Effects of prodigiosin family compounds from Pseudoalteromonas sp. 1020R on the activities of protein phosphatases and protein kinases
Pseudoalteromonas sp. strain 1020R produces prodigiosin and its closely related congeners, which differ in the length of their alkyl side chains. These red-pigmented compounds were found to exhibit cytotoxicity against human leukemia cell lines. The compounds also showed dose-dependent inhibitory ef...
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| Veröffentlicht in: | Journal of enzyme inhibition and medicinal chemistry 2015-08, Vol.30 (4), p.533-538 |
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| container_title | Journal of enzyme inhibition and medicinal chemistry |
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| creator | Soliev, Azamjon B. Hosokawa, Kakushi Enomoto, Keiichi |
| description | Pseudoalteromonas sp. strain 1020R produces prodigiosin and its closely related congeners, which differ in the length of their alkyl side chains. These red-pigmented compounds were found to exhibit cytotoxicity against human leukemia cell lines. The compounds also showed dose-dependent inhibitory effects on protein phosphatase 2A and protein tyrosine phosphatase 1B (PTP1B), while remaining relatively inactive against protein kinases, including protein tyrosine kinase, Ca
2+
/calmodulin-dependent protein kinase and protein kinases A and C. Comparative studies of the individual pigmented compounds on PTP1B inhibition showed that as the chain length of the alkyl group at the C-3 position of the compound increased, the inhibitory effect on PTP1B decreased. These results suggest that protein phosphatases but not protein kinases might be involved in the cytotoxicity of the prodigiosin family of compounds against malignant cells. |
| doi_str_mv | 10.3109/14756366.2014.951347 |
| format | Article |
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2+
/calmodulin-dependent protein kinase and protein kinases A and C. Comparative studies of the individual pigmented compounds on PTP1B inhibition showed that as the chain length of the alkyl group at the C-3 position of the compound increased, the inhibitory effect on PTP1B decreased. These results suggest that protein phosphatases but not protein kinases might be involved in the cytotoxicity of the prodigiosin family of compounds against malignant cells.</description><identifier>ISSN: 1475-6366</identifier><identifier>EISSN: 1475-6374</identifier><identifier>DOI: 10.3109/14756366.2014.951347</identifier><identifier>PMID: 25373498</identifier><language>eng</language><publisher>England: Informa Healthcare</publisher><subject>Cell Line, Tumor ; Cytotoxicity ; enzyme inhibition ; Enzyme Inhibitors - isolation & purification ; Enzyme Inhibitors - pharmacology ; Humans ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Prodigiosin - isolation & purification ; Prodigiosin - pharmacology ; Protein Kinases - drug effects ; Pseudoalteromonas - chemistry ; structure-activity relationship</subject><ispartof>Journal of enzyme inhibition and medicinal chemistry, 2015-08, Vol.30 (4), p.533-538</ispartof><rights>2014 Informa UK Ltd. All rights reserved: reproduction in whole or part not permitted 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c363t-6e4005036d3d88e859d83965835cbe6b068e68b9498c421d606e7f5b8def25503</citedby><cites>FETCH-LOGICAL-c363t-6e4005036d3d88e859d83965835cbe6b068e68b9498c421d606e7f5b8def25503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25373498$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Soliev, Azamjon B.</creatorcontrib><creatorcontrib>Hosokawa, Kakushi</creatorcontrib><creatorcontrib>Enomoto, Keiichi</creatorcontrib><title>Effects of prodigiosin family compounds from Pseudoalteromonas sp. 1020R on the activities of protein phosphatases and protein kinases</title><title>Journal of enzyme inhibition and medicinal chemistry</title><addtitle>J Enzyme Inhib Med Chem</addtitle><description>Pseudoalteromonas sp. strain 1020R produces prodigiosin and its closely related congeners, which differ in the length of their alkyl side chains. These red-pigmented compounds were found to exhibit cytotoxicity against human leukemia cell lines. The compounds also showed dose-dependent inhibitory effects on protein phosphatase 2A and protein tyrosine phosphatase 1B (PTP1B), while remaining relatively inactive against protein kinases, including protein tyrosine kinase, Ca
2+
