@article{APS6808,
author = {Zong-Jie Cui},
title = {Muscarinic stimulation of calcium/calmodulin-dependent protein kinase II in isolated rat pancreatic acini},
journal = {Acta Pharmacologica Sinica},
volume = {18},
number = {3},
year = {2016},
keywords = {},
abstract = {AIM: To study whether M3 receptor occupation would lead to activation of
calcium/calmodulin-dependent protein kinase II (CaM kinase II).
METHODS: In this study, we isolated rat pancreatic acini by collagenase
digestion; measured the Ca2+/calmodulin-independent activity of
autophosphorylated form of the CaM kinase II both before and after stimulation of
the acini with muscarinic secretagogue bethanechol (Bet).
RESULTS: Bet stimulated the activation of, or generation of Ca(2+)-independent
activity of, this kinase, in a concentration (0.0001-1 mmol.L-1) and time (5-300
s)-dependent manner; with Bet of 100 mumol.L-1, Ca(2+)-independent activity
increased from an unstimulated level of 4.5 +/- 0.3 (n = 4) to 8.9 +/- 1.3 (n =
4, P < 0.05) at 5 s. Another Ca2+ mobilizing secretagogue cholecystokinin (CCK)
also activated the kinase; at 1 mumol.L-1, CCK increased Ca(2+)-independent
kinase activity to 12.9 +/- 0.5 (n = 6, P < 0.05). Vasoactive intestinal peptide
(VIP) at 1 mumol.L-1 did not produce significant Ca(2+)-independent kinase
activity (from control 3.90 +/- 0.28 to 4.53 +/- 0.47, n = 6, P > 0.05). Atropine
completely blocked Bet activation of the kinase.
CONCLUSION: CaM kinase II plays a pivotal role in digestive enzyme secretion,
especially during the initial phase of amylase secretion.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/6808}
}