CaM kinase II: a protein kinase with extraordinary talents germane to insulin exocytosis

Diabetes ◽  
1999 ◽  
Vol 48 (4) ◽  
pp. 675-684 ◽  
Author(s):  
R. A. Easom
Keyword(s):  
Protein Kinase ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Insulin Exocytosis

scholarly journals Muscarinic activation of Ca2+/calmodulin-dependent protein kinase II in pancreatic islets. Temporal dissociation of kinase activation and insulin secretion

1996 ◽  
Vol 317 (1) ◽  
pp. 167-172 ◽  
Author(s):  
Eric L. BABB ◽  
Jim TARPLEY ◽  
Michael LANDT ◽  
Richard A. EASOM
Keyword(s):  
Insulin Secretion ◽  
Protein Kinase ◽  
Pancreatic Islets ◽  
Cam Kinase Ii ◽  
Muscarinic Agonist ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Kinase Activation ◽  
Protein Kinase Ii ◽  
Dependent Protein

We have demonstrated previously that glucose activates the multifunctional Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) in isolated rat pancreatic islets in a manner consistent with a role of this enzyme in the regulation of insulin secretion [Wenham, Landt and Easom (1994) J. Biol. Chem. 269, 4947–4952]. In the current study, the muscarinic agonist, carbachol, has been shown to induce the conversion of CaM kinase II into a Ca2+-independent, autonomous form indicative of its activation. Maximal activation (2-fold) was achieved by 15 s, followed by a rapid return to basal levels by 1 min. This response was primarily the result of the mobilization of Ca2+ from intracellular stores since it was not affected by a concentration (20 μM) of verapamil that completely prevented the activation of CaM kinase II by glucose. Surprisingly, carbachol added prior to, or simultaneously with, glucose attenuated nutrient activation of CaM kinase II. This effect was mimicked by cholecystokinin-8 (CCK-8) and thapsigargin, suggesting its mediation by phospholipase C and the mobilization of intracellular Ca2+. In contrast, carbachol, CCK-8 and thapsigargin markedly potentiated glucose (12 mM)-induced insulin secretion. These results suggest that CaM kinase II activation can be temporally dissociated from insulin secretion but do not exclude the potential dependence of insulin exocytosis on CaM kinase II-mediated protein phosphorylation.

scholarly journals Co-distribution of calmodulin-dependent protein kinase II and inositol trisphosphate receptors in an apical domain of gastrointestinal mucosal cells.

1996 ◽  
Vol 44 (11) ◽  
pp. 1243-1250 ◽  
Author(s):  
L M Matovcik ◽  
A R Maranto ◽  
C J Soroka ◽  
F S Gorelick ◽  
J Smith ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Pancreatic Acinar Cells ◽  
Apical Region ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein ◽  
Type 3 ◽  
Insp3 Receptor

The Type 3 inositol 1,4,5-trisphosphate (InsP3) receptor is expressed at high levels in gastrointestinal tissues. This receptor has 16 potential phosphorylation sites for calcium/calmodulin-dependent protein kinase II (CaM kinase II). To determine if the Type 3 InsP3 receptor is likely to be a physiologic substrate for CaM kinase II, localizations of the Type 3 InsP3 receptor and CaM kinase II were compared in tissues of the gastrointestinal tract. Cellular and subcellular localizations were determined by immunofluorescence microscopy in rat intestine, pancreas, and stomach, and in isolated rabbit gastric glands. Both proteins were found in the apical region of intestinal enterocytes, pancreatic acinar cells, and gastric parietal, chief, and surface mucous cells. CaM kinase II was found throughout the entire intracellular canalicular F-actin domain of parietal cells, whereas the type 3 InsP3 receptor was restricted to the neck region. Thus, in several gastrointestinal tissues the Type 3 InsP3 receptor is specifically localized to a portion of the apical cytoskeletal domain in which resides the calcium-responsive effector CaM kinase II.

Purification and characterization of calcium-calmodulin kinase II from human parathyroid glands

1991 ◽  
Vol 131 (1) ◽  
pp. 155-162 ◽  
Author(s):  
M. Kato ◽  
M. Hagiwara ◽  
Y. Nimura ◽  
S. Shionoya ◽  
H. Hidaka
Keyword(s):  
Protein Kinase ◽  
Parathyroid Adenoma ◽  
Kinase Activity ◽  
Parathyroid Glands ◽  
Protein Kinase Activity ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Major Protein Band ◽  
Dependent Protein

ABSTRACT Calmodulin has been identified in parathyroid cells and is thought to play an important role in the production or secretion of parathyroid hormone. However, a detailed investigation of calmodulinbinding proteins in parathyroid glands has not been conducted. In this study, we attempted to determine the presence of calmodulin-binding protein in human parathyroid adenoma by affinity chromatography. The eluted protein from a calmodulin-coupled Sepharose 4B column with EGTA was analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis which revealed a major protein band of Mr 50 000. A Ca2+/calmodulin-dependent protein kinase activity was detected at the protein peak using dephosphorylated casein as a substrate. The 50 kDa band was identified as calcium/calmodulin-dependent protein kinase II (CaM-kinase II) by immunoblotting. The substrate specificity, pH dependency and affinity for calmodulin of this enzyme were identical to those of CaM-kinase II from rat brain. Also, the kinase activity was sensitive to KN-62, a specific inhibitor of CaM-kinase II. In total, 0·48 mg of this kinase was purified from 3 g human parathyroid adenoma. Journal of Endocrinology (1991) 131, 155–162

