Geiser F. 2004. Metabolic rate and body temperature reduction during hibernation and daily torpor. Annu. Rev. Physiol. 66, 239–274. https://doi.org/10.1146/annurev.physiol.66.032102.115105

Article  CAS  PubMed  Google Scholar 

Carey H.V., Andrews M.T., Martin S.L. 2003. Mammalian hibernation: Cellular and molecular responses to depressed metabolism and low temperature. Physiol. Rev. 83 (4), 1153–1181. https://doi.org/10.1152/physrev.00008.2003

Article  CAS  PubMed  Google Scholar 

Shihamirova Z., Dzhafarova A., Klichkhanov N. 2020. Hematological characteristics and erythrokinetic indices in little ground squirrels during arousal from hibernation. Probl. Cryobiol. Cryomed. 30 (2), 132–147.

Article  Google Scholar 

Klichkhanov N.K., Nikitina E.R., Shihamirova Z.M., Astaeva M.D., Chalabov S.I., Krivchenko A.I. 2021. Erythrocytes of little ground squirrels undergo reversible oxidative stress during arousal from hibernation. Front. Physiol. 12, 730657. https://doi.org/10.3389/fphys.2021.730657

Article  PubMed  PubMed Central  Google Scholar 

Rotermund Jr A.J., Veltman J.C. 1981. Modification of membrane-bound lipids in erythrocytes of cold-acclimated and hibernating 13-lined ground squirrels. Compar. Biochem. Physiol. Part B: Compar. Biochem. 69 (3), 523–528. https://doi.org/10.1016/0305-0491(81)90345-X

Article  Google Scholar 

Saldanha C., Silva-Herdade A.S. 2017. Physiological properties of human erythrocytes in inflammation. J. Cell. Biotechnol. 3 (1), 15–20. https://doi.org/10.3233/JCB-179003

Article  Google Scholar 

Carvalho F.A., de Almeida J.L., Freitas-Santos T., Saldanha C. 2009. Modulation of erythrocyte acetylcholinesterase activity and its association with G protein-band 3 interactions. J. Membr. Biol. 228, 89–97. https://doi.org/10.1007/s00232-009-9162-8

Article  CAS  PubMed  Google Scholar 

Dodge J.T., Mitchell C., Hanahan D.J. 1963. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 100 (1), 119–130. https://doi.org/10.1016/0003-9861(63)90042-0

Article  CAS  PubMed  Google Scholar 

Lowry D.H., Rosebrough H.J., Farr A.L., Randall R.J. 1951. Protein measurement with the Folin-phenol reagent. J. Biol. Chem. 193 (1), 265–275. https://doi.org/10.1016/s0021-9258(19)52451-6

Article  CAS  PubMed  Google Scholar 

Ellman Y.L., Courtney K.D., Andres V.J., Feathestone R.M. 1961. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7 (1), 88–95. https://doi.org/10.1016/0006-2952(61)90145-9

Article  CAS  PubMed  Google Scholar 

Klichkhanov N.K., Dzhafarova A.M., Al-Rabeei M.A.M. 2017. Kinetic characteristics of acetylcholinesterase and structural-functional state of rat erythrocyte membranes at moderate hypothermia. Biochem. (Mosc.) Suppl. Series A: Membr. Cell Biol. 11 (4), 275–286. https://doi.org/10.1134/S1990747817040055

Article  Google Scholar 

Jha R., Rizvi S.I. 2009. Age-dependent decline in erythrocyte acetylcholinesterase activity: Correlation with oxidative stress. Biomed. Pap. Med. Fac. Univ. Palacky. Olomouc. Czech. Repub. 153(3), 195–198. https://doi.org/10.5507/bp.2009.032

Article  CAS  PubMed  Google Scholar 

Grifman M., Ginzberg D., Soreq H. 1997. Antisense oligodeoxynucleotide dependent suppression of acetylcholinesterase expression reduces process extension from primary mammalian neurons. Advan. Behav. Biol. 49, 557–562. https://doi.org/10.1007/978-1-4615-5337-3_79

Article  Google Scholar 

Paulick M.G., Bertozzi C.R. 2008. The glycosylphosphatidylinositol anchor: A complex membrane-anchoring structure for proteins. Biochemistry. 47(27), 6991–7000. https://doi.org/10.1021/bi8006324

Article  CAS  PubMed  Google Scholar 

Arsov Z., Schara M., Zorko M., Štrancar J. 2004. The membrane lateral domain approach in the studies of lipid–protein interaction of GPI-anchored bovine erythrocyte acetylcholinesterase. Eur. Biophys. J. 33, 715–725. https://doi.org/10.1007/s00249-004-0417-0

Article  CAS  PubMed  Google Scholar 

Catalá A., Díaz M. 2016. Impact of lipid peroxidation on the physiology and pathophysiology of cell membranes. Front. Physiol. 7, 423. https://doi.org/10.3389/fphys.2016.00423

Article  PubMed  PubMed Central  Google Scholar 

Gaschler M.M., Stockwell B.R. 2017. Lipid peroxidation in cell death. Biochem. Biophys. Res. Commun. 482(3), 419–425. https://doi.org/10.1016/j.bbrc.2016.10.086

Article  CAS  PubMed  PubMed Central  Google Scholar 

Melo A.S.D., Ferreira M.D.A., Verás A.S.C., Lira M.D.A., Lima L.E.D., Vilela M.D.S., Araújo P.R.B. 2003. Partial replacement of soybean meals for urea and forage cactus in lactating cow diets. I. Performance. Revista Brasileira de Zootecnia. 32, 727–736. https://doi.org/10.4025/actascianimsci.v25i2.567

Article  Google Scholar 

Schallreuter K.U., Elwary S.M., Gibbons N.C., Rokos H., Wood J.M. 2004. Activation/deactivation of acetylcholinesterase by H2O2: More evidence for oxidative stress in vitiligo. Biochem. Biophys. Res. Commun. 315 (2), 502–508. https://doi.org/10.1016/j.bbrc.2004.01.082

Article  CAS  PubMed  Google Scholar 

Molochkina E.M., Zorina O.M., Fatkullina L.D., Goloschapov A.N., Burlakova E.B. 2005. H2O2 modifies membrane structure and activity of acetylcholinesterase. Chem. Biol. Interact. 157 (30), 401–404. https://doi.org/10.1016/j.cbi.2005.10.075

Article  CAS  PubMed  Google Scholar 

Satchwell T.J., Hawley B.R., Bell A.J., Ribeiro M.L., Toye A.M. 2014. The cytoskeletal binding domain of band 3 is required for multiprotein complex formation and retention during erythropoiesis. Blood. 124 (21), 4003. https://doi.org/10.3324/haematol.2014.114538

Article  CAS  Google Scholar 

Pantaleo A., Ferru E., Pau, M. C., Khadjavi,A., Mandili G., Mattè, A., Turrini F. 2016. Band 3 erythrocyte membrane protein acts as redox stress sensor leading to its phosphorylation by p72 Syk. Oxid. Med. Cell. Longevity. 2016(1), 6051093. https://doi.org/10.1155/2016/6051093

Kawashima S.K., Fujii T. 2008. Basic and clinical aspects of non-neuronal acetylcholine: overview of non-neuronal cholinergic systems and their biological significance. J. Pharmacol. Sci. 106 (2), 167–173. https://doi.org/10.1254/jphs.FM0070073

Article  CAS  PubMed  Google Scholar