Ryanodine receptor 1 mediates Ca2+ transport and influences the biomechanical properties in RBCs |
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| Authors: | Xianwei Wang Xi Chen Zhiyu Tang Weijuan Yao Xiao Liu Risheng Wei Xifu Wang Weibo Ka Dagong Sun Dongqi He Zongyao Wen Shu Chien |
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| Institution: | 1. Department of Biophysics, Health Science Center, Peking University, Beijing 100191, PR China;2. Department of Cardiology, Peking University Shougang Hospital, Beijing 100144, PR China;3. Department of Medical Physics, Health Science Center, Peking University, Beijing 100191, PR China;4. Department of Bioengineering and Medicine, University of California, San Diego, La Jolla, CA 92093-0412, USA;1. National Heart and Lung Institute, Imperial College London, London, UK;2. Royal Brompton and Harefield NHS Foundation Trust, London, UK;4. Respiratory Medicine Unit, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7FZ, UK;3. Medical Research Service, The Department of Veterans Affairs, Nebraska-Western Iowa Health Care System, Omaha, Nebraska 68105;4. Departments of Biochemistry & Molecular Biology, Internal Medicine and Pharmacology & Experimental Neuroscience, University of Nebraska Medical Center, Omaha, Nebraska 68198;1. Department of Mechanical Engineering, Carnegie Mellon University, USA;2. Institute of Computational Mathematics, Academy of Mathematics and Systems Science, Chinese Academy of Sciences, China;1. Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China;2. Electron Microscopy Analysis Laboratory, The Health Science Center, Peking University, Beijing, 100191, China;3. Center for Protein Science, Peking University, Beijing, 100871, China;1. The Department of Cardiology, The First Affiliated Hospital of Harbin Medical University, No.23, YouZheng Road, NanGang District, Harbin 150001, Heilongjiang Province, China;2. The Department of Gastroenterology, The Second Affiliated Hospital of Harbin Medical University, Harbin, China |
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| Abstract: | Ryanodine receptors (RyRs) are a family of Ca2+ channel proteins that mediate the massive release of Ca2+ from the endoplasmic reticulum into the cytoplasma. In the present study, we manipulated the incorporation of RyR1 into RBC membrane and investigated its influences on the intracellular Ca2+ (Ca2+]in) level and the biomechanical properties in RBCs. The incorporation of RyR1 into RBC membranes was demonstrated by both immunofluorescent staining and the change of Ca2+]in of RBCs. In the presence of RyR1, Ca2+]in showed biphasic changes, i.e., it increased with the extracellular Ca2+ (Ca2+]ex) up to 5 μM and then decreased with the further increase of Ca2+]ex. However, Ca2+]in remained constant in the absence of the RyR1. The results of biomechanical measurements on RBCs, including deformability, osmotic fragility, and membrane microviscosity, reflected similar biphasic changes of Ca2+]in mediated by RyR1 with the increases of Ca2+]ex. Therefore, it is believed that RyR1 can incorporate into RBC membrane in vitro, and mediate Ca2+ influx, and then regulate RBC biomechanical properties. This information suggests that RBCs may serve as a model to study the function of RyR1 as a Ca2+ release channel. |
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