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. 1987 Feb 15;242(1):115–121. doi: 10.1042/bj2420115

Re-evaluation of the structural integrity of red-cell glycoproteins during aging in vivo and nutrient deprivation.

A Brovelli, C Seppi, A Bardoni, C Balduini, H U Lutz
PMCID: PMC1147672  PMID: 3593232

Abstract

Results presented in this paper show that removal of white-cell contaminations from human red blood cells by filtration through cellulose [Beutler, West & Blume (1976) J. Lab. Clin. Med. 88, 328-333] is a necessity whenever red cells are incubated at elevated temperatures or haemolysed after density separation. Omission of this precaution results in proteolysis of sialoglycoproteins in membranes from less-dense (young), but not dense (old), subpopulations. This proteolytic damage occurs during haemolysis of the cytoplasmic domain of glycophorin. A different type of proteolysis occurs if white-cell-contaminated red cells are incubated in the absence of glucose at elevated temperatures. Red cells release sialoglycopeptides. This process is stimulated by Ca2+ ions and is accompanied by the release of vesicles that differ from spectrin-free vesicles [Lutz, Liu & Palek (1977) J. Cell Biol. 73, 548-560]. This sialoglycopeptide release is dependent on white-cell contamination and is not required for the release of spectrin-free vesicles.

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