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Platelet factor 4 and the platelet secreted proteoglycan: immunologic
characterization by crossed immunoelectrophoresis
SP Levine, LK Knieriem and MA Rager
Department of Medicine, University of Texas Health Science Center, San
Antonio.
Platelet factor 4 (PF4) is a hydrophobic, alpha-granule protein with potent
antiheparin activity. It also binds to a chondroitin sulfate- containing
proteoglycan (PG) isolated from platelets. In order to evaluate further the
relationship between PF4 and the chondroitin sulfate-containing
proteoglycan in resting platelets, the PF4-binding proteoglycan from human
platelets has been purified using purified PF4 as an affinity ligand and
used to prepare polyclonal antiserum. Two antisera have been characterized:
one reacts primarily with chondroitin sulfate (CS), the other reacts with
the protein core of the platelet proteoglycan after chondroitinase AC
digestion. PF4 and PG core protein antigen are present in separate,
dissimilar precipitin arcs when triton- solubilized platelets are analyzed
by crossed immunoelectrophoresis using polyclonal antisera to purified PF4
and PG. PF4 was demonstrated in a complex with a separate chondroitin
sulfate antigen by crossed immunoelectrophoresis (CIE) experiments in which
either anti-PF4 or anti-CS antisera was incorporated in the intermediate
gel. Both the PF4- chondroitin sulfate complex and the proteoglycan are
secreted from platelets when fresh, washed human platelets are stimulated
by human alpha-thrombin. This second antigen may represent the PG after
posttranslational modification of a precursor form of the proteoglycan.
Volume 75,
Issue 4,
pp. 902-910,
02/15/1990
Copyright © 1990 by The American Society of Hematology
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