Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways

Aims: We hypothesized that oral L-glutamine supplementations could attenuate muscle damage and oxidative stress, mediated by glutathione (GSH) in high-intensity aerobic exercise by increasing the 70-kDa heat shock proteins (HSP70) and heat shock factor 1 (HSF1). Main methods: Adult male Wistar rats...

Full description

Bibliographic Details
Main Authors: Petry, E., Cruzat, Vinicius, Heck, T., Leite, J., de Bittencourt Jr, P., Tirapegui, J.
Format: Journal Article
Published: Elsevier 2014
Subjects:
Online Access:http://hdl.handle.net/20.500.11937/5924
_version_ 1848744931968942080
author Petry, E.
Cruzat, Vinicius
Heck, T.
Leite, J.
de Bittencourt Jr, P.
Tirapegui, J.
author_facet Petry, E.
Cruzat, Vinicius
Heck, T.
Leite, J.
de Bittencourt Jr, P.
Tirapegui, J.
author_sort Petry, E.
building Curtin Institutional Repository
collection Online Access
description Aims: We hypothesized that oral L-glutamine supplementations could attenuate muscle damage and oxidative stress, mediated by glutathione (GSH) in high-intensity aerobic exercise by increasing the 70-kDa heat shock proteins (HSP70) and heat shock factor 1 (HSF1). Main methods: Adult male Wistar rats were 8-week trained (60-min/day, 5 days/week) on a treadmill. During the last 21 days, the animals were supplemented with either L-alanyl-L-glutamine dipeptide (1.5 g/kg, DIP) or a solution containing the amino acids L-glutamine (1 g/kg) and L-alanine (0.67 g/kg) in their free form(GLN + ALA) or water (controls). Key findings: Plasma from both DIP- and GLN + ALA-treated animals showed higher L-glutamine concentrations and reduced ammonium, malondialdehyde, myoglobin and creatine kinase activity. In the soleus and gastrocnemius muscle of both supplemented groups, L-glutamine and GSH contents were increased and GSH disulfide (GSSG) to GSH ratio was attenuated (p < 0.001). In the soleus muscle, cytosolic and nuclear HSP70 and HSF1 were increased by DIP supplementation. GLN + ALA group exhibited higher HSP70 (only in the nucleus) and HSF1 (cytosol and nucleus). In the gastrocnemius muscle, both supplementations were able to increase cytosolic HSP70 and cytosolic and nuclear HSF1. Significance: In trained rats, oral supplementation with DIP or GLN + ALA solution increased the expression of muscle HSP70, favored muscle L-glutamine/GSH status and improved redox defenses, which attenuate markers of muscle damage, thus improving the beneficial effects of high-intensity exercise training.
first_indexed 2025-11-14T06:09:19Z
format Journal Article
id curtin-20.500.11937-5924
institution Curtin University Malaysia
institution_category Local University
last_indexed 2025-11-14T06:09:19Z
publishDate 2014
publisher Elsevier
recordtype eprints
repository_type Digital Repository
spelling curtin-20.500.11937-59242017-09-13T16:06:54Z Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways Petry, E. Cruzat, Vinicius Heck, T. Leite, J. de Bittencourt Jr, P. Tirapegui, J. HSF1 Glutathione Oxidative stress HSP70 Exercise Aims: We hypothesized that oral L-glutamine supplementations could attenuate muscle damage and oxidative stress, mediated by glutathione (GSH) in high-intensity aerobic exercise by increasing the 70-kDa heat shock proteins (HSP70) and heat shock factor 1 (HSF1). Main methods: Adult male Wistar rats were 8-week trained (60-min/day, 5 days/week) on a treadmill. During the last 21 days, the animals were supplemented with either L-alanyl-L-glutamine dipeptide (1.5 g/kg, DIP) or a solution containing the amino acids L-glutamine (1 g/kg) and L-alanine (0.67 g/kg) in their free form(GLN + ALA) or water (controls). Key findings: Plasma from both DIP- and GLN + ALA-treated animals showed higher L-glutamine concentrations and reduced ammonium, malondialdehyde, myoglobin and creatine kinase activity. In the soleus and gastrocnemius muscle of both supplemented groups, L-glutamine and GSH contents were increased and GSH disulfide (GSSG) to GSH ratio was attenuated (p < 0.001). In the soleus muscle, cytosolic and nuclear HSP70 and HSF1 were increased by DIP supplementation. GLN + ALA group exhibited higher HSP70 (only in the nucleus) and HSF1 (cytosol and nucleus). In the gastrocnemius muscle, both supplementations were able to increase cytosolic HSP70 and cytosolic and nuclear HSF1. Significance: In trained rats, oral supplementation with DIP or GLN + ALA solution increased the expression of muscle HSP70, favored muscle L-glutamine/GSH status and improved redox defenses, which attenuate markers of muscle damage, thus improving the beneficial effects of high-intensity exercise training. 2014 Journal Article http://hdl.handle.net/20.500.11937/5924 10.1016/j.lfs.2013.11.009 Elsevier unknown
spellingShingle HSF1
Glutathione
Oxidative stress
HSP70
Exercise
Petry, E.
Cruzat, Vinicius
Heck, T.
Leite, J.
de Bittencourt Jr, P.
Tirapegui, J.
Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways
title Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways
title_full Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways
title_fullStr Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways
title_full_unstemmed Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways
title_short Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways
title_sort alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: involvement of heat shock protein pathways
topic HSF1
Glutathione
Oxidative stress
HSP70
Exercise
url http://hdl.handle.net/20.500.11937/5924