GLUTAMINE AND HEAT SHOCK PROTEINS IN EXERCISE

There is substantial evidence that glutamine is important for heat shock protein (HSP) generation in both in vitro and in vivo studies, for example, to help prevent atrophy of intestinal epithelial cells via HSP70 (Wischmeyer, 2002; Agostini and Biolo, 2009; Xue et al., 2011). Fehrenbach and Neiss (1998) suggested a protective effect of HSPs in leucocytes in athletes after endurance exercise. More recently, it was demonstrated first that glutamine supplementation decreased exercise-induced intestinal permeability and reduced nuclear factor kappa B activity in peripheral blood mononuclear cells, and second, that both these anti-inflammatory actions of glutamine could be mediated through activation of HSP70 and the heat shock response (Zuhl et al., 2014).

The circulating concentration of HSP72 increases after exercise. Furthermore, extracellular HSP72 stimulates cytokine activity, the “chaperokine” capacity of HSP72 (Asea et al., 2005). As it is known that glutaminase is present on the secretory granules of human neutrophils (Castell et al., 2004), it may be possible that glutamine effects on the heat shock response might induce changes in neutrophil function. Indeed, some studies have shown that HSP is responsible for facilitating neutrophil activity (Ortega et al., 2006; Hinchado et al., 2012).

 
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