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Diabetes 53:21-24, 2004
© 2004 by the American Diabetes Association, Inc.

Exercise-Induced Protein Kinase C Isoform-Specific Activation in Human Skeletal Muscle

Sebastio Perrini1, Jan Henriksson2, Juleen R. Zierath1, and Ulrika Widegren1

1 Department of Surgical Sciences, Section for Integrative Physiology, Karolinska Institutet, Stockholm, Sweden
2 Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden

We determined whether protein kinase C (PKC) isoforms are redistributed and phosphorylated in response to acute exercise in skeletal muscle. Muscle biopsies were obtained from six healthy subjects (four women, two men; age 25 ± 1 years) before, during, and after 60 min of one-leg cycle ergometry at ~70% VO2peak. Exercise for 30 and 60 min was associated with a three- and fourfold increase in PKC-{zeta}/{lambda} abundance and a four- and threefold increase in phosphorylation, respectively, in total membranes (P < 0.05) and a decrease in PKC-{zeta}/{lambda} phosphorylation in cytosolic fractions. During exercise recovery, PKC-{zeta}/{lambda} abundance and phosphorylation remained elevated. PKC-{zeta}/{lambda} abundance and phosphorylation were increased in nonexercised muscle upon cessation of exercise, indicating a systemic response may contribute to changes in PKC abundance and phosphorylation. Exercise did not change PKC-{delta} or -{varepsilon} abundance or phosphorylation in either the cytosolic or total membrane fraction. In conclusion, exercise is associated with an isoform-specific effect on PKC. PKC-{zeta}/{lambda} are candidate PKC isoforms that may play a role in the regulation of exercise-related changes in metabolic and gene-regulatory responses.

Address correspondence and reprint requests to Juleen R. Zierath, PhD, Karolinska Institutet, Department of Surgical Sciences, Section of Integrative Physiology, S-171 77 Stockholm, Sweden. E-mail: juleen.zierath{at}fyfa.ki.se


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Diabetes Diabetes Care Clinical Diabetes Diabetes Spectrum
Copyright © 2004 by the American Diabetes Association.