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Purification and functional characterization of homodimeric gamma B- gamma
B fibrinogen from rat plasma
SO Lawrence, TW Wright, CW Francis, PJ Fay and PJ Haidaris
Department of Medicine/Hematology Unit, University of Rochester School of
Medicine and Dentistry, NY.
Heterogeneity in the human and rat plasma fibrinogen (FBG) gamma chains is
due to differential splicing of the primary gamma chain mRNA transcript.
The subunit composition of FBG containing the predominant form of the gamma
chain is homodimeric (human: A alpha 2, B beta 2, gamma 50-gamma 50; rat: A
alpha 2, B beta 2, gamma A-gamma A). The subunit composition of FBG
containing the longer, minor form of the gamma chain is heterodimeric
(human: A alpha 2, B beta 2, gamma 50- gamma 57.5; rat: A alpha 2, B beta
2, gamma A-gamma B). The variant gamma chain-FBGs comprise about 10% of the
total plasma FBG in the human and 30% in the rat. Although the presence of
homodimeric gamma B- gamma B FBG has been speculated, proof of its
existence has been difficult to obtain experimentally. We now show that 5%
to 6% of rat plasma FBG is found as homodimeric FBG with a subunit
composition of A alpha 2, B beta 2, gamma B-gamma B. Commercially purified
rat FBG was further purified by diethylaminoethyl-Sephacel chromatography
with a combined pH and ionic strength gradient. The enriched gamma B-gamma
B FBG fraction eluted at the lowest pH (6.3) and highest ionic strength
(4.5 mmho) due to its increased net negative charge. To further purify
gamma B-gamma B FBG, a Mono Q column with an NaCl gradient was used. The
subunit composition of the purified gamma B-gamma B FBG was confirmed by
its electrophoretic mobility under reducing and denaturing conditions both
as FBG, and clotted and cross-linked fibrin. Homodimeric gamma B-gamma B
FBG was unable to support adenosine diphosphate (ADP)-induced platelet
aggregation, whereas heterodimeric gamma A-gamma B FBG was able to support
ADP-induced platelet aggregation at 40% of that achieved with homodimeric
gamma A-gamma A FBG, similar to previous observations with human FBGs.
Taken together, these results support the hypothesis that the A alpha-RGD
sites alone are not sufficient for dimeric FBG support of platelet
aggregation. Furthermore, the data suggest that at least one intact
platelet recognition site at the carboxyterminus of the gamma A or gamma 50
chain is required.
Volume 82,
Issue 8,
pp. 2406-2413,
10/15/1993
Copyright © 1993 by The American Society of Hematology
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