β‐Adrenergic stimulation induces activation of protein kinase C and inositol 1,4,5‐trisphosphate increase in epidermis

Abstract

Epidermal keratinocytes express beta 2-adrenergic receptors on the cell membrane. The binding of the agonists to the beta 2-adrenergic receptors regulates activation of adenylate cyclase. This transmembrane signaling system has been regarded to be one of the important pathways for the functions of keratinocytes. We previously reported that beta-adrenergic stimulation induced a transient increase of intracellular Ca2+ in normal human epidermal keratinocytes. Thus we investigated the effects of epinephrine on another transmembrane signaling system, the phosphatidyl-inositol signal transduction pathway in pig epidermis. Treatment of pig pure epidermis with epinephrine resulted in a transient increase in inositol 1,4,5-trisphosphate with a peak at 30 s. Epinephrine induced translocation of protein kinase C from cytosol to the membrane fraction. The activation of protein kinase C, translocation of protein kinase C from cytosol to the membrane fraction, was confirmed using the beta-adrenergic agonist isoproterenol. Moreover, the effect of epinephrine on the activation of protein kinase C was inhibited by preincubation with propranolol, a beta-adrenergic antagonist. The increase in inositol 1,4,5-trisphosphate and translocation of protein kinase C by epinephrine are consistent with the view that beta-adrenergic stimulation induces turnover of inositol phospholipid in pig epidermis.