Abstract

AbstractEchinoderm coelomocytes transform from petaloid cells with large motile lamellipodia to filopodial forms. During this morphological transformation, actin filaments extensively reorganize from a random meshwork into tight bundles, which become the skeletons or cores of the filopodia. Antibody localization procedures show that fascin, a 58,000 dalton actin cross‐linking protein, becomes incorporated into the filament bundles as they form. Isolated filopodial cores have a pronounced transverse striping pattern, which has been previously identified with fascin crosslinks, and gel electrophoresis identifies a protein in the cores that co‐migrates with purified egg fascin. A few of the core fragments also have a distinctive “cap,” which we presume is the membrane insertion site for actin filaments.We have developed a radioimmunoassay for fascin and have used it to study the redistribution of this protein during transformation. Data from the assay indicate that fascin constitutes about 5% of the total cell protein and that substantially more fascin, approximately 1.5–2 times more, is found in the Triton‐insoluble cytoskeletons of the filopodial cells than in the petaloid cells. Actin, measured by the DNAase I inhibition assay accounts for approximately 10% of the total cell protein. Approximately 65% of this actin is in a soluble non‐filamentous form in the petaloid cells. Our results show that actin polymerization must occur during the cell shape change, since we find approximately 25% more actin in the filopodial cytoskeleton than in the petaloid cytoskeleton. The results show a preferential incorporation of fascin into the cytoskeleton as the cells form filopodia.

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