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Redox dependent disulfide bonding of Von Willebrand factor A1A2A2 domains

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  1. Tez No: 400823
  2. Yazar: ESRA SEYRAN
  3. Danışmanlar: DR. WESLEY STITES
  4. Tez Türü: Doktora
  5. Konular: Zooloji, Zoology
  6. Anahtar Kelimeler: Belirtilmemiş.
  7. Yıl: 2013
  8. Dil: İngilizce
  9. Üniversite: University of Arkansas
  10. Enstitü: Yurtdışı Enstitü
  11. Ana Bilim Dalı: Bitki Islahı ve Genetik Ana Bilim Dalı
  12. Bilim Dalı: Belirtilmemiş.
  13. Sayfa Sayısı: 125

Özet

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Özet (Çeviri)

Von Willebrand factor (VWF) is a large glycoprotein that plays an important role in primary hemostasis by forming a bridge between subendothelial matrix and platelets. The most striking feature of VWF is its ability to dramatically shift from a non-adhesive plasma soluble protein to a multi-functional adhesive protein, as an activated surface, attractive to the flowing platelets. The segmental structure of VWF forms the basis of its multifunctional properties. Binding sites that are independent of multimer assembly but important for the hemostatic function are located in the A1A2A3 domains of VWF. VWF A1A2A3 domain contains six cysteine residues in three disulfides, one being a vicinal disulfide. Established view is that disulfide bonds are inert motifs, stabilizing the protein structure. However vicinal disulfides in proteins are reported to function as redox activated conformational switches. In order to understand the redox dependent disulfide bonding of VWF A1A2A3 domain, we conducted experiments in reduced and oxidized glutathione environment. Disulfide mapping was performed by digesting A1A2A3 domain using GluC and analyzing it by using matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). It was evident from the MALDI-MS data that the changes occur in disulfide bonding pattern in the glutathione environment. The regulation of VWF structure and function is important in the context of cardiovascular diseases since they are associated with elevated VWF activity. Improvement of our understanding over the structure, function and conformation of VWF could possibly make this protein a drug target, advancements in this area is an interest to the pharmaceutical industry.

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