Activation and inhibition of insulin receptor autophosphorylation by trypsin treatment of intact H35 cells |
| |
Institution: | 2. Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, U.S.A.;1. Department of Geography & Geology, University of the West Indies, Jamaica;2. Department of Geography, Rutgers University, 54 Joyce Kilmer Ave, Piscataway NJ 08854, USA;1. University of Nis, Faculty of Mechanical Engineering, Department for Mechatronics and Control, Aleksandra Medvedeva 14, 18000 Nis, Serbia;2. University of Nis, Faculty of Civil Engineering and Architecture, Aleksandra Medvedeva 14, 18000 Nis, Serbia;3. Department of Computer System and Technology, Faculty of Computer Science and Information Technology, Kuala Lumpur 50603, Malaysia;4. Department of Civil Engineering, Faculty of Engineering, University of Malaya, Kuala Lumpur 50603, Malaysia;5. Institute of Ocean and Earth Sciences (IOES), University of Malaya, Kuala Lumpur 50603, Malaysia;6. Department of Civil Engineering, Razi University, Kermanshah, Iran;1. State Key Laboratory of Acoustics, Institute of Acoustics, Chinese Academy of Sciences, Beijing, 100190, China;2. University of Chinese Academy of Sciences, Beijing, 100049, China;3. Beijing Engineering Research Center of Sea Deep Drilling and Exploration, Institute of Acoustics, Chinese Academy of Sciences, Beijing, 100190, China |
| |
Abstract: | - 1.1. Treatment of intact cultured H35 cells with trypsin (1 mg/ml) for 15 min at low temperature (4°C) or for 30 sec at 37°C causes activation of the insulin receptor subsequently isolated from the cells.
- 2.2. Receptor activation was assessed by increased phosphotyrosine content of the β-subunit of the receptor, and increased autophosphorylation using 32P]-ATP.
- 3.3. Treatment of the cells for 15 min at 37°C however completely abolished insulin binding and all insulin receptor kinase activity.
- 4.4. These data demonstrate that proteolytic damage of the extracellular domain of the insulin receptor can render the receptor kinase inactive and lead to a cell which is unresponsive to insulin.
|
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|