Decrock et al. Different connexins may exhibit differing specificities for solutes. Thus, addition of phosphate to adenosine appears to shift its relative permeability from channels formed by Cx32 to channels formed by Cx This may have functional consequence because the energy status of a cell could be controlled via connexin expression and channel formation. For this reason, deletion or mutation of the various connexin isoforms produces distinctive phenotypes and pathologies.
Cx40 mutations are principally linked to atrial fibrillation. Mutations in Cx37 have not yet been described, but polymorphisms in the Cx37 gene have been implicated in the development of arterial disease.
As of this edit , this article uses content from "1. All relevant terms must be followed. From Wikipedia, the free encyclopedia. Connexin An open gap junction, composed of six identical connexin proteins. Each of these six units is a single polypeptide which passes the membrane four times referred to as four-pass transmembrane proteins.
Kaiser; Monty Krieger; Mathew P. Scott; S. Lawrence Zipursky; James Darnell Molecular Cell Biology 5th ed. New York: W. Freeman and Company. Novartis Found.
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Reporting intracellular and plasma membrane calcium environments". Cell Commun.
Cell Sci. Cell Biol. Cell Commun Signal. J Neurosci Res. Life Sci. Acta Neuropathol. June Connexins: A Guide 1st ed. Springer-Verlag Gmbh. Membrane transport protein : ion channels TC 1A. Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3. Amiloride-sensitive cation channel 1 2 3 4. Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family. Ligand-gated Light-gated Voltage-gated Stretch-activated.
Special Issue "Interplay of Connexins and Pannexins in Tissue Function and Disease"
Proteins of epithelium. Authority control TH : H1. Categories : Protein families Membrane proteins Transmembrane proteins Transmembrane transporters Transport proteins Integral membrane proteins. Namespaces Article Talk. Views Read Edit View history.
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Normally expressed in astrocytes, also detected in most of the human astrocytomas and in the astroglial component of glioneuronal tumors. The most defined mechanism for such regulation is the closure of gap junction channels in response to acidification of the intracellular space, that is, pH gating or chemical gating. In the best studied case, that of Cx43, chemical gating involves interactions between a specific segment of the cytoplasmic carboxyl-terminal domain with a specific segment of the cytoplasmic loop domain.
These interactions have been characterized at the molecular and structural levels. Additionally, there is evidence that interaction of cytoplasmic aminosulfonates and peptide reagents can also affect the gating mechanisms controlled by these inter-domain interactions. Chemical gating of connexin channels.
N2 - The physiology of gap junctions is regulated by changes in the microenvironment of the cell. AB - The physiology of gap junctions is regulated by changes in the microenvironment of the cell.
Connexins: substrates and regulators of autophagy | BMC Molecular and Cell Biology | Full Text
Abstract The physiology of gap junctions is regulated by changes in the microenvironment of the cell. Fingerprint Connexins. Gap Junctions.
Intracellular Space. Cellular Microenvironment. Connexin
Related Connexins: A Guide
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