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Article

Differential Glycosylation and Modulation of Camel and Human HSP Isoforms in Response to Thermal and Hypoxic Stresses

1
Department of Physiological Chemistry, University of Veterinary Medicine Hannover, 30559 Hannover, Germany
2
Department of Biochemistry and Chemistry of Nutrition, Faculty of Veterinary Medicine, Cairo University, Giza 12211, Egypt
*
Author to whom correspondence should be addressed.
Current address: Department of Gastroenterology, Hepatology and Endocrinology, Hannover Medical School, 30625 Hannover, Germany.
Int. J. Mol. Sci. 2018, 19(2), 402; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19020402
Received: 8 December 2017 / Revised: 18 January 2018 / Accepted: 26 January 2018 / Published: 30 January 2018
(This article belongs to the Collection Protein Folding)
Increased expression of heat shock proteins (HSPs) following heat stress or other stress conditions is a common physiological response in almost all living organisms. Modification of cytosolic proteins including HSPs by O-GlcNAc has been shown to enhance their capabilities for counteracting lethal levels of cellular stress. Since HSPs are key players in stress resistance and protein homeostasis, we aimed to analyze their forms at the cellular and molecular level using camel and human HSPs as models for efficient and moderate thermotolerant mammals, respectively. In this study, we cloned the cDNA encoding two inducible HSP members, HSPA6 and CRYAB from both camel (Camelus dromedarius) and human in a Myc-tagged mammalian expression vector. Expression of these chaperones in COS-1 cells revealed protein bands of approximately 25-kDa for both camel and human CRYAB and 70-kDa for camel HSPA6 and its human homologue. While localization and trafficking of the camel and human HSPs revealed similar cytosolic localization, we could demonstrate altered glycan structure between camel and human HSPA6. Interestingly, the glycoform of camel HSPA6 was rapidly formed and stabilized under normal and stress culture conditions whereas human HSPA6 reacted differently under similar thermal and hypoxic stress conditions. Our data suggest that efficient glycosylation of camel HSPA6 is among the mechanisms that provide camelids with a superior capability for alleviating stressful environmental circumstances. View Full-Text
Keywords: camel; heat shock proteins; HSPA6; CRYAB; O-GlcNAc; hypoxia; heat stress; protein expression camel; heat shock proteins; HSPA6; CRYAB; O-GlcNAc; hypoxia; heat stress; protein expression
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MDPI and ACS Style

Hoter, A.; Amiri, M.; Prince, A.; Amer, H.; Warda, M.; Naim, H.Y. Differential Glycosylation and Modulation of Camel and Human HSP Isoforms in Response to Thermal and Hypoxic Stresses. Int. J. Mol. Sci. 2018, 19, 402. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19020402

AMA Style

Hoter A, Amiri M, Prince A, Amer H, Warda M, Naim HY. Differential Glycosylation and Modulation of Camel and Human HSP Isoforms in Response to Thermal and Hypoxic Stresses. International Journal of Molecular Sciences. 2018; 19(2):402. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19020402

Chicago/Turabian Style

Hoter, Abdullah, Mahdi Amiri, Abdelbary Prince, Hassan Amer, Mohamad Warda, and Hassan Y. Naim 2018. "Differential Glycosylation and Modulation of Camel and Human HSP Isoforms in Response to Thermal and Hypoxic Stresses" International Journal of Molecular Sciences 19, no. 2: 402. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19020402

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