Conversion to Ca2+-Independent Form of Ca2+/Calmodulin Protein Kinase II in Rat Pancreatic Acini
dc.contributor.author | Duan R. D. , | en_US |
dc.contributor.author | Guo Y. J. , | en_US |
dc.contributor.author | Williams J. A. , | en_US |
dc.date.accessioned | 2006-04-10T18:19:58Z | |
dc.date.available | 2006-04-10T18:19:58Z | |
dc.date.issued | 1994-02-28 | en_US |
dc.identifier.citation | Duan R. D., , Guo Y. J., , Williams J. A., (1994/02/28)."Conversion to Ca2+-Independent Form of Ca2+/Calmodulin Protein Kinase II in Rat Pancreatic Acini." Biochemical and Biophysical Research Communications 199(1): 368-373. <http://hdl.handle.net/2027.42/31762> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-45P0Y4N-9C/2/9b4e92c49b2107769d96f8839a189c43 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31762 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8123036&dopt=citation | en_US |
dc.description.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+. | en_US |
dc.format.extent | 325466 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Conversion to Ca2+-Independent Form of Ca2+/Calmodulin Protein Kinase II in Rat Pancreatic Acini | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Physiology, University of Michigan, Ann Arbor, USA. | en_US |
dc.contributor.affiliationum | Department of Physiology, University of Michigan, Ann Arbor, USA. | en_US |
dc.contributor.affiliationum | Department of Physiology, University of Michigan, Ann Arbor, USA. | en_US |
dc.identifier.pmid | 8123036 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31762/1/0000703.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1006/bbrc.1994.1238 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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