Pre‐existent Hsp72 contributes to glutamine‐induced hepatic <i>hsp72</i> gene activation during heat shock recovery period in rat

Wang, Shu-Jung; Chen, Hsiang-Wen; Yang, Rei‐Cheng

doi:10.1002/mnfr.201100555

Cited by 3 publications

(2 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the contrary, Gln associated to HSP27 induction, an eff ect similar to that previously reported in rats with d-galactosamine/lipopopysaccharide-induced liver injury receiving biclycol [6]; this result support s role of HSP27 in Gln-mediated hepatoprotection. Other authors have also observed a modulating eff ect of Gln on heat shock proteins in rat livers submitted to intestinal ischemia-reperfusion and during the heat shock recovery period [31,32].…”

Section: Discussionmentioning

confidence: 86%

Glutamine Modulates Heat Shock Proteins, Endoplasmic Reticulum Stress and Cell Death in Rats with Thioacetamide-Induced Severe Acute Liver Failure

G Schemitt*,

Rosa,

S Fillmann

et al. 2024

J Biomed Res Environ Sci

View full text Add to dashboard Cite

Severe Acute Liver Failure (SALF) is characterized by sudden dysfunction of liver cells in previously healthy persons without known underlying liver disease. Effective therapeutic approaches are necessary in an attempt to minimize the damage resulting from liver failure. Glutamine is considered to be an amino acid that plays many essential metabolic functions. This study was designed to evaluate the action of glutamine in protecting against cellular disturbances resulting from Thioacetamide (TAA)-induced SALF in rats. Two doses of thioacetamide (400 mg/kg) and 3 doses of glutamine (25 mg/kg) (ip) were administered. The experiment lasted 48 hours. Glutamine reduced blood levels of AST and ALT in TAA-treated rats. Histological evaluation indicated that glutamine acted in tissue protection by reducing the inflammatory infiltrate, ballooning and centrilobular necrosis induced by SALF, consequently restoring the hepatic parenchyma. Glutamine increased total protein levels and decreased carbonylated protein levels in the liver of SALF animals. Glutamine also acted by modulating HSF-1 and heat shock proteins expression, as well as by decreasing the expression of proteins involved in endoplasmic reticulum stress (GRP78, ATF6 and CHOP), and modifying the expression of apoptosis-related (Bcl -2, Bax and caspase 3) and autophagy-related (mTOR, Beclin1 and LC3α/β) proteins. These effects related to changes in PI3K, Akt and FOXO3a expression. Data obtained support a potential hepatoprotective role of glutamine in SALF.

show abstract

Section: Discussionmentioning

confidence: 86%

Glutamine Modulates Heat Shock Proteins, Endoplasmic Reticulum Stress and Cell Death in Rats with Thioacetamide-Induced Severe Acute Liver Failure

G Schemitt*,

Rosa,

S Fillmann

et al. 2024

J Biomed Res Environ Sci

View full text Add to dashboard Cite

show abstract

“…Although glutamine is able to slightly increase HSF1 trimerization in non-stressful situations [49,56], glutamine acts physiologically as an enhancer of the HS response, which means that a pre-existent (e.g., exercise, heat stress, elevated sympathetic nervous system tonus) stress-induced HSF1 activation must be present for glutamine to fully enhance HSF1 activation and transcribing activity. In addition, iHSP70 per se participates in glutamine-induced HS response [252].…”

Section: Glutamine Metabolism and Its Importance For The Heat Shock Rmentioning

confidence: 99%

Physiological regulation of the heat shock response by glutamine: implications for chronic low-grade inflammatory diseases in age-related conditions

