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Ca 2+ /Calmodulin Kinase II Translocates in a Hippocampal Slice Model of Ischemia
Author(s) -
Kolb Stephen J.,
Hudmon Andy,
Waxham M. Neal
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.64052147.x
Subject(s) - calmodulin , enzyme , protein kinase a , hippocampal formation , enzyme assay , chemistry , biochemistry , kinase , biology , microbiology and biotechnology , endocrinology
Rat hippocampal slices were exposed to conditions that simulate an ischemic insult, and the subcellular distribution and the enzymatic activity of Ca 2+ /calmodulin‐dependent protein kinase II (CaM kinase) were monitored. Semiquantitative western blots using a monoclonal antibody to the 50‐kDa α subunit showed that there was a significant redistribution of the enzyme from a supernatant to a pellet fraction after 10 min of an anoxic/aglycemic insult. No significant change in the total amount of CaM kinase enzyme was detected in the homogenates for up to 20 min of exposure to the insult. Ca 2+ /CaM‐dependent enzyme activity did not significantly change in the pellet during the 20‐min insult. Supernatant activity decreased throughout the insult. The persistence of Ca 2+ /CaM‐dependent CaM kinase activity in the pellet fraction and the detected movement of enzyme from the supernatant to the pellet indicate that redistribution may be an important mechanism in regulating the cellular location of CaM kinase activity.