Tectorins crosslink type II collagen fibrils and connect the tectorial membrane to the spiral limbus. Andrade, L. R., Salles, F. T., Grati, M., Manor, U., & Kachar, B. Journal of Structural Biology, 194(2):139-146, 2016. ![Tectorins crosslink type II collagen fibrils and connect the tectorial membrane to the spiral limbus [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex All inner ear organs possess extracellular matrix appendices over the sensory epithelia that are crucial for their proper function. The tectorial membrane (TM) is a gelatinous acellular membrane located above the hearing sensory epithelium and is composed mostly of type II collagen, and α and β tectorins. TM molecules self-assemble in the endolymph fluid environment, interacting medially with the spiral limbus and distally with the outer hair cell stereocilia. Here, we used immunogold labeling in freeze-substituted mouse cochleae to assess the fine localization of both tectorins in distinct TM regions. We observed that the TM adheres to the spiral limbus through a dense thin matrix enriched in α- and β-tectorin, both likely bound to the membranes of interdental cells. Freeze-etching images revealed that type II collagen fibrils were crosslinked by short thin filaments (4±1.5nm, width), resembling another collagen type protein, or chains of globular elements (15±3.2nm, diameter). Gold-particles for both tectorins also localized adjacent to the type II collagen fibrils, suggesting that these globules might be composed essentially of α- and β-tectorins. Finally, the presence of gold-particles at the TM lower side suggests that the outer hair cell stereocilia membrane has a molecular partner to tectorins, probably stereocilin, allowing the physical connection between the TM and the organ of Corti.
@article{ANDRADE2016139,
title = {Tectorins crosslink type II collagen fibrils and connect the tectorial membrane to the spiral limbus},
journal = {Journal of Structural Biology},
volume = {194},
number = {2},
pages = {139-146},
year = {2016},
issn = {1047-8477},
doi = {https://doi.org/10.1016/j.jsb.2016.01.006},
url = {https://www.sciencedirect.com/science/article/pii/S1047847716300053},
author = {Leonardo R. Andrade and Felipe T. Salles and M’hamed Grati and Uri Manor and Bechara Kachar},
keywords = {Extracellular matrix, Electron microscopy, Immunogold-labeling, Tectorial membrane, Tectorins},
abstract = {All inner ear organs possess extracellular matrix appendices over the sensory epithelia that are crucial for their proper function. The tectorial membrane (TM) is a gelatinous acellular membrane located above the hearing sensory epithelium and is composed mostly of type II collagen, and α and β tectorins. TM molecules self-assemble in the endolymph fluid environment, interacting medially with the spiral limbus and distally with the outer hair cell stereocilia. Here, we used immunogold labeling in freeze-substituted mouse cochleae to assess the fine localization of both tectorins in distinct TM regions. We observed that the TM adheres to the spiral limbus through a dense thin matrix enriched in α- and β-tectorin, both likely bound to the membranes of interdental cells. Freeze-etching images revealed that type II collagen fibrils were crosslinked by short thin filaments (4±1.5nm, width), resembling another collagen type protein, or chains of globular elements (15±3.2nm, diameter). Gold-particles for both tectorins also localized adjacent to the type II collagen fibrils, suggesting that these globules might be composed essentially of α- and β-tectorins. Finally, the presence of gold-particles at the TM lower side suggests that the outer hair cell stereocilia membrane has a molecular partner to tectorins, probably stereocilin, allowing the physical connection between the TM and the organ of Corti.}
}
