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Role of membrane sialic acid and glycophorin protein in thorium induced aggregation and hemolysis of human erythrocytes.

Abstract：

:Thorium-232 ((232)Th), a natural radionuclide from the actinide family, is abundantly present in monazite and other ores. It is used as one of the prime fuel materials in nuclear industry and may pose an exposure risk to nuclear workers and members of the public. Human erythrocytes, as a classical cellular membrane model, were coincubated with (232)Th in order to elucidate whether this naturally occurring important radionuclide produced perturbations to cell membrane. Present study revealed that erythrocytes underwent aggregation or lysis depending on the ratio of (232)Th to cell. Scanning electron micrographs showed that erythrocytes transformed into equinocytes and/or spherocytes after (232)Th treatment. Further examination of erythrocyte by atomic force microscopy suggested significant increase in surface roughness after (232)Th treatment. Experiments on neuraminidase treated and/or anti-GpA antibody blocked erythrocytes suggested significant role of membrane sialic acid and glycophorin A (GpA) protein in aggregation or hemolytic effects of (232)Th. Further results showed that (232)Th caused hemolysis by colloid osmotic mechanism, as evidenced by potassium efflux, osmotic protection and osmotic fragility studies. Osmoprotection experiments indicated that hemolysis get elicited through the formation of membrane pores of approximately 2.0 nm in size. Hemolysis studies in presence of inhibitors (TEA, bumetanide, DIDS and amiloride) revealed the role of K(+) channel, Na(+)/K(+)/2Cl(-) channel, Cl(-)/HCO(3)(-) anion exchanger and Na(+)/H(+) antiporter in (232)Th induced erythrolysis. Presence of non-diffusible cation (N-methyl d-glucasamine) or anion (gluconate) in erythrocyte suspending medium further confirm the role of Na(+) and Cl(-) influx in hemolytic effect of (232)Th. These findings provide significant insight in structural, biochemical and osmotic toxic effects of (232)Th on human erythrocytes.

journal_name

Biochimie

journal_title

Biochimie

authors

Kumar A,Ali M,Pandey BN,Hassan PA,Mishra KP

doi

10.1016/j.biochi.2010.03.008

subject

Has Abstract

pub_date

2010-07-01 00:00:00

pages

869-79

issue

7

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(10)00102-1

journal_volume

92

pub_type

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