Peptide N-glycosidase F Production for N-glycan Release


Ntelitze E., Karyelioğlu M., Duman H., Karav S.

in: Advanced and Contemporary Studies in Health Sciences, Assoc. Prof. Sadettin Demirel, Editor, Duvar Yayınları, İzmir, pp.90-99, 2023

  • Publication Type: Book Chapter / Chapter Research Book
  • Publication Date: 2023
  • Publisher: Duvar Yayınları
  • City: İzmir
  • Page Numbers: pp.90-99
  • Editors: Assoc. Prof. Sadettin Demirel, Editor
  • Çanakkale Onsekiz Mart University Affiliated: Yes

Abstract

Glycans, intricate molecules composed of sugars, represent an indispensable fraction among the fundamental constituents of cellular architecture and stand as one of nature's most abundant and diverse biopolymers (Lowe & Marth, 2003). These molecular entities exhibit versatility in their existence, manifesting either as independent oligosaccharides or integrated forms within glycoconjugates. The intricate process of glycosylation, wherein oligosaccharides intricately bind to proteins to create glycoproteins, emerges as a prevalent post-translational modification witnessed within cellular mechanisms. This glycosylation phenomenon profoundly influences the development and functionality of specific brain regions, crucial segments of the gastrointestinal system, and pivotal operations within the hepatic, visual, and immune systems, thereby underlining its paramount importance in biological processes. Moreover, the landscape of eukaryotic proteins is significantly shaped by the prevalence of glycoproteins, constituting more than half of these vital cellular components (Freeze et al., 2015). The formation of glycoproteins, functioning as glycoconjugates, ensues through the attachment of one or multiple glycans to proteins, typically occurring through N- or O-linked manners, conjoined with a polypeptide structure (Varki & Lowe, 2009). Particularly within eukaryotic secretory pathways, the regulation of crucial proteins predominantly hinges on the orchestration conducted by N-linked glycans (N-glycans). Furthermore, the intricate ballet of glycoprotein folding is modulated by the delicate equilibrium orchestrated by N-glycans, as elucidated by studies delving into glycoprotein balance (Helenius & Aebi, 2001). The exploration of glycoprotein balance not only enriches our understanding of cellular dynamics but also holds substantial promise in steering the development of novel pharmaceutical interventions, envisaged to potentially combat and mitigate diverse diseases on the horizon (Hebert et al., 2014).