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Acquired secretion defect in platelets after cryopreservation in dimethyl sulfoxide
Author(s) -
Prooijen H. C.,
Heugten J. G.,
Mommersteeg M. E.,
Akkerman J. W. N.
Publication year - 1986
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1986.26486262744.x
Subject(s) - cryopreservation , platelet , adenosine triphosphate , adenine nucleotide , adenylate kinase , energy charge , adenosine diphosphate , secretion , granule (geology) , adenosine , chemistry , dimethyl sulfoxide , cytosol , nucleotide , biochemistry , biology , platelet aggregation , microbiology and biotechnology , enzyme , immunology , embryo , paleontology , organic chemistry , gene
Despite the use of preservatives, platelets are severely damaged during cryopreservation and, following freezing, function poorly in a number of in vitro tests. We report here that cryopreserved platelets show diminished aggregation in response to collagen. This may be a consequence of a secretion defect as evidenced by a 20 to 30 percent loss of dense‐ and α‐granule content (p < 0.05) and an impaired secretion mechanism. Analysis of adenine nucleotides confirmed the defect in dense granule adenosine triphosphate (ATP) and adenosine diphosphate (ADP) content (storage pool), but in addition revealed a 50 percent fall in cytosolic ATP (metabolic pool). In contrast, the adenylate energy charge, (ATP + 1/2 ADP)/(ATP + ADP + adenosine monophosphate), was normal. We concluded that platelet cryopreservation leads to a secretion defect, probably as a result of activation during freezing and thawing procedures.