Date of Graduation
Fall 2011
Degree
Master of Science in Cell and Molecular Biology
Department
Biomedical Sciences
Committee Chair
Rehana Levely
Abstract
Fibrinogen gamma' (Y') is a minor isoform of fibrinogen, a plasma protein that contains an altered Y chain due to an insertion sequence of 20 amino acids. The fibrinogen Y' chain binds to thrombin with high affinity at a positively charged surface or exosite II, mainly through its interactions at residues 410-427. Several recent studies have shown that binding of fibrinogen Y' inhibits thrombin induced platelet aggregation and the presence of fibrinogen Y' changes clot architecture. Fibrinogen Y' peptide has been shown to affect thrombin interaction with platelet receptors, mainly binding of thrombin to GpIb-α, and it prevents thrombin cleavage of protease activated receptor PAR-1. This study investigated the inhibitory effect of fibrinogen Y' peptide on thrombin- induced dense granule release and intraplatelet calcium mobilization which indicates platelets activation. My study have shown that the fibrinogen Y' peptide inhibits thrombin- induced dense granule release and calcium mobilization in platelets. In summary, fibrinogen Y' peptide binds to thrombin and inhibits the platelet response to thrombin. Thus, this study may help in assessing the effects of fibrinogen Y' and indicate the potential of fibrinogen Y' as an antithrombotic therapeutic agent.
Keywords
fibrinogen γ', thrombin, platelet activation, platelet receptors, antithrombotic
Subject Categories
Medical Molecular Biology
Copyright
© Amruta Ashtekar
Recommended Citation
Ashtekar, Amruta, "Fibrinogen Gamma' Inhibits Thrombin-Induced Platelet Activation" (2011). MSU Graduate Theses. 3018.
https://bearworks.missouristate.edu/theses/3018
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