Glucose starvation alters insulin but not IGF-I binding to Chinese hamster ovary (CHO) cells |
| |
| Authors: | J M Podskalny D G Rouiller A McElduff P Gorden |
| |
| Affiliation: | 1. Department of Pathology, Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia;2. Department of Medical Laboratory Technology, Faculty of Applied Medical Sciences, King Abdulaziz University, Jeddah, Saudi Arabia;3. Department of Pathology, Rabigh Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia;4. Department of Family and Community Medicine, Rabigh Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia;5. Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, Jeddah, Saudi Arabia;6. Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia;7. Immunology Unit, King Fahad Research Medical Centre, King Abdulaziz University, Jeddah, Saudi Arabia;8. Department of Radiology, KAU Hospital, Jeddah, Saudi Arabia;9. Department of Human Metabolism, University of Sheffield, UK;1. Laboratory of Biological Modeling, NIDDK National Institutes of Health Bethesda, MD 20892, United States;2. Department of Mathematics and Programs in Molecular Biophysics and Neuroscience, Florida State University Tallahassee, FL 32301, United States |
| |
| Abstract: | The pattern of cellular protein glycosylation can be altered in CHO cells by glucose starvation. When wild type CHO cells are deprived of glucose, 125I-insulin binding increases from a B/F of 0.033 +/- 0.004 to 0.063 +/- 0.011, due to an increase in receptor affinity. The already elevated insulin binding to mutant B4-2-1 CHO cells, whose genetic defect causes abnormal glycosylation mimicking the pattern seen in the glucose starved normal cells, is not affected by glucose starvation. In neither cell line is 125I-IGF-I binding affected by glucose starvation. These data support the hypothesis that abnormal glycosylation can alter insulin binding to its receptor. Furthermore, there is a striking difference in the susceptibility of IGF-I and insulin receptors to alterations in glycosylation. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
