title: The mechanisms of the widespread production of phosphorylated HSP25 after fatiguing muscle stimulation.
abstract: We previously showed that a widespread heat shock protein (HSP) response to fatigue of a single hindlimb muscle was responsible for a global adaptive response to an acute localized stress. We also demonstrated that the HSP response resulted from the activation of nerve afferents from the stimulated muscle. However, we did not examine the role played by the different muscle afferents or the efferent arm of HSP response. In the present study we measured the changes in phosphorylated HSP25 (pHSP25) levels in resting hindlimb muscles and the diaphragm, kidney and brain in response to a fatiguing stimulation of one tibialis anterior muscle that was repeated in five series of experiments: (1) intact muscle innervation, (2) during the selective procaine block of conduction in group IV muscle afferents, (3) after muscle nerve transection to suppress all the sensory messages, and under pharmacological blockade of the (4) alpha-adrenergic or (5) glutamatergic neurotransmission. The data showed that: (1) the pHSP25 response in hindlimb muscles resulted from the stimulation of both group III and IV muscle afferents while the pHSP25 response in the diaphragm, kidney and brain resulted from the sole activation of the group IV fibres, and (2) the blockade of alpha-adrenergic, but not glutamatergic, neurotransmission suppressed the pHSP25 response in all explored tissues except the brain. The present study highlights the role played by the group III and IV muscle afferents in the fatigue-induced pHSP25 response and shows that the sympathetic nerve supply to the muscles and kidney represents the efferent arm of the pHSP25 activation. However, the pHSP25 changes in the brain cannot be explained by the pathways investigated here.
authors.affiliation: UMR MD2, Faculty of Medicine, Aix-Marseille University, Boulevard Pierre Dramard, 13916 cedex 20, Marseille, France. yves.jammes@univ-amu.fr
authors.forename: Yves
authors.initials: Y
authors.lastname: Jammes
authors.forename: Jean Guillaume
authors.initials: JG
authors.lastname: Steinberg
authors.forename: Marine
authors.initials: M
authors.lastname: Olivier
authors.forename: Christelle
authors.initials: C
authors.lastname: Brerro-Saby
authors.forename: Jocelyne
authors.initials: J
authors.lastname: Condo
authors.forename: Sylvie
authors.initials: S
authors.lastname: Ravailhe
authors.forename: Regis
authors.initials: R
authors.lastname: Guieu
authors.forename: Stéphane
authors.initials: S
authors.lastname: Delliaux
mesh_terms: D000818:Animals; D055551:HSP27 Heat-Shock Proteins / Q000378:metabolism*; D007668:Kidney / Q000294:innervation / Q000502:physiology; D018763:Muscle Fatigue; D018482:Muscle, Skeletal / Q000294:innervation* / Q000502:physiology*; D010766:Phosphorylation; D051381:Rats; D017207:Rats, Sprague-Dawley; D013564:Sympathetic Nervous System / Q000502:physiology; D009435:Synaptic Transmission
chemical_list: D055551:HSP27 Heat-Shock Proteins; C486114:Hspb1 protein, rat
keywords: adrenergic neurotransmission; glutamatergic neurotransmission; muscle afferents; muscle fatigue; phosphorylated HSP25