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Capacity of human serum to depolymerize actin filaments
PA Janmey and SE Lind
Human blood depolymerizes filamentous (F-)actin. The interaction of actin
filaments and monomers with human serum was studied by following the
kinetics and extent of the depolymerization of pyrene-labeled F- actin and
by analysis of serum proteins adhering to immobilized actin monomers. In
physiologic Ca2+ concentrations, the depolymerization of F- actin proceeds
in two stages: a rapid phase, attributed to direct severing of filaments by
plasma gelsolin, and a slow phase attributed to the binding of actin
monomers to vitamin D-binding protein (DBP). Without Ca2+, only the slow
phase is observed. Human serum can completely depolymerize 10 to 18 mumol/L
of actin, of which approximately 5 mumol/L occurs rapidly. Depolymerization
can be accounted for by the normal serum concentrations of gelsolin and
DBP. Fibrin(ogen) and fibronectin, which bind actin in vitro, do not
contribute to the kinetics or extent of its depolymerization. Affinity
chromatography and functional assays for the presence of gelsolin-actin
complexes show that addition of G-actin to serum results in preferential
formation of actin-DBP complexes, but that addition of F- actin to serum
produces both gelsolin-actin complexes and DBP-actin complexes. The
distinctive binding of actin monomers and polymers to these two serum
proteins suggests a means by which their coordinated actions are maximized
in vivo, from the standpoint of depolymerizing filaments and clearing
monomers from the circulation.
Volume 70,
Issue 2,
pp. 524-530,
08/01/1987
Copyright © 1987 by The American Society of Hematology
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