Differential Regulation of Histone Deacetylase 4 by CaM Kinase II and Protein Kinase A in Response to Cardiac Beta-Adrenergic Signaling

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
Johannes Backs
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Histone Deacetylase ◽  
Medical Center ◽  
Differential Regulation ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Adrenergic Signaling ◽  
Histone Deacetylase 4 ◽  
Kinase A

Abstract 281 Johannes Backs, David Patrick, Thea Backs, Svetlana Bezprozvannaya, Xiaoxia Qi, Joseph A Hill, Eric N Olson, UT Southwestern Medical Center at Dallas, Dallas, TX Johannes Backs, 2007 Finalist and Presenting Author

Mechanisms of Isoflurane-increased Submaximum Ca2+-activatedForce in Rabbit Skinned Femoral Arterial Strips

1998 ◽  
Vol 89 (3) ◽  
pp. 731-740. ◽  
Author(s):  
Hiroshi Toda ◽  
Judy Y. Su
Keyword(s):  
Steady State ◽  
Protein Kinase ◽  
State Level ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Kinase C ◽  
Force Transducers ◽  
Dependent Protein ◽  
And Control ◽  
Dimensional Electrophoresis

Background Isoflurane enhances contraction in isolated intact arterial rings by a protein kinase C (PKC) activator and also causes contracture in skinned arterial strips. This study investigated the mechanisms of this isoflurane activation of the contractile proteins of skinned strips. Methods The skinned strips, mounted on photodiode force transducers, were prepared from rabbit femoral arteries treated with saponin. The strips were activated by 1 microM Ca2+ (buffered with 7 mM EGTA) with or without inhibitors for PKC and calmodulin-dependent protein kinase II (CaM kinase II). When force reached steady state, isoflurane was administered and changes in force were observed. Another group of the strips was frozen to assay myosin light chain phosphorylation (MLC-p) using two-dimensional electrophoresis and immunoblotting. Analysis of variance was used to compare the results from test and control groups. Probability values <0.05 were significant. Results Isoflurane (1-5%) dose dependently increased (24-81%) the Ca2+-activated force. At 1% and 5% isoflurane, MLC-p did not change either as the force increased or reached a new steady state level. However, with 3% isoflurane, MLC-p transiently decreased (29.1% and 17.1% of total MLC for 0% and 3% isoflurane, respectively). The 3% isoflurane-increased force was blocked by 10 microM bisindolymaleidmide, an inhibitor of PKC, but not by 10 microM Gö-6976, an inhibitor of Ca2+-dependent PKC, and was enhanced 50% by 0.1 mM KN-62, an inhibitor of CaM kinase II. Conclusions Isoflurane increased submaximum Ca2+-activated force in skinned femoral arterial strips by activating Ca2+-independent PKC, possibly epsilon isoezyme. The isoflurane-decreased MLC-p may be caused by activation of CaM kinase II.

scholarly journals The Inhibition Effects of Shenmai Injection on Acetylcholine-Induced Catecholamine Synthesis and Secretion by Modulating Nicotinic Acetylcholine Receptor Ion Channels in Cultured Bovine Adrenal Medullary Cells

2020 ◽  
Vol 2020 ◽  
pp. 1-8
Author(s):  
Xiting Zhang ◽  
Lin Li ◽  
Yi Wang ◽  
Haoping Mao ◽  
Lijuan Chai ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Inhibitory Effect ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Dependent Protein Kinase ◽  
Α Subunit ◽  
Shenmai Injection ◽  
Adrenal Medullary Cells ◽  
Dependent Protein ◽  
Medullary Cells

Shenmai injection (SMI) has been widely used for the treatment of cardiovascular diseases in China. Cardiovascular disorders are often related to excessive catecholamine (CA) secretion. Here, we report the effects of SMI on CA secretion and synthesis in cultured bovine adrenal medullary cells. We found that SMI significantly reduced CA secretion induced by 300 μM acetylcholine (ACh). Cotreatment with SMI (10 μL/mL) and either of the ACh receptor α-subunit inhibitors, HEX (α3) or DhβE (α4β2), did not produce any further inhibition, indicating that SMI may play a role through α3 and α4β2 channels. Furthermore, SMI reduced tyrosine hydroxylase (TH) activity induced by ACh by inhibiting the phosphorylation of TH at Ser19 and Ser40. TH is phosphorylated at Ser19 by Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) and at Ser40 by protein kinase A (PKA). KN-93 and H89, the antagonists of CaM kinase II and PKA, respectively, inhibited the ACh-induced phosphorylation at Ser19 and Ser40, and the addition of SMI did not augment the inhibitory effect. Taken together, our results show that SMI likely inhibits CA secretion by blocking TH activity at its Ser19 and Ser40 sites.

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