Characterization of a Novel Proteinous Toxin from Sea Anemone Actineria villosa
The sea anemone Actineria villosa expresses a lethal protein toxin. We isolated a novel 120-kDa protein, Avt120, from partially purified toxin and found it to possess extremely strong lethal activity. The 3,453-bp Avt120 gene translates to a 995-amino acid protein. The 50% lethal dose (LD 50 ) of pu...
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| Veröffentlicht in: | Protein Journal 2011-08, Vol.30 (6), p.422-428 |
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| creator | Uechi, Gen-ichiro Toma, Hiromu Arakawa, Takeshi Sato, Yoshiya |
| description | The sea anemone
Actineria villosa
expresses a lethal protein toxin. We isolated a novel 120-kDa protein, Avt120, from partially purified toxin and found it to possess extremely strong lethal activity. The 3,453-bp Avt120 gene translates to a 995-amino acid protein. The 50% lethal dose (LD
50
) of purified Avt120 in mice was 85.17 ng. Among several tested cell lines, Colo205 cells were most sensitive to Avt120: 50% of them were damaged by 38.4 ng/mL Avt120. Avt120 exerted ATP degradation activity (10 μmol ATP h
−1
mg
−1
), which was strongly inhibited by ganglioside GM1 to decrease the cytotoxicity of Avt120. |
| doi_str_mv | 10.1007/s10930-011-9347-8 |
| format | Article |
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Actineria villosa
expresses a lethal protein toxin. We isolated a novel 120-kDa protein, Avt120, from partially purified toxin and found it to possess extremely strong lethal activity. The 3,453-bp Avt120 gene translates to a 995-amino acid protein. The 50% lethal dose (LD
50
) of purified Avt120 in mice was 85.17 ng. Among several tested cell lines, Colo205 cells were most sensitive to Avt120: 50% of them were damaged by 38.4 ng/mL Avt120. Avt120 exerted ATP degradation activity (10 μmol ATP h
−1
mg
−1
), which was strongly inhibited by ganglioside GM1 to decrease the cytotoxicity of Avt120.</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1573-4943</identifier><identifier>EISSN: 1875-8355</identifier><identifier>DOI: 10.1007/s10930-011-9347-8</identifier><identifier>PMID: 21769623</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Amino acids ; Animal Anatomy ; Animals ; ATP ; Base Sequence ; Biochemistry ; Biodegradation ; Bioorganic Chemistry ; Cell Death - drug effects ; Cercopithecus aethiops ; Chemistry ; Chemistry and Materials Science ; Cnidarian Venoms - chemistry ; Cnidarian Venoms - isolation & purification ; Cnidarian Venoms - metabolism ; Cnidarian Venoms - toxicity ; Cytotoxicity ; Electrophoresis, Polyacrylamide Gel ; Ethylenediaminetetraacetic acid ; Gangliosides ; Gangliosides - metabolism ; HEK293 Cells ; Histology ; HL-60 Cells ; Humans ; Lethal Dose 50 ; Marine ; Marine biology ; Medical colleges ; Mice ; Mice, Inbred ICR ; Molecular Sequence Data ; Morphology ; NIH 3T3 Cells ; Organic Chemistry ; Proteins ; Sea Anemones - chemistry ; Sequence Alignment ; Toxins ; Vero Cells</subject><ispartof>Protein Journal, 2011-08, Vol.30 (6), p.422-428</ispartof><rights>Springer Science+Business Media, LLC 2011</rights><rights>COPYRIGHT 2011 Springer</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-83a9057619d62c6f047b6cf13700ee77735ee7c2b03901f1898b760eb5989ccc3</citedby><cites>FETCH-LOGICAL-c557t-83a9057619d62c6f047b6cf13700ee77735ee7c2b03901f1898b760eb5989ccc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10930-011-9347-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10930-011-9347-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21769623$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Uechi, Gen-ichiro</creatorcontrib><creatorcontrib>Toma, Hiromu</creatorcontrib><creatorcontrib>Arakawa, Takeshi</creatorcontrib><creatorcontrib>Sato, Yoshiya</creatorcontrib><title>Characterization of a Novel Proteinous Toxin from Sea Anemone Actineria villosa</title><title>Protein Journal</title><addtitle>Protein J</addtitle><addtitle>Protein J</addtitle><description>The sea anemone
Actineria villosa
expresses a lethal protein toxin. We isolated a novel 120-kDa protein, Avt120, from partially purified toxin and found it to possess extremely strong lethal activity. The 3,453-bp Avt120 gene translates to a 995-amino acid protein. The 50% lethal dose (LD
50
) of purified Avt120 in mice was 85.17 ng. Among several tested cell lines, Colo205 cells were most sensitive to Avt120: 50% of them were damaged by 38.4 ng/mL Avt120. Avt120 exerted ATP degradation activity (10 μmol ATP h
−1
mg
−1
