Identification of a novel Cochlin isoform in the perilymph: insights to Cochlin function and the pathogenesis of DFNA9
The COCH gene mutated in DFNA9, an autosomal dominant hereditary sensorineural hearing loss and vestibular disorder, encodes Cochlin. Previously, we reported three bovine Cochlin isoforms, p63s, p44s, and p40s, which exhibit significant molecular heterogeneity in vivo. Here we have characterized Coc...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2004-02, Vol.314 (2), p.440-446 |
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| creator | Ikezono, Tetsuo Shindo, Susumu Li, Lishu Omori, Akira Ichinose, Sachiyo Watanabe, Atsushi Kobayashi, Toshimitsu Pawankar, Ruby Yagi, Toshiaki |
| description | The
COCH gene mutated in DFNA9, an autosomal dominant hereditary sensorineural hearing loss and vestibular disorder, encodes Cochlin. Previously, we reported three bovine Cochlin isoforms, p63s, p44s, and p40s, which exhibit significant molecular heterogeneity in vivo. Here we have characterized Cochlin isoforms by generating four isoform-specific anti-Cochlin antibodies. The same three Cochlin isoforms, p63s, p44s, and p40s, were detected in human and cow inner ear tissue; however, p44s and p40s were not detected in perilymph. We identified a novel short 16
kDa isoform in human perilymph and a 18–23
kDa isoform in cow perilymph, named Cochlin-tomoprotein (CTP), corresponding to the N-terminus of full-length Cochlin (p63s) and the LCCL domain. Notably, CTP contains all of the known mutation sites associated with DFNA9. The pathogenesis of DFNA9 is not fully clarified as yet, and this novel perilymph-associated CTP isoform might provide mechanistic clues to how mutations in the
COCH gene damage the inner ear function. |
| doi_str_mv | 10.1016/j.bbrc.2003.12.106 |
| format | Article |
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COCH gene mutated in DFNA9, an autosomal dominant hereditary sensorineural hearing loss and vestibular disorder, encodes Cochlin. Previously, we reported three bovine Cochlin isoforms, p63s, p44s, and p40s, which exhibit significant molecular heterogeneity in vivo. Here we have characterized Cochlin isoforms by generating four isoform-specific anti-Cochlin antibodies. The same three Cochlin isoforms, p63s, p44s, and p40s, were detected in human and cow inner ear tissue; however, p44s and p40s were not detected in perilymph. We identified a novel short 16
kDa isoform in human perilymph and a 18–23
kDa isoform in cow perilymph, named Cochlin-tomoprotein (CTP), corresponding to the N-terminus of full-length Cochlin (p63s) and the LCCL domain. Notably, CTP contains all of the known mutation sites associated with DFNA9. The pathogenesis of DFNA9 is not fully clarified as yet, and this novel perilymph-associated CTP isoform might provide mechanistic clues to how mutations in the
COCH gene damage the inner ear function.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2003.12.106</identifier><identifier>PMID: 14733925</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Blotting, Western ; Bos ; Cattle ; COCH gene ; Cochlin ; CTP ; Deafness ; DFNA9 ; Ear, Inner - metabolism ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Extracellular Matrix Proteins ; Hereditary hearing impairment ; Human ; Humans ; Inner ear ; Isoform ; Models, Genetic ; Molecular Sequence Data ; Mutation ; Peptides - chemistry ; Perilymph - metabolism ; Protein Isoforms ; Protein Structure, Tertiary ; Proteins - chemistry ; Sequence Homology, Amino Acid ; Time Factors</subject><ispartof>Biochemical and biophysical research communications, 2004-02, Vol.314 (2), p.440-446</ispartof><rights>2003 