Reversibility of gelsolin/actin interaction in macrophages. Evidence of Ca2+-dependent and Ca2+-independent pathways

C. Chaponnier, H. L. Yin, T. P. Stossel

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

We have developed an immunoadsorption technique for quantitating EGTA-resistant gelsolin/actin complexes in macrophages extracted with Triton X-100. We report here that the proportion of gelsolin complexes irreversibly to actin is low in freshly harvested macrophages. The amount of the EGTA-resistant complex increases spontaneously during incubation of the cells in suspension at 37°C, or after exposure to the Ca2+ ionophore ionomycin. On the other hand, exposure of suspended cells to the chemotactic oligopeptide, FMLP, or plating of the cells onto tissue culture dishes causes the EGTA-resistant complex to dissociate rapidly. Plating even prevents Ca2+ ionomycin-treated cells with elevated intracellular Ca2+ from inducing this complex. Therefore, our results suggest that macrophages possess a mechanism, not directly involving Ca2+, for dissociating actin/gelsolin EGTA-resistant complexes. This mechanism may be a Ca2+-independent signal for leukocyte activation.

Original languageEnglish (US)
Pages (from-to)97-106
Number of pages10
JournalJournal of Experimental Medicine
Volume165
Issue number1
StatePublished - 1987

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Gelsolin
Egtazic Acid
Actins
Macrophages
Ionomycin
Oligopeptides
Ionophores
Octoxynol
Suspensions
Leukocytes

ASJC Scopus subject areas

  • Immunology

Cite this

Reversibility of gelsolin/actin interaction in macrophages. Evidence of Ca2+-dependent and Ca2+-independent pathways. / Chaponnier, C.; Yin, H. L.; Stossel, T. P.

In: Journal of Experimental Medicine, Vol. 165, No. 1, 1987, p. 97-106.

Research output: Contribution to journalArticle

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