Journal of Applied Physiology
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J Appl Physiol 92: 657-664, 2002; doi:10.1152/japplphysiol.00854.2001
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Vol. 92, Issue 2, 657-664, February 2002

Role of kallikrein-kininogen system in insulin-stimulated glucose transport after muscle contractions

C. L. Dumke, J. Kim, E. B. Arias, and G. D. Cartee

Biodynamics Laboratory, Department of Kinesiology, University of Wisconsin, Madison, Wisconsin 53706

Serum proteins [molecular weight (MW) > 10,000] are essential for increased insulin-stimulated glucose transport after in vitro muscle contractions. We investigated the role of the kallikrein-kininogen system, including bradykinin, which is derived from kallikrein (MW > 10,000)-catalyzed degradation of serum protein kininogen (MW > 10,000), on this contraction effect. In vitro electrical stimulation of rat epitrochlearis muscles was performed in 1) rat serum ± kallikrein inhibitors; 2) human plasma (normal or kallikrein-deficient); 3) rat serum ± bradykinin receptor-2 inhibitors; or 4) serum-free buffer ± bradykinin. 3-O-methylglucose transport (3-MGT) was measured 3.5 h later. Serum ± kallikrein inhibitors tended (P = 0.08) to diminish postcontraction insulin-stimulated 3-MGT. Contractions in normal plasma enhanced insulin-stimulated 3-MGT vs. controls, but contractions in kallikrein-deficient plasma did not. Supplementing rat serum with bradykinin receptor antagonist HOE-140 during contraction did not alter insulin-stimulated 3-MGT. Muscles stimulated to contract in serum-free buffer plus bradykinin did not have enhanced insulin-stimulated 3-MGT. Bradykinin was insufficient for postcontraction-enhanced insulin sensitivity. However, results with kallikrein inhibitors and kallikrein-deficient plasma suggest kallikrein plays a role in this improved insulin action.

bradykinin; bradydinin receptor-2; insulin sensitivity; muscle contraction; exercise


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