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-a71f82d2c02dbf34b4d4539717a7ddfcaeeb410708a09e526bc20fd09b9344123</citedby><cites>FETCH-LOGICAL-c449t-a71f82d2c02dbf34b4d4539717a7ddfcaeeb410708a09e526bc20fd09b9344123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2003.12.106$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14733925$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ikezono, Tetsuo</creatorcontrib><creatorcontrib>Shindo, Susumu</creatorcontrib><creatorcontrib>Li, Lishu</creatorcontrib><creatorcontrib>Omori, Akira</creatorcontrib><creatorcontrib>Ichinose, Sachiyo</creatorcontrib><creatorcontrib>Watanabe, Atsushi</creatorcontrib><creatorcontrib>Kobayashi, Toshimitsu</creatorcontrib><creatorcontrib>Pawankar, Ruby</creatorcontrib><creatorcontrib>Yagi, Toshiaki</creatorcontrib><title>Identification of a novel Cochlin isoform in the perilymph: insights to Cochlin function and the pathogenesis of DFNA9</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The
COCH gene mutated in DFNA9, an autosomal dominant hereditary sensorineural hearing loss and vestibular disorder, encodes Cochlin. Previously, we reported three bovine Cochlin isoforms, p63s, p44s, and p40s, which exhibit significant molecular heterogeneity in vivo. Here we have characterized Cochlin isoforms by generating four isoform-specific anti-Cochlin antibodies. The same three Cochlin isoforms, p63s, p44s, and p40s, were detected in human and cow inner ear tissue; however, p44s and p40s were not detected in perilymph. We identified a novel short 16
kDa isoform in human perilymph and a 18–23
kDa isoform in cow perilymph, named Cochlin-tomoprotein (CTP), corresponding to the N-terminus of full-length Cochlin (p63s) and the LCCL domain. Notably, CTP contains all of the known mutation sites associated with DFNA9. The pathogenesis of DFNA9 is not fully clarified as yet, and this novel perilymph-associated CTP isoform might provide mechanistic clues to how mutations in the
COCH gene damage the inner ear function.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Bos</subject><subject>Cattle</subject><subject>COCH gene</subject><subject>Cochlin</subject><subject>CTP</subject><subject>Deafness</subject><subject>DFNA9</subject><subject>Ear, Inner - metabolism</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Extracellular Matrix Proteins</subject><subject>Hereditary hearing impairment</subject><subject>Human</subject><subject>Humans</subject><subject>Inner ear</subject><subject>Isoform</subject><subject>Models, Genetic</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Peptides - chemistry</subject><subject>Perilymph - metabolism</subject><subject>Protein Isoforms</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>Time Factors</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0EoqHwBzigPXHbdPyR3RhxqVJKK1XtBSRultcedx3t2sF2IvXfs0siuLWnGb165jnMS8hHCksKtLnYLrsumSUD4EvKpqx5RRYUJNSMgnhNFgDQ1EzSX2fkXc5bAEpFI9-SMypaziVbLcjh1mIo3nmji4-hiq7SVYgHHKpNNP3gQ-VzdDGN1bSWHqsdJj88jbv-y5Rk_9iXXJX4j3b7YP6adLBHXpc-PmLA7POsv7q-v5TvyRunh4wfTvOc_Lz-9mNzU989fL_dXN7VRghZat1St2aWGWC2c1x0wooVly1tdWutMxqxExRaWGuQuGJNZxg4C7KTXAjK-Dn5fPTuUvy9x1zU6LPBYdAB4z6rNVDgct28CNJWCsGbdgLZETQp5pzQqV3yo05PioKaa1FbNdei5loUZVM22z-d7PtuRPv_5NTDBHw9Ajg94-AxqWw8BoPWJzRF2eif8_8BYbie2w</recordid><startdate>20040206</startdate><enddate>20040206</enddate><creator>Ikezono, Tetsuo</creator><creator>Shindo, Susumu</creator><creator>Li, Lishu</creator><creator>Omori, Akira</creator><creator>Ichinose, Sachiyo</creator><creator>Watanabe, Atsushi</creator><creator>Kobayashi, Toshimitsu</creator><creator>Pawankar, Ruby</creator><creator>Yagi, Toshiaki</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040206</creationdate><title>Identification of a novel Cochlin isoform in the perilymph: insights to Cochlin function and the pathogenesis of DFNA9</title><author>Ikezono, Tetsuo ; Shindo, Susumu ; Li, Lishu ; Omori, Akira ; Ichinose, Sachiyo ; Watanabe, Atsushi ; Kobayashi, Toshimitsu ; Pawankar, Ruby ; Yagi, Toshiaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c449t-a71f82d2c02dbf34b4d4539717a7ddfcaeeb410708a09e526bc20fd09b9344123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Bos</topic><topic>Cattle</topic><topic>COCH gene</topic><topic>Cochlin</topic><topic>CTP</topic><topic>Deafness</topic><topic>DFNA9</topic><topic>Ear, Inner - metabolism</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Extracellular Matrix Proteins</topic><topic>Hereditary hearing impairment</topic><topic>Human</topic><topic>Humans</topic><topic>Inner ear</topic><topic>Isoform</topic><topic>Models, Genetic</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Peptides - chemistry</topic><topic>Perilymph - metabolism</topic><topic>Protein Isoforms</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ikezono, Tetsuo</creatorcontrib><creatorcontrib>Shindo, Susumu</creatorcontrib><creatorcontrib>Li, Lishu</creatorcontrib><creatorcontrib>Omori, Akira</creatorcontrib><creatorcontrib>Ichinose, Sachiyo</creatorcontrib><creatorcontrib>Watanabe, Atsushi</creatorcontrib><creatorcontrib>Kobayashi, Toshimitsu</creatorcontrib><creatorcontrib>Pawankar, Ruby</creatorcontrib><creatorcontrib>Yagi, Toshiaki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ikezono, Tetsuo</au><au>Shindo, Susumu</au><au>Li, Lishu</au><au>Omori, Akira</au><au>Ichinose, Sachiyo</au><au>Watanabe, Atsushi</au><au>Kobayashi, Toshimitsu</au><au>Pawankar, Ruby</au><au>Yagi, Toshiaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a novel Cochlin isoform in the perilymph: insights to Cochlin function and the pathogenesis of DFNA9</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2004-02-06</date><risdate>2004</risdate><volume>314</volume><issue>2</issue><spage>440</spage><epage>446</epage><pages>440-446</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The
COCH gene mutated in DFNA9, an autosomal dominant hereditary sensorineural hearing loss and vestibular disorder, encodes Cochlin. Previously, we reported three bovine Cochlin isoforms, p63s, p44s, and p40s, which exhibit significant molecular heterogeneity in vivo. Here we have characterized Cochlin isoforms by generating four isoform-specific anti-Cochlin antibodies. The same three Cochlin isoforms, p63s, p44s, and p40s, were detected in human and cow inner ear tissue; however, p44s and p40s were not detected in perilymph. We identified a novel short 16
kDa isoform in human perilymph and a 18–23
kDa isoform in cow perilymph, named Cochlin-tomoprotein (CTP), corresponding to the N-terminus of full-length Cochlin (p63s) and the LCCL domain. Notably, CTP contains all of the known mutation sites associated with DFNA9. The pathogenesis of DFNA9 is not fully clarified as yet, and this novel perilymph-associated CTP isoform might provide mechanistic clues to how mutations in the
COCH gene damage the inner ear function.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14733925</pmid><doi>10.1016/j.bbrc.2003.12.106</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2004-02, Vol.314 (2), p.440-446 |
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| subjects | Amino Acid Sequence Animals Blotting, Western Bos Cattle COCH gene Cochlin CTP Deafness DFNA9 Ear, Inner - metabolism Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Extracellular Matrix Proteins Hereditary hearing impairment Human Humans Inner ear Isoform Models, Genetic Molecular Sequence Data Mutation Peptides - chemistry Perilymph - metabolism Protein Isoforms Protein Structure, Tertiary Proteins - chemistry Sequence Homology, Amino Acid Time Factors |
| title | Identification of a novel Cochlin isoform in the perilymph: insights to Cochlin function and the pathogenesis of DFNA9 |
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