Characterization of pericentrin isoforms in vivo
Pericentrin was first identified as a mouse centrosomal protein and is now referred to as pericentrin A. A larger homologous protein in humans with a C-terminal calmodulin-binding domain was later identified as pericentrin B. Pericentrin has been shown to be one of the key components in ciliogenesis...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-12, Vol.351 (3), p.745-749 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Miyoshi, Ko Asanuma, Masato Miyazaki, Ikuko Matsuzaki, Shinsuke Tohyama, Masaya Ogawa, Norio |
| description | Pericentrin was first identified as a mouse centrosomal protein and is now referred to as pericentrin A. A larger homologous protein in humans with a C-terminal calmodulin-binding domain was later identified as pericentrin B. Pericentrin has been shown to be one of the key components in ciliogenesis, but
in vivo pericentrin products have remained ambiguous. Here we characterized pericentrin isoforms in mice. Two pericentrin transcripts of 9.5 and 6.9
kb were recognized on the mouse tissue Northern blots, while a cRNA probe for a 5′-terminal sequence shared by pericentrin A and B failed to hybridize to the 6.9-kb message. Two pericentrin cDNAs were identified, which encoded pericentrin B and a novel isoform, pericentrin S, sharing with pericentrin B a C-terminal calmodulin-binding motif. Three pericentrin proteins of 360, 255, and 250
kDa revealed by immunoprecipitation analysis were thought to correspond to pericentrin B, pericentrin S, and an unknown N-terminal product. |
| doi_str_mv | 10.1016/j.bbrc.2006.10.101 |
| format | Article |
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in vivo pericentrin products have remained ambiguous. Here we characterized pericentrin isoforms in mice. Two pericentrin transcripts of 9.5 and 6.9
kb were recognized on the mouse tissue Northern blots, while a cRNA probe for a 5′-terminal sequence shared by pericentrin A and B failed to hybridize to the 6.9-kb message. Two pericentrin cDNAs were identified, which encoded pericentrin B and a novel isoform, pericentrin S, sharing with pericentrin B a C-terminal calmodulin-binding motif. Three pericentrin proteins of 360, 255, and 250
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in vivo pericentrin products have remained ambiguous. Here we characterized pericentrin isoforms in mice. Two pericentrin transcripts of 9.5 and 6.9
kb were recognized on the mouse tissue Northern blots, while a cRNA probe for a 5′-terminal sequence shared by pericentrin A and B failed to hybridize to the 6.9-kb message. Two pericentrin cDNAs were identified, which encoded pericentrin B and a novel isoform, pericentrin S, sharing with pericentrin B a C-terminal calmodulin-binding motif. Three pericentrin proteins of 360, 255, and 250
kDa revealed by immunoprecipitation analysis were thought to correspond to pericentrin B, pericentrin S, and an unknown N-terminal product.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens - chemistry</subject><subject>Antigens - physiology</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Centrosome</subject><subject>Cilium</subject><subject>Isoform</subject><subject>Kendrin</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Organ Specificity</subject><subject>Pericentrin</subject><subject>Protein Binding</subject><subject>Tissue Distribution</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UE1LAzEQDaJorf4BD7Inb7tOPprdgBcpfkHBSw_eQppOMKW7qcm2oL_elF3w5lxm5s17D-YRckOhokDl_aZaraKtGICsBuyETCgoKBkFcUomkC8lU_TjglymtAGgVEh1Ti5oDY3gjZwQmH-aaGyP0f-Y3oeuCK7Y5c1i10ffFT4FF2Kbijwf_CFckTNntgmvxz4ly-en5fy1XLy_vM0fF6UVDPrScSka1wgrODDBa-QUc9VSCGlnxiGjTNSinjElsOYuo87VCMI0SjHHp-RusN3F8LXH1OvWJ4vbrekw7JOmasaYBJ6JbCDaGFKK6PQu-tbEb01BH2PSG32MSR9jGrEsuh3d96sW13-SMZdMeBgImF88eIw6WY-dxbWPaHu9Dv4__1-Z-XfC</recordid><startdate>20061222</startdate><enddate>20061222</enddate><creator>Miyoshi, Ko</creator><creator>Asanuma, Masato</creator><creator>Miyazaki, Ikuko</creator><creator>Matsuzaki, Shinsuke</creator><creator>Tohyama, Masaya</creator><creator>Ogawa, Norio</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></search><sort><creationdate>20061222</creationdate><title>Characterization of pericentrin isoforms in vivo</title><author>Miyoshi, Ko ; Asanuma, Masato ; Miyazaki, Ikuko ; Matsuzaki, Shinsuke ; Tohyama, Masaya ; Ogawa, Norio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-f3648f84c4302437e31eeee76446c5afe21247475294e73f46cff7e04a8992f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens - chemistry</topic><topic>Antigens - physiology</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Centrosome</topic><topic>Cilium</topic><topic>Isoform</topic><topic>Kendrin</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Organ Specificity</topic><topic>Pericentrin</topic><topic>Protein Binding</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miyoshi, Ko</creatorcontrib><creatorcontrib>Asanuma, Masato</creatorcontrib><creatorcontrib>Miyazaki, Ikuko</creatorcontrib><creatorcontrib>Matsuzaki, Shinsuke</creatorcontrib><creatorcontrib>Tohyama, Masaya</creatorcontrib><creatorcontrib>Ogawa, Norio</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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyoshi, Ko</au><au>Asanuma, Masato</au><au>Miyazaki, Ikuko</au><au>Matsuzaki, Shinsuke</au><au>Tohyama, Masaya</au><au>Ogawa, Norio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of pericentrin isoforms in vivo</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-12-22</date><risdate>2006</risdate><volume>351</volume><issue>3</issue><spage>745</spage><epage>749</epage><pages>745-749</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Pericentrin was first identified as a mouse centrosomal protein and is now referred to as pericentrin A. A larger homologous protein in humans with a C-terminal calmodulin-binding domain was later identified as pericentrin B. Pericentrin has been shown to be one of the key components in ciliogenesis, but
in vivo pericentrin products have remained ambiguous. Here we characterized pericentrin isoforms in mice. Two pericentrin transcripts of 9.5 and 6.9
kb were recognized on the mouse tissue Northern blots, while a cRNA probe for a 5′-terminal sequence shared by pericentrin A and B failed to hybridize to the 6.9-kb message. Two pericentrin cDNAs were identified, which encoded pericentrin B and a novel isoform, pericentrin S, sharing with pericentrin B a C-terminal calmodulin-binding motif. Three pericentrin proteins of 360, 255, and 250
kDa revealed by immunoprecipitation analysis were thought to correspond to pericentrin B, pericentrin S, and an unknown N-terminal product.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17084386</pmid><doi>10.1016/j.bbrc.2006.10.101</doi><tpages>5</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Antigens - chemistry Antigens - physiology Base Sequence Binding Sites Centrosome Cilium Isoform Kendrin Mice Molecular Sequence Data Organ Specificity Pericentrin Protein Binding Tissue Distribution |
| title | Characterization of pericentrin isoforms in vivo |
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