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* Department of Otolaryngology, University of Minnesota, Minneapolis, Minnesota; and
School of Life Sciences, University of Sussex, Falmer, United Kingdom
Correspondence: Address reprint requests to Vladimir Tsuprun, University of Minnesota, Rm. 109, Lions Research Bldg., 2001 Sixth St. SE, Minneapolis, MN 55455. Tel.: 612-625-0512; Fax: 1-612-626-9871; E-mail: tsupr001{at}umn.edu.
Recent studies have indicated that the tip links and kinocilial links of sensory hair bundles in the inner ear have similar properties and share a common epitope, and that cadherin 23 may also be a component of each link type. Transmission electron microscopy was therefore used to study and compare the fine structure of the tip links and kinocilial links in avian sensory hair bundles. Tannic acid treatment revealed a thin strand, 150200 nm long and 811 nm thick, present in both link types. Fourier analysis of link images showed that the strand of both link types is formed from two filaments coiled in a helix-like arrangement with an axial period of 2025 nm, with each filament composed of globular structures that are
4 nm in diameter. Differences in the radius and period of the helix-like structure may underlie the observed variation in the length of tip and kinocilial links. The similar helix-like structure of the tip links and kinocilial links is in accord with the presence of a common cell-surface antigen (TLA antigen) and similarities in the physical and chemical properties of the two link types. The spacing of the globular structures comprising each filament of the two link types is similar to the 4.3 nm center-to-center spacing reported for the globular cadherin repeat, and is consistent with the suggestion that cadherin 23 is the tip link.
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