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T.","Grati, M.","Manor, U.","Kachar, B."],"bibdata":{"bibtype":"article","type":"article","title":"Tectorins crosslink type II collagen fibrils and connect the tectorial membrane to the spiral limbus","journal":"Journal of Structural Biology","volume":"194","number":"2","pages":"139-146","year":"2016","issn":"1047-8477","doi":"https://doi.org/10.1016/j.jsb.2016.01.006","url":"https://www.sciencedirect.com/science/article/pii/S1047847716300053","author":[{"firstnames":["Leonardo","R."],"propositions":[],"lastnames":["Andrade"],"suffixes":[]},{"firstnames":["Felipe","T."],"propositions":[],"lastnames":["Salles"],"suffixes":[]},{"firstnames":["M’hamed"],"propositions":[],"lastnames":["Grati"],"suffixes":[]},{"firstnames":["Uri"],"propositions":[],"lastnames":["Manor"],"suffixes":[]},{"firstnames":["Bechara"],"propositions":[],"lastnames":["Kachar"],"suffixes":[]}],"keywords":"Extracellular matrix, Electron microscopy, Immunogold-labeling, Tectorial membrane, Tectorins","abstract":"All inner ear organs possess extracellular matrix appendices over the sensory epithelia that are crucial for their proper function. The tectorial membrane (TM) is a gelatinous acellular membrane located above the hearing sensory epithelium and is composed mostly of type II collagen, and α and β tectorins. TM molecules self-assemble in the endolymph fluid environment, interacting medially with the spiral limbus and distally with the outer hair cell stereocilia. Here, we used immunogold labeling in freeze-substituted mouse cochleae to assess the fine localization of both tectorins in distinct TM regions. We observed that the TM adheres to the spiral limbus through a dense thin matrix enriched in α- and β-tectorin, both likely bound to the membranes of interdental cells. Freeze-etching images revealed that type II collagen fibrils were crosslinked by short thin filaments (4±1.5nm, width), resembling another collagen type protein, or chains of globular elements (15±3.2nm, diameter). Gold-particles for both tectorins also localized adjacent to the type II collagen fibrils, suggesting that these globules might be composed essentially of α- and β-tectorins. Finally, the presence of gold-particles at the TM lower side suggests that the outer hair cell stereocilia membrane has a molecular partner to tectorins, probably stereocilin, allowing the physical connection between the TM and the organ of Corti.","bibtex":"@article{ANDRADE2016139,\r\n title = {Tectorins crosslink type II collagen fibrils and connect the tectorial membrane to the spiral limbus},\r\n journal = {Journal of Structural Biology},\r\n volume = {194},\r\n number = {2},\r\n pages = {139-146},\r\n year = {2016},\r\n issn = {1047-8477},\r\n doi = {https://doi.org/10.1016/j.jsb.2016.01.006},\r\n url = {https://www.sciencedirect.com/science/article/pii/S1047847716300053},\r\n author = {Leonardo R. Andrade and Felipe T. Salles and M’hamed Grati and Uri Manor and Bechara Kachar},\r\n keywords = {Extracellular matrix, Electron microscopy, Immunogold-labeling, Tectorial membrane, Tectorins},\r\n abstract = {All inner ear organs possess extracellular matrix appendices over the sensory epithelia that are crucial for their proper function. The tectorial membrane (TM) is a gelatinous acellular membrane located above the hearing sensory epithelium and is composed mostly of type II collagen, and α and β tectorins. TM molecules self-assemble in the endolymph fluid environment, interacting medially with the spiral limbus and distally with the outer hair cell stereocilia. Here, we used immunogold labeling in freeze-substituted mouse cochleae to assess the fine localization of both tectorins in distinct TM regions. We observed that the TM adheres to the spiral limbus through a dense thin matrix enriched in α- and β-tectorin, both likely bound to the membranes of interdental cells. Freeze-etching images revealed that type II collagen fibrils were crosslinked by short thin filaments (4±1.5nm, width), resembling another collagen type protein, or chains of globular elements (15±3.2nm, diameter). Gold-particles for both tectorins also localized adjacent to the type II collagen fibrils, suggesting that these globules might be composed essentially of α- and β-tectorins. Finally, the presence of gold-particles at the TM lower side suggests that the outer hair cell stereocilia membrane has a molecular partner to tectorins, probably stereocilin, allowing the physical connection between the TM and the organ of Corti.}\r\n}\r\n\r\n","author_short":["Andrade, L. R.","Salles, F. 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