title: Changes in passive electric parameters of human erythrocyte membrane during hyperthermia: role of spectrin phosphorylation.
abstract: In prefixed by 1 mmol/l OsO4 human erythrocytes, the discocyte shape was preserved upon heating to temperatures which include the denaturation temperature of the main peripheral protein spectrin. Nevertheless, the suspension of fixed cells displayed threshold decrease in its capacitance and resistance at the temperature range where spectrin denaturates. The same changes were established using intact cells and their resealed ghosts. For packed cells (ghosts), the capacitance and resistance decreased about 17% (31%) and 30% (19%). These data indicate a decrease in the beta dispersion of erythrocyte membrane associated, according to a previous study (Ivanov 1997), with the heat denaturation of spectrin at 49.5 degrees C. The amplitude of the 49.5 degrees C decrease in beta dispersion was reversibly reduced in intact erythrocytes and white ghosts following reversible decrease in the phosphorylation of their membrane proteins. It was fully eliminated in ghosts following their resealing with alkaline phosphatase (0.1 mg/ml) which dephosphorylated membrane proteins. These findings are discussed in relation to similar changes found in normal and tumour tissues and cells during hyperthermia.
authors.affiliation: Thracian University, Stara Zagora, Medical Institute, Dept. Physics and Biophysics, Bulgaria. vmisz@bgcict.acad.bg
authors.forename: I T
authors.initials: IT
authors.lastname: Ivanov
mesh_terms: D000255:Adenosine Triphosphate / Q000502:physiology; D004553:Electric Conductivity; D004574:Electromagnetic Fields; D004910:Erythrocyte Membrane / Q000378:metabolism / Q000502:physiology*; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D010766:Phosphorylation; D013049:Spectrin / Q000378:metabolism* / Q000502:physiology*; D013816:Thermodynamics; D013817:Thermography
chemical_list: D013049:Spectrin; D000255:Adenosine Triphosphate