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Protein kinase A activity and NO are involved in the regulation of crucian carp (Carassius carassius) red blood cell osmotic fragility.
Andreyeva, Aleksandra Yu; Kladchenko, Ekaterina S; Sudnitsyna, Julia S; Krivchenko, Aleksander I; Mindukshev, Igor V; Gambaryan, Stepan.
Afiliación
  • Andreyeva AY; Department of Animal Physiology and Biochemistry, Moscow Representative Office A.O. Kovalevsky Institute of Biology of the Southern Seas of RAS, Leninsky ave 38, Moscow, Russia, 119991. andreevaal@gmail.com.
  • Kladchenko ES; Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Toreza, 44, St-Petersburg, Russia, 194223. andreevaal@gmail.com.
  • Sudnitsyna JS; Department of Animal Physiology and Biochemistry, Moscow Representative Office A.O. Kovalevsky Institute of Biology of the Southern Seas of RAS, Leninsky ave 38, Moscow, Russia, 119991.
  • Krivchenko AI; Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Toreza, 44, St-Petersburg, Russia, 194223.
  • Mindukshev IV; Center for Theoretical Problems of Physicochemical Pharmacology, RAS, Srednyaya Kalitnikovskaya Str., 30, Moscow, Russia, 109029.
  • Gambaryan S; Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Toreza, 44, St-Petersburg, Russia, 194223.
Fish Physiol Biochem ; 47(4): 1105-1117, 2021 Aug.
Article en En | MEDLINE | ID: mdl-34052972
Activation of the cAMP pathway by ß-adrenergic stimulation and cGMP pathway by activation of guanylate cyclase substantially affects red blood cell (RBC) membrane properties in mammals. However, whether similar mechanisms are involved in RBC regulation of lower vertebrates, especially teleosts, is not elucidated yet. In this study, we evaluated the effects of adenylate cyclase activation by epinephrine and forskolin, guanylate cyclase activation by sodium nitroprusside, and the role of Na+/H+-exchanger in the changes of osmotic fragility and regulatory volume decrease (RVD) response in crucian carp RBCs. Western blot analysis of protein kinase A and protein kinase G substrate phosphorylation revealed that changes in osmotic fragility were regulated via the protein kinase A, but not protein kinase G signaling pathway. At the same time, the RVD response in crucian carp RBCs was not affected either by activation of adenylate or guanylate cyclase. Adenylate cyclase/protein kinase A activation significantly decreased RBC osmotic fragility, i.e., increased cell rigidity. Inhibition of Na+/H+-exchanger by amiloride had no effect on the epinephrine-mediated decrease of RBC osmotic fragility. NO donor SNP did not activate guanylate cyclase, however affected RBCs osmotic fragility by protein kinase G-independent mechanisms. Taken together, our data demonstrated that the cAMP/PKA signaling pathway and NO are involved in the regulation of crucian carp RBC osmotic fragility, but not in RVD response. The authors confirm that the study has no clinical trial.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Carpas / Proteínas Quinasas Dependientes de AMP Cíclico / Proteínas de Peces / Óxido Nítrico Límite: Animals / Humans Idioma: En Revista: Fish Physiol Biochem Año: 2021 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Carpas / Proteínas Quinasas Dependientes de AMP Cíclico / Proteínas de Peces / Óxido Nítrico Límite: Animals / Humans Idioma: En Revista: Fish Physiol Biochem Año: 2021 Tipo del documento: Article Pais de publicación: Países Bajos