Beneficial impact of human placenta extracts on erythrocyte membrane thermostability
Autor: | E.D. Rozanova, O. A. Nardid, E. Bobrova, S.V. Repina, Yu. Govorova, S. V. Narozhnyi |
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Rok vydání: | 2018 |
Předmět: |
human placenta extracts
human erythrocytes thermal denaturation of membrane proteins Chemistry Human placenta membrane barrier function 03 medical and health sciences Erythrocyte membrane 0302 clinical medicine Biochemistry cytosol microviscosity 030220 oncology & carcinogenesis anti-inflammatory activity lcsh:Science (General) thermal hemolysis 030217 neurology & neurosurgery lcsh:Q1-390 Thermostability |
Zdroj: | Trakia Journal of Sciences, Vol 16, Iss 3, Pp 204-211 (2018) |
ISSN: | 1313-3551 1312-1723 |
DOI: | 10.15547/tjs.2018.03.006 |
Popis: | PURPOSE: To study the influence of human placenta extract (HPE) and its individual fractions on the thermal stability of human erythrocyte membrane. METHODS: HPE fractions were isolated by gel chromatography. Thermal hemolysis of erythrocytes, exposed to 55°C was measured spectrophotometrically. Cytosol microvscosity and barrier function of erythrocyte membranes at hyperthermia were investigated by EPR spin probe TEMPON. Thermal denaturation of erythrocyte membrane proteins were studied by differential scanning calorimetry. RESULTS: Pre-treatment of erythrocytes with HPE or its fractions inhibited thermal hemolysis. Low-molecular fractions (below 4 kDa and 12-20 kDa) were the most effective in thermal hemolysis inhibition ((31.7±3.3) % and (31.5±3.2) %, respectively). The latter fractions markedly reduced the hyperthermia (55°C)-induced permeability of erythrocytes for ferricyanide ions and inhibited the thermo-induced structural transitions in erythrocyte membrane between 40 and 50°C, which are associated with cytoskeletal proteins. HPE fractions reversibly increased the denaturation temperatures of erythrocyte membrane proteins, except that of spectrin, and enlarged the enthalpy of denaturation of all membrane proteins. CONCLUSIONS: HPE and its individual fractions increased the thermal stability of erythrocyte membranes and erythrocytes. This effect was attributed to the reversible binding of some low molecular ingredient of HPE to the integral proteins and consequent stabilization of their interaction with under-membrane cytoskeleton. |
Databáze: | OpenAIRE |
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