/calmodulin-dependent protein kinase and protein kinases A and C. Comparative studies of the individual pigmented compounds on PTP1B inhibition showed that as the chain length of the alkyl group at the C-3 position of the compound increased, the inhibitory effect on PTP1B decreased. These results suggest that protein phosphatases but not protein kinases might be involved in the cytotoxicity of the prodigiosin family of compounds against malignant cells.</description><subject>Cell Line, Tumor</subject><subject>Cytotoxicity</subject><subject>enzyme inhibition</subject><subject>Enzyme Inhibitors - isolation & purification</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Humans</subject><subject>Phosphoprotein Phosphatases - antagonists & inhibitors</subject><subject>Prodigiosin - isolation & purification</subject><subject>Prodigiosin - pharmacology</subject><subject>Protein Kinases - drug effects</subject><subject>Pseudoalteromonas - chemistry</subject><subject>structure-activity relationship</subject><issn>1475-6366</issn><issn>1475-6374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9Uctu1DAUtRCIPuAPEPKSzQx-x1khVBWoVKkVKmvL8YMxJHawnaL5gX43jqYzS1a-Pvc8ZB8A3mG0pRj1HzHruKBCbAnCbNtzTFn3Apyv8EbQjr08zUKcgYtSfiFEMMHsNTgjnHaU9fIcPF1770wtMHk452TDz5BKiNDrKYx7aNI0pyXaAn1OE7wvbrFJj9W1W4q6wDJvIUYEfYcpwrpzUJsaHkMN7mhZXbObd6nMO111abiO9rT4HeKKvQGvvB6Le_t8XoIfX64frr5tbu--3lx9vt0YKmjdCMcQ4ogKS62UTvLeStoLLik3gxMDEtIJOfTtaYYRbAUSrvN8kNZ5wpvwEnw4-Lb8P4srVU2hGDeOOrq0FIVF3xEsWUcalR2oJqdSsvNqzmHSea8wUmsD6tiAWhtQhwaa7P1zwjJMzp5Exy9vhE8HQog-5Un_TXm0qur9mLLPOppQVvv_RPwDNpGWaw</recordid><startdate>20150801</startdate><enddate>20150801</enddate><creator>Soliev, Azamjon B.</creator><creator>Hosokawa, Kakushi</creator><creator>Enomoto, Keiichi</creator><general>Informa Healthcare</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>7X8</scope></search><sort><creationdate>20150801</creationdate><title>Effects of prodigiosin family compounds from Pseudoalteromonas sp. 1020R on the activities of protein phosphatases and protein kinases</title><author>Soliev, Azamjon B. ; Hosokawa, Kakushi ; Enomoto, Keiichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c363t-6e4005036d3d88e859d83965835cbe6b068e68b9498c421d606e7f5b8def25503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Cell Line, Tumor</topic><topic>Cytotoxicity</topic><topic>enzyme inhibition</topic><topic>Enzyme Inhibitors - isolation & purification</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Humans</topic><topic>Phosphoprotein Phosphatases - antagonists & inhibitors</topic><topic>Prodigiosin - isolation & purification</topic><topic>Prodigiosin - pharmacology</topic><topic>Protein Kinases - drug effects</topic><topic>Pseudoalteromonas - chemistry</topic><topic>structure-activity relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Soliev, Azamjon B.</creatorcontrib><creatorcontrib>Hosokawa, Kakushi</creatorcontrib><creatorcontrib>Enomoto, Keiichi</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 enzyme inhibition and medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Soliev, Azamjon B.</au><au>Hosokawa, Kakushi</au><au>Enomoto, Keiichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of prodigiosin family compounds from Pseudoalteromonas sp. 1020R on the activities of protein phosphatases and protein kinases</atitle><jtitle>Journal of enzyme inhibition and medicinal chemistry</jtitle><addtitle>J Enzyme Inhib Med Chem</addtitle><date>2015-08-01</date><risdate>2015</risdate><volume>30</volume><issue>4</issue><spage>533</spage><epage>538</epage><pages>533-538</pages><issn>1475-6366</issn><eissn>1475-6374</eissn><abstract>Pseudoalteromonas sp. strain 1020R produces prodigiosin and its closely related congeners, which differ in the length of their alkyl side chains. These red-pigmented compounds were found to exhibit cytotoxicity against human leukemia cell lines. The compounds also showed dose-dependent inhibitory effects on protein phosphatase 2A and protein tyrosine phosphatase 1B (PTP1B), while remaining relatively inactive against protein kinases, including protein tyrosine kinase, Ca
2+
/calmodulin-dependent protein kinase and protein kinases A and C. Comparative studies of the individual pigmented compounds on PTP1B inhibition showed that as the chain length of the alkyl group at the C-3 position of the compound increased, the inhibitory effect on PTP1B decreased. These results suggest that protein phosphatases but not protein kinases might be involved in the cytotoxicity of the prodigiosin family of compounds against malignant cells.</abstract><cop>England</cop><pub>Informa Healthcare</pub><pmid>25373498</pmid><doi>10.3109/14756366.2014.951347</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of enzyme inhibition and medicinal chemistry, 2015-08, Vol.30 (4), p.533-538 |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Cell Line, Tumor Cytotoxicity enzyme inhibition Enzyme Inhibitors - isolation & purification Enzyme Inhibitors - pharmacology Humans Phosphoprotein Phosphatases - antagonists & inhibitors Prodigiosin - isolation & purification Prodigiosin - pharmacology Protein Kinases - drug effects Pseudoalteromonas - chemistry structure-activity relationship |
| title | Effects of prodigiosin family compounds from Pseudoalteromonas sp. 1020R on the activities of protein phosphatases and protein kinases |
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