Involvement of bradykinin in acute exercise-induced increase of glucose uptake and GLUT-4 translocation in skeletal muscle: Studies in normal and diabetic humans and rats

Taguchi, Tetsuya; Kishikawa, Hiroki; Motoshima, Hiroyuki; Sakai, Kenichiro; Nishiyama, Tadao; Yoshizato, Kazuaki; Shirakami, Atsuhisa; Toyonaga, Tetsushi; Shirotani, Tetsuya; Araki, Eiichi; Shichiri, Motoaki

doi:10.1053/meta.2000.6755

Cited by 54 publications

(61 citation statements)

References 48 publications

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“…1) The kallikrein-kininogen system is activated by muscle contractile activity (2,27,35,36). 2) There is abundant evidence that activation of this system can enhance insulin sensitivity (6, 10, 15, Fig.…”

Section: Discussionmentioning

confidence: 99%

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

Dumke

Kim

Arias

et al. 2002

Journal of Applied Physiology

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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.

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Section: Discussionmentioning

confidence: 99%

“…Bradykinin is released by contracting skeletal muscle (2,27,35,36). At least under some conditions, bradykinin may play a role in enhanced insulin sensitivity (6,10,15,17,39).…”

mentioning

confidence: 99%

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

Dumke

Kim

Arias

et al. 2002

Journal of Applied Physiology

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“…[84][85][86][87][88] The provision of kinins accelerates GLUT4 translocation to the sarcolemma and increases glucose transport activity by an insulin-, protein kinase C-, and phosphatidyl-inositol-3-kinase-independent pathway. 81,82 The action of kinins on glucose transport is linked in part to Ca 2+ -influx across the sarcolemma and in part to Ca 2+ -release from intracellular stores (figure 4). 78 This mechanism mimics contraction-dependent glucose transport activity in the slow-twitch red fibre, which is a Ca 2+ -dependent process.…”

Section: O P Y R I G H T J R a A S L I M I T E D R E P R O D U C T mentioning

confidence: 99%

Review: Angiotensin-converting enzyme in skeletal muscle: sentinel of blood pressure control and glucose homeostasis

Dietze¹,

Henriksen

2008

J Renin Angiotensin Aldosterone Syst

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Recent evidence suggests a coordinated regulation by the local renin-angiotensin system (RAS) and tissue kallikrein-kinin system (TKKS) of blood flow and substrate supply in oxidative red myofibres of skeletal muscle tissue during endurance exercise.The performance of these myofibres is dependent on the increased oxidation of substrates facilitated by augmenting nutritive blood flow and glucose uptake. Humoral factors released by the contracting fibres, such as adenosine and kinins, are suggested to be responsible for this metabolic adjustment.The considerable drain of blood volume and the enormous consumption of glucose during endurance exercise require a control mechanism for the maintenance of blood pressure (BP) and glucose homeostasis. This is achieved by the sympathetic nervous system and its subordinate RAS, which is located in the nutritive vessels and parenchyma of the red myofibres. The angiotensin-converting enzyme (ACE) is the primary enzyme responsible for kinin degradation during exercise, underscoring the important interrelationship between the RAS and the TKKS in the critical role of kinins in the multifactorial regulation of muscle bioenergetics and glucose and BP homeostasis. Importantly, overactivity of the ACE, as occurs in individuals displaying risk factors such as overweight, causes exaggerated BP response and reduced glucose disposal. If they persist over years, compensatory responses to this ACE overactivity, such as hypersecretion of insulin and compliance of the vessel walls, will inevitably be exhausted, leading ultimately to the manifestation of type 2 diabetes and hypertension. This concept also provides a unifying explanation for the beneficial effects of ACE-inhibitors and Angiotensin II receptor antagonists in the treatment of hypertension and insulin resistance.Need for control of blood pressure and glucose homeostasis during endurance exercise performance The regulation of muscle bioenergetics during exercise has been studied for more than 100 years.

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“…Actually, when mediated by the B 2 R activation, bradykinin increases the translocation of GLUT4 for the membrane during exercise via increase of tyrosine kinase activity induced by insulin in its receptors (62) . Such fact leads to a transient increase of inositol 1,4,5-triphosphate involved in the excitementcontraction joining mechanism via increase of cytoplasmatic calcium (63) .…”

Section: -9/+9 Polymorphism Of the Bradykinin β β β β β 2 Receptor (Bmentioning

confidence: 99%

Polimorfismos genéticos determinantes da performance física em atletas de elite

Dias

Pereira²,

Negräo³

2007

Rev Bras Med Esporte

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Este artigo direciona-se à revisão de publicações sobre os "genes candidatos" e sua relação com os fenótipos de performance física humana em atletas de elite. Nosso objetivo é trazer ao conhecimento do leitor informações atualizadas sobre marcadores e variantes genéticas que podem levar certos indivíduos a sobressair-se em modalidades esportivas específicas. Além disso, serão descritos os mecanismos pelos quais um gene pode contribuir para a performance física, detalhando em cada momento as propriedades celulares, fisiológicas e moleculares do sistema em questão. Por esse motivo, limitamos nossa discussão a um número pequeno de variantes genéticas: polimorfismos R577X do gene da alfa-actinina 3 (ACTN3), C34T do gene da AMP deaminase (AMPD1), I/D da enzima conversora de angiotensina (ECA), -9/+9 do receptor beta2 de bradicinina (BDKRB2) e 985+185/1170 do gene da enzima creatina quinase M (CK-M). Esperamos com este artigo informar e sensibilizar o leitor para o fato de que a identificação de talentos e a otimização do potencial individual do atleta, com conseqüente sucesso no esporte, estão diretamente associados a variantes genéticas.

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Involvement of bradykinin in acute exercise-induced increase of glucose uptake and GLUT-4 translocation in skeletal muscle: Studies in normal and diabetic humans and rats

Cited by 54 publications

References 48 publications

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

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

Review: Angiotensin-converting enzyme in skeletal muscle: sentinel of blood pressure control and glucose homeostasis

Polimorfismos genéticos determinantes da performance física em atletas de elite

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