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Articles in PresS, published online ahead of print May 29, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00163.2002
Submitted on April 10, 2002
Accepted on December 31, 1969
1 Physiology and Biophysics, State University of New York, Stony Brook, NY, USA
2 Neuroscience, Albert Einstein College of Medicine, Bronx, NY, USA
3 Ophthalmology and Visual Sciences, UIC College of Medicine, Chicago, IL, USA
4 Chemical Sciences, University of Catania, Catania, Italy
5 Neuroscience, Institute Pasteur, Paris, France
* To whom correspondence should be addressed. E-mail: thomas.white{at}sunysb.edu.
We have identified a novel gap junction gene that encodes a protein designated connexin31.9 (Cx31.9) by searching the human genome sequence database. Cx31.9 was most homologous to human Cx32.4, and did not cluster with either the purported alpha or beta connexin subfamilies. Expression of Cx31.9 was detected by RT-PCR in human mRNA from several tissues including cerebral cortex, heart, liver, lung, kidney, spleen and testis. A partial Cx31.9 sequence was also represented in the human EST database. Cx31.9 formed intercellular channels in both paired Xenopus oocytes and transfected N2A cells that were distinguished by their apparent low unitary conductance (12-15 pS), and their remarkable insensitivity to transjunctional voltage. In contrast, Cx31.9 channels were gated by cytoplasmic acidification or exposure to halothane like other connexins. Cx31.9 was able to form heterotypic channels with the highly voltage sensitive Xenopus Cx38 (XenCx38), providing an opportunity to study gating in heterotypic channels formed by hemichannels (connexons) composed of connexins with widely divergent properties. Thus, Cx31.9 is a novel human connexin that forms channels with unique functional properties.
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