), which was strongly inhibited by ganglioside GM1 to decrease the cytotoxicity of Avt120.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animal Anatomy</subject><subject>Animals</subject><subject>ATP</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biodegradation</subject><subject>Bioorganic Chemistry</subject><subject>Cell Death - drug effects</subject><subject>Cercopithecus aethiops</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cnidarian Venoms - chemistry</subject><subject>Cnidarian Venoms - isolation & purification</subject><subject>Cnidarian Venoms - metabolism</subject><subject>Cnidarian Venoms - toxicity</subject><subject>Cytotoxicity</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Gangliosides</subject><subject>Gangliosides - metabolism</subject><subject>HEK293 Cells</subject><subject>Histology</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>Lethal Dose 50</subject><subject>Marine</subject><subject>Marine biology</subject><subject>Medical colleges</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Molecular Sequence Data</subject><subject>Morphology</subject><subject>NIH 3T3 Cells</subject><subject>Organic Chemistry</subject><subject>Proteins</subject><subject>Sea Anemones - chemistry</subject><subject>Sequence Alignment</subject><subject>Toxins</subject><subject>Vero Cells</subject><issn>1572-3887</issn><issn>1573-4943</issn><issn>1875-8355</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp1kVtPFTEUhRuiAQR_gC-kwRdfBnuZ3h5PTrwlREzE56bTs4slMy20c4j66-1xQCPR9GE37bd2V_dC6AUlZ5QQ9bpSYjjpCKWd4b3q9B46pELxrjc9f_JrzzqutTpAz2q9JoRpo9g-OmBUSSMZP0QX66-uOD9DiT_cHHPCOWCHP-Y7GPGnkmeIKW8rvszfYsKh5Al_BodXCaacAK_8HFPTOnwXxzFXd4yeBjdWeH5fj9CXt28u1--784t3H9ar884LoeZOc2eIUJKajWReBtKrQfpAuSIEQCnFRSueDYQbQgPVRg9KEhiE0cZ7z4_Qq6XvTcm3W6iznWL1MI4uQfNrKaHKCEl73dDTR-h13pbU3FmtiRFtiKxBLxfoyo1gYwp5bmPZ9bQrRaUQ7WHeqLN_UG1tYIq-DSTEdv6XgC4CX3KtBYK9KXFy5XszaHcZ2iVD2zK0uwztzu_Jvd_tMMHmt-IhtAawBajtKl1B-fOh_3f9CYFWo5w</recordid><startdate>20110801</startdate><enddate>20110801</enddate><creator>Uechi, Gen-ichiro</creator><creator>Toma, Hiromu</creator><creator>Arakawa, Takeshi</creator><creator>Sato, Yoshiya</creator><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TK</scope><scope>7TM</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>20110801</creationdate><title>Characterization of a Novel Proteinous Toxin from Sea Anemone Actineria villosa</title><author>Uechi, Gen-ichiro ; Toma, Hiromu ; Arakawa, Takeshi ; Sato, Yoshiya</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-83a9057619d62c6f047b6cf13700ee77735ee7c2b03901f1898b760eb5989ccc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adenosine Triphosphate - 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chemistry</topic><topic>Sequence Alignment</topic><topic>Toxins</topic><topic>Vero Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Uechi, Gen-ichiro</creatorcontrib><creatorcontrib>Toma, Hiromu</creatorcontrib><creatorcontrib>Arakawa, Takeshi</creatorcontrib><creatorcontrib>Sato, Yoshiya</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Science Journals</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Protein Journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Uechi, Gen-ichiro</au><au>Toma, Hiromu</au><au>Arakawa, Takeshi</au><au>Sato, Yoshiya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a Novel Proteinous Toxin from Sea Anemone Actineria villosa</atitle><jtitle>Protein Journal</jtitle><stitle>Protein J</stitle><addtitle>Protein J</addtitle><date>2011-08-01</date><risdate>2011</risdate><volume>30</volume><issue>6</issue><spage>422</spage><epage>428</epage><pages>422-428</pages><issn>1572-3887</issn><eissn>1573-4943</eissn><eissn>1875-8355</eissn><abstract>The sea anemone
Actineria villosa
expresses a lethal protein toxin. We isolated a novel 120-kDa protein, Avt120, from partially purified toxin and found it to possess extremely strong lethal activity. The 3,453-bp Avt120 gene translates to a 995-amino acid protein. The 50% lethal dose (LD
50
) of purified Avt120 in mice was 85.17 ng. Among several tested cell lines, Colo205 cells were most sensitive to Avt120: 50% of them were damaged by 38.4 ng/mL Avt120. Avt120 exerted ATP degradation activity (10 μmol ATP h
−1
mg
−1
), which was strongly inhibited by ganglioside GM1 to decrease the cytotoxicity of Avt120.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>21769623</pmid><doi>10.1007/s10930-011-9347-8</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Protein Journal, 2011-08, Vol.30 (6), p.422-428 |
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| language | eng |
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| subjects | Adenosine Triphosphate - metabolism Amino Acid Sequence Amino acids Animal Anatomy Animals ATP Base Sequence Biochemistry Biodegradation Bioorganic Chemistry Cell Death - drug effects Cercopithecus aethiops Chemistry Chemistry and Materials Science Cnidarian Venoms - chemistry Cnidarian Venoms - isolation & purification Cnidarian Venoms - metabolism Cnidarian Venoms - toxicity Cytotoxicity Electrophoresis, Polyacrylamide Gel Ethylenediaminetetraacetic acid Gangliosides Gangliosides - metabolism HEK293 Cells Histology HL-60 Cells Humans Lethal Dose 50 Marine Marine biology Medical colleges Mice Mice, Inbred ICR Molecular Sequence Data Morphology NIH 3T3 Cells Organic Chemistry Proteins Sea Anemones - chemistry Sequence Alignment Toxins Vero Cells |
| title | Characterization of a Novel Proteinous Toxin from Sea Anemone Actineria villosa |
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