ISSN:
0886-1544
Keywords:
actin
;
echinoderm
;
fascin
;
filopodia
;
actin cross-linking protein
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Medicine
Notes:
Echinoderm 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.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/cm.970010203
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