Literature DB >> 8647714

Cytoskeletal and calcium-binding proteins in the mammalian organ of Corti: cell type-specific proteins displaying longitudinal and radial gradients.

A K Pack1, N B Slepecky.   

Abstract

Whole mounts and tissue sections of the organ of Corti from two representative mammalian species, the Mongolian gerbil (Meriones unguiculatus) and the guinea pig (Cavea porcellus) were probed with antibodies to cytoskeletal and calcium-binding proteins (actin, tubulin, including post-translational modifications, spectrin, fimbrin, calmodulin, parvalbumin, calbindin, S-100 and calretinin). All of the proteins tested were expressed in both species. New findings include the following. Actin is present in large accumulations in cell bodies of the Deiters cells under the outer hair cells (OHC), as well as in the filament networks previously described. These accumulations are more prominent in the apical turns. Tubulin is present in sensory cells in the tyrosinated (more dynamic) form, while tubulin in the supporting cells is post-translationally modified, indicating greater stability. Fimbrin, present in the stereocilia of both IHCs and OHCs, is similar to the isoform of fimbrin found in the epithelial cells of the intestine (fimbrin-I), which implies that actin bundling by fimbrin is reduced in the presence of increased calcium. Parvalbumin appears to be an IHC-specific calcium-binding protein in the gerbil as well as in the guinea pig; labeling displays a longitudinal gradient, with hair cells at the apex staining intensely and hair cells at the base staining weakly. Calbindin displays a similar longitudinal gradient, with staining intense in the IHCs and OHCs at the apex and weak to absent in the base. In the middle turns of the guinea pig cochlea, OHCs in the first row near the pillar cells lose immunoreactivity to calbindin before those in the second and third rows. Calmodulin is found throughout the whole cochlea in the IHCs and OHCs in the stereocilia, cuticular plate, and cell body. Calretinin is present in IHCs and Deiters cells in both species, as well as the tectal cell (modified Hensen cell) in the gerbil. S-100 is a supporting cell-specific calcium-binding protein which has not been localized in the sensory cells of these two species. The supporting cells containing S-100 include the inner border, inner phalangeal, pillar, Deiters, tectal (in gerbil) and Hensen cells, where labeling displays a longitudinal gradient decreasing in intensity towards the apex (opposite to what has been seen with labeling for other proteins in the cochlea).

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Year:  1995        PMID: 8647714     DOI: 10.1016/0378-5955(95)00173-5

Source DB:  PubMed          Journal:  Hear Res        ISSN: 0378-5955            Impact factor:   3.208


  39 in total

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2.  Myosin-1c interacts with hair-cell receptors through its calmodulin-binding IQ domains.

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4.  Changes in cytochemistry of sensory and nonsensory cells in gentamicin-treated cochleas.

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Journal:  J Assoc Res Otolaryngol       Date:  2003-06

5.  Generation of inner ear hair cells by direct lineage conversion of primary somatic cells.

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6.  Characterization of the transcriptome of nascent hair cells and identification of direct targets of the Atoh1 transcription factor.

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7.  A novel missense variant in PRKCB segregates low-frequency hearing loss in an autosomal dominant family with Meniere's disease.

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8.  Calretinin and calbindin distribution patterns specify subpopulations of type I and type II spiral ganglion neurons in postnatal murine cochlea.

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Journal:  J Comp Neurol       Date:  2014-07-01       Impact factor: 3.215

9.  Comparative examination of inner ear in wild type and pituitary adenylate cyclase activating polypeptide (PACAP)-deficient mice.

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10.  Ca2+-binding protein 2 inhibits Ca2+-channel inactivation in mouse inner hair cells.

Authors:  Maria Magdalena Picher; Anna Gehrt; Sandra Meese; Aleksandra Ivanovic; Friederike Predoehl; SangYong Jung; Isabelle Schrauwen; Alberto Giulio Dragonetti; Roberto Colombo; Guy Van Camp; Nicola Strenzke; Tobias Moser
Journal:  Proc Natl Acad Sci U S A       Date:  2017-02-09       Impact factor: 11.205

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