Key result
Isolating bay scallop gill basal apparatus reveals a unique protein named ankyrin.
Why the study?
The extent of the contribution of striated rootlets to cellular architecture in the basal apparatus of molluscan ciliated gill epithelium has been somewhat underestimated due to preservation challenges.
The study isolated the basal apparatus from scallop gill epithelium and identified a unique 230-250 kDa protein, named ankyrin, comprising the striated rootlets.
Should not alter clinical practice; leaves open ankyrin conservation and function in mammalian cardiovascular cells.
The basal apparatus, consisting of an array of interconnected basal bodies bearing bifurcating striated rootlets encompassing a nucleus, has been isolated from hypertonically deciliated columnar gill epithelial cells of the bay scallop Aequipecten irradians through gentle lysis with Triton X-100. The rootlets, 8-10 mum in length, were not easily preserved with conventional electron microscope fixatives, suggesting that the extent of their contribution to cellular architecture has been somewhat underestimated, even though Englemann described many of the structural details of the basal apparatus in 1880. The striated rootlets were soluble at high but not at low pH, in 2 M solutions of sodium azide and potassium thiocyanate but not sodium or potassium chloride, in 1% deoxycholate but not digitonin, and in the denaturing solvents 6 M guanidine-HC1, 8 M urea, and 1% sodium dodecylsulfate at 100 degrees C. The protein found consistently when rootlets were solubilized migrated on SDS-polyacrylamide gels as a closely spaced doublet with apparent molecular weights of 230,000 and 250,000 daltons. This unique protein, distinct from tropocollagen or various muscle components, has been named ankyrin because of the rootlet's anchor-like function in the cell.
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R. E. Stephens (1975) studied this question. The basal apparatus from the bay scallop gill epithelium was isolated and found to contain a unique 230,000-250,000 dalton protein named ankyrin.
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