We have cloned the gene for Drosophila gelsolin. Two mRNAs are produce
d from this gene by differential splicing. The protein encoded by the
longer mRNA has a signal peptide and its electrophoretic mobility when
translated in vitro in the presence of microsomes is higher than when
it is translated without microsomes. The protein translated from the
shorter mRNA does not show this difference. This indicates that Drosop
hila like vertebrates has two forms of gelsolin, one secreted, the oth
er cytoplasmic. The mRNA for both is present ubiquitously in the early
embryo. Later, the cytoplasmic form is expressed in parts of the gut.
The RNA for the secreted form is expressed in the fat body, and the s
ecreted protein is abundant in extracellular fluid (hemolymph). The cy
toplasmic form of gelsolin co-localizes with F-actin in the cortex of
the cells in the embryo and in larval epithelia. However, during cellu
larization of the blastoderm it is reduced at the base of the cleavage
furrow, a structure similar to the contractile ring in dividing cells
.