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Hypochlorite modified LDL are a stronger agonist for platelets than copper oxidized LDL
Author(s) -
Volf Ivo,
Roth Astrid,
Cooper Julian,
Moeslinger Thomas,
Koller Elisabeth
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02104-9
Subject(s) - hypochlorite , chemistry , in vivo , platelet , low density lipoprotein , apolipoprotein b , lipoprotein , biochemistry , albumin , agonist , platelet activation , biophysics , cholesterol , medicine , organic chemistry , receptor , biology , microbiology and biotechnology
Experimental low density lipoprotein (LDL) oxidation is usually performed using trace copper, although the in vivo relevance of this method has been called into question. Such LDL augment adenosine 5′‐diphosphate (ADP) induced platelet aggregation, presumably by the action of lipid derived compounds. In striking contrast, we find that LDL oxidized to a comparable extent by hypochlorite, an in vivo occurring oxidant, reveal themselves to be potent promoters of platelet aggregation. Interestingly, hypochlorite modified LDL seem to mediate their influence on human platelets by means of the modified apolipoprotein B‐100 (apoB) moiety. Also, the finding that hypochlorite modified albumin is able to trigger platelet aggregation suggests an essential role for hypochlorite modified protein(s) in the process of platelet activation.