Ultrastructural organization of proteoglycans and fibrillar matrix of the tectorial membrane

Vladimir Tsuprun, Peter Santi

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

The molecular and supramolecular structure of the tectorial membrane (TM) was studied by transmission electron microscopy (TEM). Collagen (type A) fibrils in the TM were found associated with proteoglycans (PGs) and type B fibrils. Most PGs were orthogonally oriented and attached D-periodically to collagen fibrils. Computer averaged projections of PG particles and linear aggregates of PGs in crystalline arrays, stained with Cuprolinic blue, showed an elongated, electron-dense structure 50-65 nm in length and 10 nm in width. Image analysis of type B fibrils showed that they are constructed of globular domains arranged with a periodicity of 12-14 nm. Each globular domain contains two thin 'arms', extended in opposite directions, which contact the 'arms' of adjacent fibrils. Numerous type B fibrils were found between collagen fibrils. They are attached to adjacent collagen fibrils by the 'arms' of their globular domains. An association of type B fibrils and PGs with collagen seems to result in the local ordered arrangement of the TM matrix. A hypothetical model of the TM matrix supramolecular structure is presented.

Original languageEnglish (US)
Pages (from-to)107-118
Number of pages12
JournalHearing Research
Volume110
Issue number1-2
DOIs
StatePublished - Aug 1997

Bibliographical note

Funding Information:
This research was supported by a grant from the NIDCD. The authors thank Daniel Swartz for his critical reading of the manuscript and for the computer-drawn TM model.

Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.

Keywords

  • Collagen
  • Proteoglycan
  • Tectorial membrane
  • Thin fibril
  • Transmission electron microscopy

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