Fugu (Takifugu rubripes) serum GlcNAc-binding lectin is a kalliklectin but has different properties from those of a reported homologue
A 40-kDa lectin with N-acetyl-d-glucosamine-binding ability was purified from the sera of fugu (Takifugu rubripes) by affinity chromatography and subsequent gel filtration. N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lect...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2015-09, Vol.158 (3), p.189-195 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Tsutsui, Shigeyuki Yamamura, Nozomi Yoshida, Takaya Nakamura, Osamu |
| description | A 40-kDa lectin with N-acetyl-d-glucosamine-binding ability was purified from the sera of fugu (Takifugu rubripes) by affinity chromatography and subsequent gel filtration. N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lectin is a homologue of kalliklectin, a novel lectin that was previously found in the flathead teleost Platycephalus indicus and has structural similarity to mammalian plasma kallikreins and coagulation factor XI. This is the second report of a kalliklectin, but the fugu kalliklectin differs in its sugar-binding spectra, intersubunit association and tissue distribution from the previously identified flathead kalliklectin. These findings indicate that kalliklectins vary in properties among fish species. |
| doi_str_mv | 10.1093/jb/mvv033 |
| format | Article |
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N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lectin is a homologue of kalliklectin, a novel lectin that was previously found in the flathead teleost Platycephalus indicus and has structural similarity to mammalian plasma kallikreins and coagulation factor XI. This is the second report of a kalliklectin, but the fugu kalliklectin differs in its sugar-binding spectra, intersubunit association and tissue distribution from the previously identified flathead kalliklectin. These findings indicate that kalliklectins vary in properties among fish species.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvv033</identifier><identifier>PMID: 25796064</identifier><language>eng</language><publisher>England</publisher><subject>Acetylglucosamine - chemistry ; Acetylglucosamine - metabolism ; Amino Acid Sequence ; Animals ; DNA, Complementary - genetics ; Factor XI - chemistry ; Factor XI - metabolism ; Kallikreins - chemistry ; Kallikreins - genetics ; Lectins - blood ; Lectins - chemistry ; Lectins - genetics ; Molecular Sequence Data ; Phylogeny ; Sequence Homology, Amino Acid ; Takifugu - blood ; Takifugu - genetics</subject><ispartof>Journal of biochemistry (Tokyo), 2015-09, Vol.158 (3), p.189-195</ispartof><rights>The Authors 2015. Published by Oxford University Press on behalf of the Japanese Biochemical Society. 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N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lectin is a homologue of kalliklectin, a novel lectin that was previously found in the flathead teleost Platycephalus indicus and has structural similarity to mammalian plasma kallikreins and coagulation factor XI. This is the second report of a kalliklectin, but the fugu kalliklectin differs in its sugar-binding spectra, intersubunit association and tissue distribution from the previously identified flathead kalliklectin. These findings indicate that kalliklectins vary in properties among fish species.</description><subject>Acetylglucosamine - chemistry</subject><subject>Acetylglucosamine - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>DNA, Complementary - genetics</subject><subject>Factor XI - chemistry</subject><subject>Factor XI - metabolism</subject><subject>Kallikreins - chemistry</subject><subject>Kallikreins - genetics</subject><subject>Lectins - blood</subject><subject>Lectins - chemistry</subject><subject>Lectins - genetics</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Sequence Homology, Amino Acid</subject><subject>Takifugu - blood</subject><subject>Takifugu - genetics</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMlOwzAQhi0EgrIceAHkYzkEvDSLjxVikxBcQOIWeRm3bpM42HElXoDnJlULp1n0zafRj9AlJTeUCH67UrftZkM4P0ATWuZFxoqcHqIJIYxmgs0-T9BpjKvtyDg_RicsL0VBitkE_TykRcLTd7l2dtuFpILrIV7jCCG1-LHRr3OdKdcZ1y1wA3pwHXYRS7yWTePW-41KA17KiI2zFgJ0A-6D7yEMDiK2wbd4WPoI2NvxMkDvwwAGL33rG79IcI6OrGwiXOzrGfp4uH-_e8pe3h6f7-YvmZ4RNmRcSFrxShVQEStFycEKw0QBohRKWcqoNLY02lJLDGhWlgBgtGJKi1xIxs_QdOcdv_tKEIe6dVFD08gOfIo1LUlVjV5ORvR6h-rgYwxg6z64VobvmpJ6G3u9UvUu9pG92muTasH8k385818esIHA</recordid><startdate>20150901</startdate><enddate>20150901</enddate><creator>Tsutsui, Shigeyuki</creator><creator>Yamamura, Nozomi</creator><creator>Yoshida, Takaya</creator><creator>Nakamura, Osamu</creator><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>7X8</scope></search><sort><creationdate>20150901</creationdate><title>Fugu (Takifugu rubripes) serum GlcNAc-binding lectin is a kalliklectin but has different properties from those of a reported homologue</title><author>Tsutsui, Shigeyuki ; Yamamura, Nozomi ; Yoshida, Takaya ; Nakamura, Osamu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c402t-39a1838b6e80fa973ef9d296e979bbf121adf7dcf1f0dec277eeedcb2bc959a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Acetylglucosamine - chemistry</topic><topic>Acetylglucosamine - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>DNA, Complementary - genetics</topic><topic>Factor XI - chemistry</topic><topic>Factor XI - metabolism</topic><topic>Kallikreins - chemistry</topic><topic>Kallikreins - genetics</topic><topic>Lectins - blood</topic><topic>Lectins - chemistry</topic><topic>Lectins - genetics</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Sequence Homology, Amino Acid</topic><topic>Takifugu - blood</topic><topic>Takifugu - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsutsui, Shigeyuki</creatorcontrib><creatorcontrib>Yamamura, Nozomi</creatorcontrib><creatorcontrib>Yoshida, Takaya</creatorcontrib><creatorcontrib>Nakamura, Osamu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsutsui, Shigeyuki</au><au>Yamamura, Nozomi</au><au>Yoshida, Takaya</au><au>Nakamura, Osamu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fugu (Takifugu rubripes) serum GlcNAc-binding lectin is a kalliklectin but has different properties from those of a reported homologue</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2015-09-01</date><risdate>2015</risdate><volume>158</volume><issue>3</issue><spage>189</spage><epage>195</epage><pages>189-195</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>A 40-kDa lectin with N-acetyl-d-glucosamine-binding ability was purified from the sera of fugu (Takifugu rubripes) by affinity chromatography and subsequent gel filtration. N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lectin is a homologue of kalliklectin, a novel lectin that was previously found in the flathead teleost Platycephalus indicus and has structural similarity to mammalian plasma kallikreins and coagulation factor XI. This is the second report of a kalliklectin, but the fugu kalliklectin differs in its sugar-binding spectra, intersubunit association and tissue distribution from the previously identified flathead kalliklectin. These findings indicate that kalliklectins vary in properties among fish species.</abstract><cop>England</cop><pmid>25796064</pmid><doi>10.1093/jb/mvv033</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of biochemistry (Tokyo), 2015-09, Vol.158 (3), p.189-195 |
| issn | 0021-924X 1756-2651 |
| language | eng |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Acetylglucosamine - chemistry Acetylglucosamine - metabolism Amino Acid Sequence Animals DNA, Complementary - genetics Factor XI - chemistry Factor XI - metabolism Kallikreins - chemistry Kallikreins - genetics Lectins - blood Lectins - chemistry Lectins - genetics Molecular Sequence Data Phylogeny Sequence Homology, Amino Acid Takifugu - blood Takifugu - genetics |
| title | Fugu (Takifugu rubripes) serum GlcNAc-binding lectin is a kalliklectin but has different properties from those of a reported homologue |
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