English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The effect of phorbol 12-myristate 13-acetate (PMA) on hepatocyte alpha 1-adrenergic receptors was determined by [3H]prazosin binding to plasma membranes from control and PMA-treated hepatocytes. Membranes from hepatocytes incubated with PMA (1 microgram/ml) for 1 h exhibited a 40% decrease in alpha 1-adrenergic receptors (481 +/- 10 fmol/mg of protein; mean +/- S.E.M. for three separate experiments) relative to vehicle-treated (dimethylformamide) hepatocytes (802 +/- 91 fmol/mg of protein; n = 3), with no significant effect on the KD. The PMA-induced decrease in alpha 1-adrenergic receptors was maximal by 30 min and half-maximal inhibition of [3H]prazosin binding occurred with a PMA concentration of approx. 15 ng/ml. Pretreatment of hepatocytes with staurosporine (5 microM) blocked the effect of PMA, and 4 beta-phorbol 13-monoacetate was ineffective, suggesting the involvement of protein kinase C (PKC). Treatment of hepatocytes with primaquine (300 microM) for 15 min decreased hepatocyte plasma membrane alpha 1-adrenergic receptors by 34.0 +/- 2.4% (mean +/- S.E.M. of three experiments). Removal of primaquine allowed essentially complete recovery (98 +/- 4%; mean +/- S.E.M. for five separate experiments) of plasma membrane [3H]prazosin binding within 20 min, suggesting that the alpha 1-adrenergic receptor undergoes endocytotic recycling. Addition of PMA (1 microgram/ml) to hepatocytes immediately after removal of primaquine, completely inhibited the increase in plasma membrane alpha 1-adrenergic receptors relative to control cells, but had no effect on hepatocytes whose cell surface alpha 1-receptors remaining after primaquine treatment had been inactivated by alkylation. These observations suggested that activation of PKC may facilitate the internalization of the alpha 1-adrenergic receptor in hepatocytes.

Regulation of hepatocyte plasma membrane α1-adrenergic receptors by 4β-phorbol 12-myristate 13-acetate