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Functional implications of calcium permeability of the channel formed by pannexin 1
Correspondence to Natalia Prevarskaya: natacha.prevarskaya{at}univ-lille1.fr
Although human pannexins (PanX) are homologous to gap junction molecules, their physiological function in vertebrates remains poorly understood. Our results demonstrate that overexpression of PanX1 results in the formation of Ca2+-permeable gap junction channels between adjacent cells, thus, allowing direct intercellular Ca2+ diffusion and facilitating intercellular Ca2+ wave propagation. More intriguingly, our results strongly suggest that PanX1 may also form Ca2+-permeable channels in the endoplasmic reticulum (ER). These channels contribute to the ER Ca2+ leak and thereby affect the ER Ca2+ load. Because leakage remains the most enigmatic of those processes involved in intracellular calcium homeostasis, and the molecular nature of the leak channels is as yet unknown, the results of this work provide new insight into calcium signaling mechanisms. These results imply that for vertebrates, a new protein family, referred to as pannexins, may not simply duplicate the connexin function but may also provide additional pathways for intra- and intercellular calcium signaling and homeostasis.
Y.V. Panchin's present addresses are Institute for Information Transmission Problems, Russian Academy of Sciences, Moscow 101447, Russia; and the A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia.
D.V. Ivanov's present address is Dept. of Ophthalmology, Bascom Palmer Eye Institute, University of Miami Miller School of Medicine, Miami, FL 33136.
D. Gordienko's present address is Dept. of Basic Medical Sciences, St. George's University of London, London SW17 0RE, England, UK.
A.V. Baranova's present addresses are Dept. of Molecular and Microbiology, Georges Mason University, Manassas, VA 20110; and the Russian Academy of Medical Science, 123098 Moscow, Russia.
Abbreviations used in this paper: BODIPY, boron dipyrromethene difluoride; HEK, human embryonic kidney; ODN, oligodeoxynucleotide; RyR, ryanodine receptor; SERCA, sarcoplasmic/ER Ca2+-ATPase; TG, thapsigargin.
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