thrombin exosites I and II and for many helpful discussions.



and you may need to create a new Wiley Online Library account.Enter your email address below and we will send you your usernameIf the address matches an existing account you will receive an email with instructions to retrieve your username Active thrombin binds through exosite II to the γ′ chain in γA/γ′ fibrin, where it converts more fibrinogen to fibrin, thereby causing thrombus growth.

Alternate mRNA splicing near the 3′ end of the gene produces γA and γB forms of γ‐fibrinogenBiochemical and chromatographic studies of certain activities associated with human fibrinogen preparationsRecombinant human fibrinogen and sulfation of the γ′ chainThe C‐terminal sequences of the γ 57.5 chain of human fibrinogen constitute a plasmin sensitive epitope that is exposed in crosslinked fibrinDemonstration of a large molecular weight variant of the γ chain of normal human plasma fibrinogenHuman plasma fibrinogen heterogeneity: Evidence for an extended carboxyl‐terminal sequence in a normal γ chain variant (γ′)Fibrin monomer protects thrombin from inactivation by heparin‐antithrombin III.



Two potential binding sites for the highly negatively charged γ′ chain include anion‐binding exosites I and II [In this manuscript, expression of recombinant fibrinogen γ′/γ′ homodimers is used to definitively identify the sulfated tyrosine residues in the γ′ chain. Enter a 10-digit Phone Number. Fluorescein‐labeled VRPEHPAETE‐Y(POTo map the binding site of the γ′ peptide on thrombin, competitive binding assays were performed using ligands for exosite I and II.




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