Atrophy of the stria vascularis is a genetically determined deafness of aging characterized by a bilateral symmetrical sensori‐neural hearing loss showing flat audiometric patterns and excellent speech discrimination. The temporal bones of individuals exhibiting this type of hearing loss were studied by serial sections and surface preparations for light microscopy and by electron microscopy. The atrophic changes are most severe in the apical regions of the cochleas and involve the marginal, intermediate and basal cells in that order of severity. It seems probable that atrophy of the stria vascularis causes some deficiency in the quality of endolymph throughout the cochlear duct, regardless of the location of the atrophy. Typically all other structures of the cochlear duct are normal, and the sense organ when stimulated within its sensitivity range is capable of normal stimulus coding, thus accounting for the usually excellent speech discrimination.

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Keratan sulfate proteoglycan (KSPG) and dermatan sulfate proteoglycan (DSPG) are associated with collagen fibrils in adult rabbit cornea. Because certain cytochemical data suggested that proteoglycans are associated with type VI collagen in the fetal rabbit cornea, we developed polyclonal antibodies specific to the core proteins of rabbit corneal KSPG (lumican and/or fibromodulin) and DSPG (decorin and/or biglycan) and used the antibodies as immunocytochemical probes to determine proteoglycan ultrastructural location.Immunogold particles were associated with Type VI collagen fdaments but not with collagen fibrils in fetal and neonate rabbit cornea. Association of corneal KSPG and DSPG with Type VI collagen was immunocytochemidy codmed

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