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Conversion to Ca2+-independent form of Ca2+/calmodulin protein kinase II in rat pancreatic acini

Duan, Rui-Dong LU ; Guo, Yi-Jun and Williams, John A (1994) In Biochemical and Biophysical Research Communications 199(1). p.368-373
Abstract
CCK rapidly converted Ca2+/calmodulin kinase II (CaMK II) to a Ca(2+)-independent form with peak action at 30 sec followed by decline to the basal level at 10 min. The threshold concentration of CCK for this action was 30 pM and maximum effect occurred at 1 nM, which induced a 6-10-fold increase. Bombesin and carbachol similarly induced CaMK II autonomous activity, whereas secretin and JMV 180 did not. lonomycin induced a more stable elevation of CaMK II autonomous activity and the intracellular Ca2+ chelator, BAPTA/AM, blocked the effect of CCK. In conclusion, pancreatic CaMK II is rapidly activated by a large increase in [Ca2+]i generated by either stimulation of phosphatidylinositol pathway or by an influx of extracellular Ca2+.
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author
; and
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
199
issue
1
pages
6 pages
publisher
Elsevier
external identifiers
  • scopus:0028179179
ISSN
1090-2104
DOI
10.1006/bbrc.1994.1238
language
English
LU publication?
no
id
5309dddf-ab10-4918-98f2-65577e56b834
date added to LUP
2019-02-03 10:09:25
date last changed
2021-01-03 10:11:53
@article{5309dddf-ab10-4918-98f2-65577e56b834,
  abstract     = {{CCK rapidly converted Ca2+/calmodulin kinase II (CaMK II) to a Ca(2+)-independent form with peak action at 30 sec followed by decline to the basal level at 10 min. The threshold concentration of CCK for this action was 30 pM and maximum effect occurred at 1 nM, which induced a 6-10-fold increase. Bombesin and carbachol similarly induced CaMK II autonomous activity, whereas secretin and JMV 180 did not. lonomycin induced a more stable elevation of CaMK II autonomous activity and the intracellular Ca2+ chelator, BAPTA/AM, blocked the effect of CCK. In conclusion, pancreatic CaMK II is rapidly activated by a large increase in [Ca2+]i generated by either stimulation of phosphatidylinositol pathway or by an influx of extracellular Ca2+.}},
  author       = {{Duan, Rui-Dong and Guo, Yi-Jun and Williams, John A}},
  issn         = {{1090-2104}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{368--373}},
  publisher    = {{Elsevier}},
  series       = {{Biochemical and Biophysical Research Communications}},
  title        = {{Conversion to Ca2+-independent form of Ca2+/calmodulin protein kinase II in rat pancreatic acini}},
  url          = {{http://dx.doi.org/10.1006/bbrc.1994.1238}},
  doi          = {{10.1006/bbrc.1994.1238}},
  volume       = {{199}},
  year         = {{1994}},
}