ISSN:
0091-7419
Keywords:
thrombocyte-rich plasma
;
disulfide-bonded protein aggregates
;
erythrocyte fragmentation
;
human erythrocytes
;
in vitro aging
;
ATP-depletion
;
spectrin-free vesicles
;
fragments of erythrocytes
;
Life Sciences
;
Molecular Cell Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
When human erythrocytes are depleted of endogenous ATP they release spectrin-free vesicles as a light vesicle fraction [Lutz et al: J Cell Biol 73:548, 1977] and chains of rounded vesicles as well as flattened myelin forms in a heavy vesicle fraction. The heavy fraction retains some spectrin, and glycophorin is partially degraded. The release of both types of fragments is not dependent upon added Ca+2, and 50 μM EGTA does not prevent the vesicle release. Concomitant with vesicle release, a large fraction of the major protein components of the cell is found in disulfide-bonded aggregates.A protocol is outlined to recover erythrocyte-specific fragments from thrombocyte-rich plasma. It allows detection of spectrin-free vesicles in whole blood stored under blood bank conditions for 12 days. In freshly drawn blood no such vesicles are observed, but particles are obtained that are different from thrombocyte fragments and that show a prominent glycoprotein running slightly faster than glycophorin.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jss.400080314
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