Heat Stress-induced Protein Glycosylation in Mammalian Cells

• Published in: Trends in Glycoscience and Glycotechnology 1995/05/02, Vol.7(35), pp.191-204
• Main Authors: Henle, Kurt J., Jethmalani, Sunita M., Nagle, William A.
• Format: Article
• Language: English
• Subjects: calreticulin; GP50; heat shock proteins; stress glycosylation; thermotolerance
• ISSN: 0915-7352; 1883-2113
• DOI: 10.4052/tigg.7.191

The cellular stress response is a model for the regulation of gene expression and represents a highly conserved mechanism for cells that respond to a changing environment. The cellular stress response includes a significant glycobiological component, which although not well characterized, appears essential and complementary to the role of“classical” heat shock proteins (HSPs). This review concentrates on the glycobio-logical component of the mammalian stress response, where several major heat stress-induced glycoproteins have been identified to date. For example, the expression and glycosylation of GP50 and GP62 is associated with the development of thermotolerance, while P-SG67 and P-SG64 are glycosylated “promptly”, i.e., within minutes after the initiation of heat stress. GP50 in CHO cells is homologous to the serpin family-related retinoic acid-inducible mouse J6 gene product, whereas P-SG67 and P-SG64 are glycosylated variants of the multifunctional ER protein, calreticulin. Potential functions for stress glycoproteins and their possible interaction with HSPs are discussed. The availability of molecular probes for stress glycoproteins should facilitate studies to understand their functions and to utilize them in biotechnological applications.