Abstract
Ultrastructure of the tectorial membrane in the chinchilla cochlea was studied by transmission electron microscopy using different fixatives and staining procedures. It was shown that the tectorial membrane is a highly structured matrix composed of collagen type A fibrils, noncollagenous type B fibrils and proteoglycan. The localization of type B fibrils surrounding bundles of parallel type A fibrils was observed. Staining of the tectorial membranes with the cationic dye Cuprolinic blue in a 'critical electrolyte concentration' method revealed proteoglycan, D-periodically associated with collagen type A fibrils and orthogonal to them. The appearance and size of the proteoglycan, and its binding to collagen, were similar to small proteoglycans observed in cartilage and other tissues. In many regions of the tectorial membrane the collagen-bound proteoglycan forms crystalline-like arrays. The images of these arrays processed by Fourier analysis show long linear aggregates of proteoglycan arranged parallel each other.
Original language | English (US) |
---|---|
Pages (from-to) | 31-38 |
Number of pages | 8 |
Journal | Matrix Biology |
Volume | 15 |
Issue number | 1 |
DOIs | |
State | Published - Apr 1996 |
Bibliographical note
Funding Information:This research was supported by a grant from the NIDCD.
Keywords
- Cochlea
- Collagen
- Electron microscopy
- Proteoglycan
- Tectorial membrane