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MW Mosesson, GA Homandberg and DL Amrani
Human plasma fibrinogen is produced by liver parenchymal cells. Such
molecules contain two classes of gamma-chains (gamma A, gamma'), which
differ with respect to their COOH-terminal sequences. When fibrin is
crosslinked in the presence of factor XIIIa and Ca2+, three types of
gamma-dimer are formed (gamma A-gamma A; gamma A-gamma'; gamma'- gamma'). A
separate fibrinogen pool is located in platelet alpha- granules. We
analyzed this fibrinogen to determine whether gamma'- chains were present
to the same extent (7%) that they are found in plasma fibrinogen.
Electrophoretic analysis (Laemmli system) of reduced samples of the clot
that formed subsequent to release of fibrinogen from thrombin-stimulated
washed platelets, revealed a single crosslinked gamma-dimer band in the
gamma A-gamma A position. Material collected into EDTA-containing buffer
and subsequently crosslinked in the presence of added factor XIII and Ca2+
also revealed a gamma A- gamma A dimer band. This finding was further
investigated by Western blotting of reduced gel specimens that had been
reacted with an anti- gamma-chain antibody followed by 125I-labeled protein
A. A single type of gamma-chain, gamma A, was present in the fibrinogen
from a Triton X- 100 or 10 M urea platelet lysate, or in noncrosslinked
fibrin obtained from thrombin-treated platelets. Crosslinked reduced fibrin
from thrombin-treated platelets or that prepared from the Triton lysate
revealed a single type of gamma-dimer, gamma A-gamma A. We conclude that
there are no gamma'-chains (less than 1%) in platelet fibrinogen. This
structural difference from hepatic fibrinogen probably results from
differences in the processing and/or regulation of the fibrinogen
gamma-chain gene in megakaryocytes.
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| Copyright © 1984 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||