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

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

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)657-664
Number of pages8
JournalJournal of Applied Physiology
Volume92
Issue number2
DOIs
StatePublished - 2002

Keywords

  • Bradydinin receptor-2
  • Bradykinin
  • Exercise
  • Insulin sensitivity
  • Muscle contraction

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