scholarly journals Daily Supplementation of L-Glutamine in Atrial Fibrillation Patients: The Effect on Heat Shock Proteins and Metabolites

Cells ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 1729 ◽  
Author(s):  
Roeliene Starreveld ◽  
Kennedy S. Ramos ◽  
Agnes J. Q. M. Muskens ◽  
Bianca J. J. M. Brundel ◽  
Natasja M. S. de Groot

Pharmaco-therapeutic strategies of atrial fibrillation (AF) are moderately effective and do not prevent AF onset and progression. Therefore, there is an urgent need to develop novel therapies. Previous studies revealed heat shock protein (HSP)-inducing compounds to mitigate AF onset and progression. Such an HSP inducing compound is L-glutamine. In the current study we investigate the effect of L-glutamine supplementation on serum HSP27 and HSP70 levels and metabolite levels in patients with AF patients (n = 21). Hereto, HSP27 and HSP70 levels were determined by ELISAs and metabolites with LC-mass spectrometry. HSP27 levels significantly decreased after 3-months of L-glutamine supplementation [540.39 (250.97–1315.63) to 380.69 (185.68–915.03), p = 0.004] and normalized to baseline levels after 6-months of L-glutamine supplementation [634.96 (139.57–3103.61), p < 0.001]. For HSP70, levels decreased after 3-months of L-glutamine supplementation [548.86 (31.50–1564.51) to 353.65 (110.58–752.50), p = 0.045] and remained low after 6-months of L-glutamine supplementation [309.30 (118.29–1744.19), p = 0.517]. Patients with high HSP27 levels at baseline showed normalization of several metabolites related to the carbohydrates, nucleotides, amino acids, vitamins and cofactors metabolic pathways after 3-months L-glutamine supplementation. In conclusion, L-glutamine supplementation reduces the serum levels of HSP27 and HSP70 within 3-months and normalizes metabolite levels. This knowledge may fuel future clinical studies on L-glutamine to improve cardioprotective effects that may attenuate AF episodes.

2007 ◽  
Vol 7 (3) ◽  
pp. 447-451
Author(s):  
Roman Laszlo ◽  
Mathias C. Busch ◽  
Stefan Wohrl ◽  
Sabine B. Schleicher ◽  
Ralf E. WeBel ◽  
...  

2005 ◽  
Vol preprint (2007) ◽  
pp. 1
Author(s):  
Miao Yang ◽  
Hao Tan ◽  
Longxian Cheng ◽  
Meian He ◽  
Qingyi Wei ◽  
...  

2020 ◽  
Author(s):  
Daiqi Liu ◽  
Zhaojia Wang ◽  
Panagiotis Korantzopoulos ◽  
Tong Liu

2019 ◽  
Vol 20 (23) ◽  
pp. 5843 ◽  
Author(s):  
Stephen John Bentley ◽  
Aileen Boshoff

The etiological agent of African trypanosomiasis, Trypanosoma brucei (Tb), has been identified to possess an expanded and diverse group of heat shock proteins, which have been implicated in cytoprotection, differentiation, and subsequently progression and transmission of the disease. Heat shock protein 70 (Hsp70) is a highly conserved and ubiquitous molecular chaperone that is important in maintaining protein homeostasis in the cell. Its function is regulated by a wide range of co-chaperones, and inhibition of these functions and interactions with co-chaperones are emerging as potential therapeutic targets for numerous diseases. This study sought to biochemically characterize the cytosolic TbHsp70 and TbHsp70.4 proteins and to investigate if they functionally co-operate with the Type I J-protein, Tbj2. Expression of TbHsp70 was shown to be heat inducible, while TbHsp70.4 was constitutively expressed. The basal ATPase activities of TbHsp70.4 and TbHsp70 were stimulated by Tbj2. It was further determined that Tbj2 functionally co-operated with TbHsp70 and TbHsp70.4 as the J-protein was shown to stimulate the ability of both proteins to mediate the refolding of chemically denatured β-galactosidase. This study provides further insight into this important class of proteins, which may contribute to the development of new therapeutic strategies to combat African Trypanosomiasis.


2017 ◽  
Vol 13 (1) ◽  
Author(s):  
Sophie Z. Lin ◽  
Todd C. Crawford ◽  
Kaushik Mandal

2008 ◽  
Vol 78 (3) ◽  
pp. 422-428 ◽  
Author(s):  
B. J.J.M. Brundel ◽  
L. Ke ◽  
A.-J. Dijkhuis ◽  
X. Qi ◽  
A. Shiroshita-Takeshita ◽  
...  

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