Leite

Cruzat

Krause

et al. 2016

Nutrire

View full text Add to dashboard Cite

Aging is an intricate process modulated by different molecular and cellular events, such as genome instability, epigenetic and transcriptional changes, molecular damage, cell death and senescence, inflammation, and metabolic dysfunction. Particularly, protein quality control (chaperone systems) tends to be negatively affected by aging, thus leading to cellular senescence in metabolic tissues and, as a consequence, to the increasing dissemination of inflammation throughout the body. The heat shock (HS) response and its associated expression of the 70 kDa family of heat shock proteins (HSP70), which are anti-inflammatory molecular chaperones, are found to be markedly decreased during muscle inactivity and aging, while evidence supports the loss of HSP70 as a key mechanism which may drive muscle atrophy, contractile dysfunction, and reduced regenerative capacity. In addition, abnormal stress response is linked with higher incidence of neurodegenerative diseases as well as low-grade inflammatory diseases that are associated with physical inactivity and obesity. Therefore, strategies to increase or, at least, to maintain the levels of HSP70, and its accompanying HS response to stress, are key to reduce biological cell dysfunctions that occur in aging. In this sense, physical exercise is of note as it is the most powerful inducer of the HS response, comparable only to heat stress and fever-like conditions. On the other hand, the amino acid L-glutamine, whose production within the skeletal muscle and liberation into the blood stream is dependent on muscle activity, is a potentializer of HSP70 expression and HS response, particularly via its entering in hexosamine biosynthetic pathway (HBP). Herein, we discuss the collaborative role of glutamine (and its donors/precursors) and physical exercise (mostly responsible for glutamine release into the circulation) as potential tools to increase HSP70 expression and the HS response in the elderly.

show abstract

Prophylactic Inhalation of L-Alanyl-L-Glutamine Enhances Heat Shock Protein 72 and Attenuates Endotoxin-Induced Lung Injury in Rats

Ms²,

Lj³

et al. 2015

Physiol Res

View full text Add to dashboard Cite

Studies have demonstrated that heat shock protein 70 (HSP70) plays an important role in the protection of stressed organisms. The development of strategies for enhancing HSPs expression may provide novel means of minimizing inflammatory lung conditions, such as acute lung injury. This study aimed to examine the effect of L-alanyl-L-glutamine (GLN) inhalation in enhancing pulmonary HSP72 (inducible HSP70) expression and attenuating lung damage in a model of acute lung injury induced by Lipopolysaccharide (LPS) inhalation. The experimental rats were randomly assigned to one of four experimental groups: (1) NS: saline inhalation; (2) NS-LPS: pretreatment by saline inhalation 12 h before LPS inhalation; (3) GLN: glutamine inhalation; (4) GLN-LPS: pretreatment by glutamine inhalation 12 h before LPS inhalation. The results show that GLN compared with saline administration, led to significant increase in lung HSP72 both in non LPS-treated rats and LPS-treated rats. In LPS-treated rats, pretreatment by GLN inhalation produced less lung injury as evidenced by the decrease in lung injury score and dramatic decrease in lactate dehydrogenase (LDH) activity and polymorphonuclear leukocyte cell differentiation counts (PMN %) in the bronchoalveolar lavage fluid. The study indicates that prophylactic glutamine inhalation associated with the enhancement of HSP72 synthesis attenuates tissue damage in experimental lung injury.

show abstract

Pre‐existent Hsp72 contributes to glutamine‐induced hepatic hsp72 gene activation during heat shock recovery period in rat

Abstract: Glutamine switched on alteration pathway in inducing hsp72 gene activation. The existence of Hsp72 plays a critical role in the reactivation of hsp72 gene. Glutamine sustained the induction of intracellular Hsp72, which could be beneficial in protecting the liver from various injuries.

Cited by 3 publications

References 35 publications

Glutamine Modulates Heat Shock Proteins, Endoplasmic Reticulum Stress and Cell Death in Rats with Thioacetamide-Induced Severe Acute Liver Failure

Glutamine Modulates Heat Shock Proteins, Endoplasmic Reticulum Stress and Cell Death in Rats with Thioacetamide-Induced Severe Acute Liver Failure

Physiological regulation of the heat shock response by glutamine: implications for chronic low-grade inflammatory diseases in age-related conditions

Prophylactic Inhalation of L-Alanyl-L-Glutamine Enhances Heat Shock Protein 72 and Attenuates Endotoxin-Induced Lung Injury in Rats

Contact Info

Product

Resources

About