Effects of L-proline on cellular responses of hen erythrocytes subjected to thermal stress.


Journal

Journal of thermal biology
ISSN: 0306-4565
Titre abrégé: J Therm Biol
Pays: England
ID NLM: 7600115

Informations de publication

Date de publication:
Feb 2021
Historique:
received: 12 06 2020
revised: 02 01 2021
accepted: 12 01 2021
entrez: 25 2 2021
pubmed: 26 2 2021
medline: 21 10 2021
Statut: ppublish

Résumé

Little is known on the protective effects of L-proline on hen erythrocytes. The aim of the study was to determine the protective effects of this amino acid at concentrations of 50 μg/mL, 100 μg/mL, 200 μg/mL in hen erythrocytes subjected to temperatures 41 °C, 43 °C and 45 °C for 1 h and 4 h. The following cellular parameters were determined: viability, morphological alterations, caspase 3/7 activity, heat shock protein HSP70 1A activity and glutathione level. The results showed that exposure to 43 °C and 45 °C resulted in a decrease of viability and increased morphological alterations of the non-treated erythrocytes. Caspase 3/7 activity was increased only at 45 °C, however HSP70 1A activity and glutathione level were increased in the temperature-dependent manner. On the other hand, erythrocytes additionally exposed to L-proline showed alterations of the parameters when compared to the non-treated cells. L-proline at 50 μg/mL and 100 μg/mL increased caspase 3/7 activity at both 41 °C and 43 °C, however it was less augmented at all the concentrations at 45 °C. Glutathione level was decreased in heat-stressed (at 43 °C and 45 °C) hen erythrocytes treated with L-proline (at 50 μg/mL and 100 μg/mL) but it was increased at 200 μg/mL. HSP70 1A activity was augmented in a concentration- and temperature-dependent manner. The results indicate that proapoptotic or antiapoptotic effects of L-proline depend on its concentration and temperature of heat stress and thermoprotective effects induced by the amino acid on some parameters in hen erythrocytes may be a result of stimulation of antioxidative defense and stimulation of HSP70 1A activity.

Identifiants

pubmed: 33627283
pii: S0306-4565(21)00022-X
doi: 10.1016/j.jtherbio.2021.102855
pii:
doi:

Substances chimiques

Avian Proteins 0
HSP72 Heat-Shock Proteins 0
Proline 9DLQ4CIU6V
Caspase 3 EC 3.4.22.-
Caspase 7 EC 3.4.22.-
Glutathione GAN16C9B8O

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

102855

Informations de copyright

Copyright © 2021 Elsevier Ltd. All rights reserved.

Auteurs

Aleksandra Szabelak (A)

Department of Hydrobiology and Protection of Environment, University of Life Sciences in Lublin, ul. Dobrzańskiego 37, 20-262, Lublin, Poland.

Adam Bownik (A)

Department of Hydrobiology and Protection of Environment, University of Life Sciences in Lublin, ul. Dobrzańskiego 37, 20-262, Lublin, Poland. Electronic address: adambownik@wp.pl.

Sebastian Knaga (S)

Institute of Biological Basis of Animal Production, University of Life Sciences in Lublin, ul. Akademicka 13, 20-950, Lublin, Poland.

Kornel Kasperek (K)

Institute of Biological Basis of Animal Production, University of Life Sciences in Lublin, ul. Akademicka 13, 20-950, Lublin, Poland.

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Classifications MeSH