Publications by authors named "Agata A Nowak"

We have examined the effect of the O-linked glycan (OLG) structures of VWF on its interaction with the platelet receptor glycoprotein Ibα. The 10 OLGs were mutated individually and as clusters (Clus) on either and both sides of the A1 domain: Clus1 (N-terminal side), Clus2 (C-terminal side), and double cluster (DC), in both full-length-VWF and in a VWF construct spanning D' to A3 domains. Mutations did not alter VWF secretion by HEK293T cells, multimeric structure, or static collagen binding.

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Article Synopsis
  • The study investigates how N-linked glycans (NLGs) influence the production and secretion of von Willebrand Factor (VWF).
  • Blocking or altering specific NLG sites in VWF disrupts its secretion, with certain mutations leading to significant reductions in expression.
  • Mutations at specific sites caused VWF to be retained in the endoplasmic reticulum, produced fewer storage bodies, and increased free thiol reactivity, highlighting the importance of NLGs for VWF functioning.
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Synopsis of recent research by authors named "Agata A Nowak"

  • - Agata A Nowak's research primarily focuses on the role of glycosylation in the function and secretion of von Willebrand Factor (VWF), particularly how O-linked and N-linked glycan structures influence its interaction with platelet receptors and its overall synthesis.
  • - In her studies, she has demonstrated that while mutations in O-linked glycan structures affect the interaction of VWF with glycoprotein Ib, they do not impact its secretion or multimeric structure under various conditions, indicating a specific functional significance of these glycans.
  • - Additionally, her work highlights the critical importance of N-linked glycosylation, revealing that the presence of these glycans is essential for the proper synthesis and secretion of VWF, pointing to specific sites that are crucial in this process.