Role of the ALG7 gene in the postnatal development of hamster submandibular gland

Date
2001
DOI
Authors
Erkan, Fatih
Version
OA Version
Citation
Abstract
Protein N-glycosylation is important for correct execution of many cellular functions during development including cell proliferation, polarization and differentiation. Increasing evidence indicates that a key determinant of protein Nglycosylation, the ALG7 gene, plays critical roles in these processes. An early growth response gene and conserved from yeast to mammals, ALG7 has been shown to affect cell cycle progression and arrest, as well as changes in the cell polarity. Since the level of expression of ALG7 has profound effects on diverse cellular function during development, we have postulated that ALG7 influences the activity of specific N-glycoproteins by affecting the extent of N-glycosylation and that its regulation is important to N-glycosylation machinery. In order to elucidate molecular mechanism underlying the involvement of ALG7 gene in developmental processes, we first examined the expression and localization of GPT, protein product of ALG7, and other developmentally relevant proteins, F-actin and p1 integrin , during hamster submandibular gland postnatal development. We also examined the effects of deregulated expression of ALG7 on the extent of specific N-glycoproteins in yeast. Results have indicated that regulated expression of ALG 7 gene is likely to affect various aspects SMG development. Studies with yeast confirmed that this is because ALG7 regulates the N-glycosylation capacity of proliferating and differentiating cells. We conclude that modulation of ALG7 expression leads to selective changes in the glycosylation status of specific N-glycoproteins. Therefore by affecting N-glycosylation status of proteins, ALG7 may regulate various cell functions during the development of submandibular gland.
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Thesis (M.Sc.D.)--Boston University, Henry M. Goldman School of Dental Medicine, 2001 (Oral Biology).
Includes bibliographical references (leaves 78-90).
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This work is protected by copyright. Downloading is restricted to the BU community. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.