Identification of actin-binding protein and villin in toad bladder epithelia.
Two actin-modulating proteins, actin-binding protein and villin, have been identified and functionally characterized in toad bladder epithelial cells. A 270-kdalton protein from bladder epithelial extracts 1) cross-reacts with antibodies to purified toad oocyte or rabbit macrophage actin-binding protein and comigrates with these proteins on gel electrophoresis, 2) contains all of the actin filament cross-linking activity found in epithelial cell extracts, and 3) its activity is calcium insensitive. A 95-kdalton protein from the same extracts 1) cross-reacts with antibodies to purified toad oocyte villin and comigrates with purified villin from the oocyte and chicken intestine on polyacrylamide gels, and 2) is capable of decreasing the viscosity of actin solutions only in the presence of calcium. These proteins offer potential sites for calcium-dependent and -independent regulation of toad bladder epithelial cell structure.
D000818:Animals; D002024:Bufo marinus; D002118:Calcium / Q000494:pharmacology; D002352:Carrier Proteins / Q000032:analysis*; D003429:Cross Reactions; D004848:Epithelium / Q000032:analysis; D005260:Female; D018260:Gelsolin; D005779:Immunodiffusion; D008840:Microfilament Proteins; D008970:Molecular Weight; D001743:Urinary Bladder / Q000032:analysis*
D002352:Carrier Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; C016953:brevin; C026615:villin; D002118:Calcium