Skip Navigation LinksHome > January 2008 - Volume 40 - Issue 1 > Active and Passive Tension Interact to Promote Akt Signaling...
Medicine & Science in Sports & Exercise:
doi: 10.1249/MSS.0b013e318158e450
BASIC SCIENCES: Original Investigations

Active and Passive Tension Interact to Promote Akt Signaling with Muscle Contraction


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Purpose: The extent to which factors associated with muscle contraction activate Akt remains unclear. This study examined the influences of mechanical (active and passive tension), neural (activation frequency), and metabolic (glycogen depletion) factors on Akt activation during in situ contractions.

Methods: Muscle length was modified to produce comparable active contractile forces in three protocols, despite a twofold difference in stimulation frequency (15 vs 30 Hz); a fourth protocol used 30-Hz stimulation at optimal length to produce greater active forces. Two protocols were performed at optimal length, using 15- or 30-Hz stimulation (15 Hzopt and 30 Hzopt, respectively). Two other protocols used 30-Hz stimulation at shortened or lengthened positions (30 Hzsub and 30 Hzsupra, respectively).

Results: The principal finding was that the 30-Hzopt protocol induced significantly greater Akt phosphorylation (approximately threefold relative to control) than did the other protocols, suggesting that activation of this signaling pathway is most sensitive to active tension. This result could not be attributed to differences in glycogen depletion, stimulation frequency, or fatigue. Despite producing the lowest force-time integral, the 30-Hzsupra protocol, which had the greatest passive tension, exhibited a greater degree of Akt phosphorylation than did the 15-Hzopt and 30-Hzsub protocols. Although these differences were not significant, they suggest a possible secondary role for passive tension, which may interact with active tension in activating the Akt signaling pathway.

Conclusion: Akt activation seems more sensitive to active contractile tension than to passive tension. Activation frequency seems to play no role in the phosphorylation of Akt.

© 2008 American College of Sports Medicine


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