Abstract
The capsaicin receptor, TRPV1, is a sensory neuron-specific ion channel that serves as a polymodal detector of pain-producing chemical and physical stimuli. It has been reported that inflammatory mediators such as ATP and bradykinin phosphorylate TRPV1 in a PKC dependent pathway. Two serine residues in the cytoplasmic domains of TRPV1, Ser502 and Ser800 were found to be involved in phosphorylation of TRPV1 by PKC. We made an antibody gainst phosphorylated Ser800 of TRPV1 because Ser800 is known to function as a substrate only for PKC-dependent phosphorylation. We examined the amount of phosphorylated TRPV1 upon treatment with PMA using the antibody in Western blot analysis and immunostaining. We detected the increase in the amount of phosphorylated TRPV1 upon PMA stimulation in both HEK293 cells expressing TRPV1 and cultured rat DRG neurons. [Jpn J Physiol 54 Suppl:S169 (2004)]
