Functional characterization of a naturally occurring Cx50 truncation.

Purpose: Lens connexins undergo proteolytic cleavage of their C termini during fiber maturation. Although the functional significance of this is unknown, cleavage has been correlated with changes in channel-gating properties. This study evaluates the functional consequences of this endogenous truncation by characterizing the properties of a C-terminal truncated Cx50 protein.

Cloning and functional expression of invertebrate connexins from Halocynthia pyriformis.

Unlike many other ion channels, unrelated gene families encode gap junctions in different animal phyla. Connexin and pannexin genes are found in deuterostomes, while protostomal species use innexin genes. Connexins are often described as vertebrate genes, despite the existence of invertebrate deuterostomes.

Biophysical characterization of zebrafish connexin35 hemichannels.

A subset of connexins can form unopposed hemichannels in expression systems, providing an opportunity for comparison of hemichannel gating properties with those of intact gap junction channels. Zebrafish connexin35 (Cx35) is a member of the Cx35/Cx36 subgroup of connexins highly expressed in the retina and brain. In the present study, we have shown that Cx35 expression in Xenopus oocytes and N2A cells produced large outward whole cell currents on cell depolarization.

Altered gating properties of functional Cx26 mutants associated with recessive non-syndromic hearing loss.

Connexins (Cx) form gap junctions that allow the exchange of small metabolites and ions. In the inner ear, Cx26 is the major gap junction protein and mutations in the Cx26-encoding gene, GJB2, are the most frequent cause of autosomal recessive non-syndromic hearing loss (DFNB1). We have functionally analyzed five Cx26 mutations associated with DFNB1, comprising the following single amino-acid substitutions: T8M, R143W, V153I, N206S and L214P.

Connexin 48.5 is required for normal cardiovascular function and lens development in zebrafish embryos.

Gap junctions are composed of connexin (Cx) proteins and mediate intercellular communication required for many developmental and physiological processes. Here we describe the isolation and characterization of Cx48.5, a zebrafish connexin with the highest sequence identity to mammalian Cx46.

Molecular cloning, functional analysis, and RNA expression analysis of connexin45.6: a zebrafish cardiovascular connexin.

In the vertebrate cardiovascular system, gap junctions function in intercellular communication essential for both the coordinated propagation of the heartbeat and the control of vasomotor responses in the vascular system. Connexins, the protein subunits of gap junctions, are coded by a multigene family. In this study, a connexin gene (zfCx45.