Reproduction of light intensity-dependent activation of transducin in rod and cone by phototransduction model

被引:0
|
作者
Hosoki, Yukari [1 ]
Koike, Chieko [2 ]
Takeda, Yukari [1 ]
Amano, Akira [1 ]
机构
[1] Department of Life Sciences, Ritsumeikan University
[2] Department of Pharmaceutical Sciences, Ritsumeikan University
来源
Transactions of Japanese Society for Medical and Biological Engineering | 2014年 / 52卷 / 03期
基金
日本学术振兴会;
关键词
Phototransduction; Rhodopsin; Transducin; Visual cell model;
D O I
10.11239/jsmbe.52.145
中图分类号
学科分类号
摘要
Visual impairment has serious impact on our quality of life. Although stem cell-based therapies contribute to improve retinal diseases, it is essentially critical to have quantitative data of the physiological characteristics of retinal cellular functions and related neural networks for reliable treatment. In the phototransduction system of retinal photoreceptor cells, visual pigments are activated by the incident light and stimulate transducin, which in turn send electrical signals to downstream neural networks. A single visual pigment may activate hundreds of transducin, amplifying the incoming signal. Efficacy of the signal amplification system has been reported to be light intensity-dependent. Experimentally, a positive correlation between light intensity and activated transducin has been observed at a lower stimulation intensity range, whereas activated transducin starts to decrease at very high intensity light stimulation. Since none of the proposed phototransduction models were able to reproduce the complex characteristics of the signal transduction system of retinal photoreceptor cells, we propose a model that may reproduce the light intensity-dependent amplification of incoming signals in both rods and cones. The present model successfully reproduced the experimental data. © 2014, Japan Soc. of Med. Electronics and Biol. Engineering. All rights reserved.
引用
收藏
页码:145 / 155
页数:10
相关论文
共 18 条
  • [1] Tachibanaki S., Tsushima S., Kawamura S., Low ampilification and fast visual pigment phosphorylation as mechanisms characterizing cone photoresponses, Proceedings of the National Academy of Science, 98, 24, pp. 14044-14049, (2001)
  • [2] Forti S., Menini A., Rispoli G., Torre V., Kinetics of Phototransduction in Retinal Rods of the Newt Triturus Cristatus, J. Physiol, 419, pp. 265-295, (1989)
  • [3] Liu X.D., Kourennyi D.E., Effects of tetraethy-lammonium on Kx channels and simulated light response in rod photoreceptors, Ann. Biomed. Eng, 32, 10, pp. 1428-1442, (2004)
  • [4] Hamer R.D., Nicholas S.C., Tranchina D., Liebman P.A., Lamb T.D., Multiple Steps of Phosphorylation of Activated Rhodopsin Can Account for the Reproducibility of Vertebrate Rod Single-photon Responses, The Journal of General Physiology, 122, pp. 419-444, (2003)
  • [5] Hamer R.D., Nicholas S.C., Tranchina D., Lamb T.D., Jarvinen J.L., Toward a unified model of vertebraterod phototransduction, Visual Neuroscience, 22, 4, pp. 417-436, (2005)
  • [6] Korenbrot J.I., Speed, adaptation, and stability of the response to light in cone photoreceptors: The functional role of Ca-dependent modulation of ligand sensitivity in cGMP-gated ion channel, The Journal of General Physiology, 139, 1, pp. 31-56, (2012)
  • [7] Kandori H., Shichida Y., Yoshizawa T., Photoisomerization in Rhodopsin, Biochemistry, 66, 11, pp. 1197-1209, (2001)
  • [8] Tachibanaki S., Imai H., Mizukami T., Okada T., Imamoto Y., Matsuda T., Fukada Y., Terakita A., Shichida Y., Presence of Two Rhodopsin Intermediates Responsible for Transducin Activation, Biochemistry, 36, pp. 14173-14180, (1997)
  • [9] Maeda T., Imanishi Y., Palczewski K., Rhodopsin phosphorylation: 30 years later, Progress in Retinal and Eye Research, 22, 4, pp. 417-434, (2003)
  • [10] Ohguro H., Molecular Mechanisms of rhodopsin phosphorylation and dephosphorylation, Biophysical Society of Japan, 37, 4, pp. 155-160, (1997)