The I1-imidazoline receptor in PC12 pheochromocytoma cells activates protein kinases C, extracellular signal-regulated kinase (ERK) and c-jun N-terminal kinase (JNK)
作者： Lincoln Edwards , Daniel Fishman , Peleg Horowitz , Nicole Bourbon , Mark Kester
DOI: 10.1046/J.1471-4159.2001.00632.X
关键词:
摘要: We sought to further elucidate signal transduction pathways for the I1-imidazoline receptor in PC12 cells by testing involvement of protein kinase C (PKC) isoforms (βII, e, ζ), and mitogen-activated kinases (MAPK) ERK JNK. Stimulation with moxonidine increased enzymatic activity classical βII isoform membranes about 75% redistributed atypical into (40% increase membrane-bound activity), but novel PKC was unaffected. Moxonidine clonidine also greater than two-fold proportion ERK-1 ERK-2 phosphorylated active form. In addition, JNK exposure moxonidine. Activation followed similar time courses peaks at 90 min. The action on activation blocked I1-receptor antagonist efaroxan D609, an inhibitor phosphatidylcholine-selective phospholipase C (PC-PLC), previously implicated as initial event signaling. Inhibition or depletion Two-day treatment I1/α2-agonist cell number up 50% a dose related manner. These data suggest that JNK, along PKC, are signaling components pathway, this may play role growth.
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