Insulin stimulates glucose transport into muscle cells and adipocytes via a process that involves the translocation of GLUT4 proteins from intracellular stores to the cell membrane. The pathway by which this translocation takes place has not been fully elucidated. The purpose of this study was to determine the effect of the calciumdependent calmodulin protein kinase II (CAMKII) inhibitor KN-62 on insulin stimulated 3-0-methylglucose transport in isolated rat epitrochlearis muscles. The primary finding of this investigation was that KN-62 decreased insulin stimulated glucose transport by -35%. KN-04, a structural analogue of KN-62, did not affect insulin stimulated glucose transport. Additional experiments showed that the L-type calcium (Ca 2+) channel inhibitor nifedipine inhibited glucose transport to a similar extent as KN-62 (-29%). Furthermore, no additive inhibitory effect was seen when KN-62 and nifedipine were used in combination. The results of this investigation suggest that CAMKII has a critical role in insulin stimulated glucose transport, and this role may be dependent upon L-type Cat- channel activation. / School of Physical Education
| Identifer | oai:union.ndltd.org:BSU/oai:cardinalscholar.bsu.edu:handle/187384 |
| Date | January 2002 |
| Creators | Fick, Christopher A. |
| Contributors | Craig, Bruce W. |
| Source Sets | Ball State University |
| Detected Language | English |
| Format | v, 61 leaves : ill. ; 28 cm. |
| Source | Virtual Press |
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