Expression and activity of protein kinase D/protein kinase C mu in myocardium: evidence for alpha1-adrenergic receptor- and protein kinase C-mediated regulation.
作者： Robert S Haworth , Martin W Goss , Enrique Rozengurt , Metin Avkiran
关键词: Biology 、 Autophosphorylation 、 Endocrinology 、 MAP kinase kinase kinase 、 Protein kinase C 、 Internal medicine 、 Molecular biology 、 Receptor 、 Kinase 、 Signal transduction 、 Mitogen-activated protein kinase kinase 、 Bisindolylmaleimide
摘要: Protein kinase D (PKD), which is also known as protein C (PKC) mu, a novel serine/threonine that can be activated in parallel with or downstream of PKC various cell types, but its expression and regulation myocardium have not been characterized. In the present study, two proteins 110 115 kDa were detected rat ventricular using antibodies directed at extreme N- C-terminus PKD. Both highly expressed fetal heart showed developmental decline abundance. Fractionation studies PKD was distributed between myocyte non-myocyte fractions neonatal heart, found predominantly fraction adult heart. cultured myocytes, an vitro assay revealed increased autophosphorylation (EC50 2.8 nM) response to phorbol-12-myristate-13-acetate (PMA). Exposure norepinephrine induced dose-dependent increase 0.6 microM). Pretreatment alpha1-adrenergic receptor (AR) antagonist prazosin blocked norepinephrine-induced autophosphorylation, while beta1-AR atenolol had no effect, indicating activation by occurred via alpha1-AR. Involvement alpha1-AR confirmed exposure myocytes agonist phenylephrine, similar profile The effects both stimulation PMA on mediated PKC, since these could attenuated pretreatment inhibitor bisindolylmaleimide. These data show myocardium, where subject control, activity regulated through alpha1-AR- PKC-mediated pathways.
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