Gap junctional intercellular communication is thought to play a key role in development and may also be involved in epilepsy (Aronica et al., 2001). Connexin43 forms gap-junctional channels and regulates the permeability of these gap junctions to small organic molecules. Permeability of connexin43 is known to be regulated by phosphorylation at er368 by protein kinase C (Yogo et al., 2002; Bao et al., 2004a). Phosphorylation of Ser368 by PKC induces a conformational change of connexin43 that results in a decrease in gap junction permeability (Bao et al., 2004b).1) Aronica E, Gorter JA, Jansen GH, Leenstra S, Yankaya B, Troost D (2001) Expression of connexin 43 and connexin 32 gap-junction proteins in epilepsy-associated brain tumors and in the perilesional epileptic cortex. Acta Neuropathol (Berl) 101:449-459. More
Peptide corresponding to amino acid residues from the C-terminal region of rat connexin43.
WB
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Western blot of rat cerebellar lysate showing specific immunolabeling of the ~43k connexin43 protein.
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