Abstract
Cochlin is colocalized with type II collagen in the extracellular matrix of cochlea and has been suggested to interact with this collagen. Here we show that the second von Willebrand type A domain of cochlin has affinity for type II collagen, as well as type I and type IV collagens whereas the LCCL-domain of cochlin has no affinity for these proteins. The implications of these findings for the mechanism whereby cochlin mutations cause the dominant negative DFNA9-type hearing loss are discussed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Line
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Cochlea / metabolism
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Collagen Type I / metabolism*
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Collagen Type II / metabolism*
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Collagen Type IV / metabolism*
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Extracellular Matrix / metabolism
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Extracellular Matrix Proteins
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Hearing Loss / genetics
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Hearing Loss / metabolism
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Humans
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Protein Structure, Tertiary / genetics
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Proteins / chemistry
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Proteins / genetics
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Proteins / metabolism*
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von Willebrand Factor / chemistry
Substances
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COCH protein, human
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Collagen Type I
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Collagen Type II
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Collagen Type IV
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Extracellular Matrix Proteins
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Proteins
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von Willebrand Factor