Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806
Many cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on dig...
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| Veröffentlicht in: | Environmental toxicology 2005-06, Vol.20 (3), p.314-322 |
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| creator | Agrawal, M.K Zitt, A Bagchi, D Weckesser, J Bagchi, S.N Elert, E. von |
| description | Many cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D. magna are trypsins and chymotrypsins, which differ from those of bovine origin in substrate specificity and susceptibility to synthetic inhibitors. An extract from Microcystis aeruginosa strain PCC 7806 inhibited both types of D. magna proteases. Subsequent fractionation of the extract by high-performance liquid chromatography indicated that several inhibitors are produced by M. aeruginosa that differ in their specificity for the trypsins and chymotrypsins of D. magna. Two fractions differed in their inhibitory effect on proteases of D. magna and bovine origin; therefore, assessment of the impact of cyanobacterial protease inhibitors on natural communities requires the use of digestive proteases from ecologically relevant grazers. |
| doi_str_mv | 10.1002/tox.20123 |
| format | Article |
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The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D. magna are trypsins and chymotrypsins, which differ from those of bovine origin in substrate specificity and susceptibility to synthetic inhibitors. An extract from Microcystis aeruginosa strain PCC 7806 inhibited both types of D. magna proteases. Subsequent fractionation of the extract by high-performance liquid chromatography indicated that several inhibitors are produced by M. aeruginosa that differ in their specificity for the trypsins and chymotrypsins of D. magna. Two fractions differed in their inhibitory effect on proteases of D. magna and bovine origin; therefore, assessment of the impact of cyanobacterial protease inhibitors on natural communities requires the use of digestive proteases from ecologically relevant grazers.</description><identifier>ISSN: 1520-4081</identifier><identifier>EISSN: 1522-7278</identifier><identifier>DOI: 10.1002/tox.20123</identifier><identifier>PMID: 15892063</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animal, plant and microbial ecology ; Animals ; Applied ecology ; Bacterial Toxins - chemistry ; Bacterial Toxins - toxicity ; Biological and medical sciences ; Chromatography, High Pressure Liquid ; chymotrypsin ; Chymotrypsin - antagonists & inhibitors ; Chymotrypsin - metabolism ; Cladocera ; cyanobacteria ; Daphnia ; Daphnia - enzymology ; Daphnia magna ; Ecotoxicology, biological effects of pollution ; Electrophoresis, Polyacrylamide Gel ; enzyme activity ; Enzyme Inhibitors - pharmacology ; Freshwater ; Fundamental and applied biological sciences. Psychology ; General aspects ; inhibition ; inhibitor ; microcystin ; microcystins ; microcystis ; Microcystis - chemistry ; Microcystis - pathogenicity ; Microcystis aeruginosa ; peptide ; Peptide Hydrolases - metabolism ; peptides ; protease ; proteinase inhibitors ; proteinases ; Proteins - metabolism ; proteolysis ; trypsin ; Trypsin - metabolism</subject><ispartof>Environmental toxicology, 2005-06, Vol.20 (3), p.314-322</ispartof><rights>Copyright © 2005 Wiley Periodicals, Inc.</rights><rights>2005 INIST-CNRS</rights><rights>(c) 2005 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4463-55d7b1601d293e141c67fb46dccb0a3a995d58e479e10d067db71881ef2b18133</citedby><cites>FETCH-LOGICAL-c4463-55d7b1601d293e141c67fb46dccb0a3a995d58e479e10d067db71881ef2b18133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Ftox.20123$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Ftox.20123$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>309,310,314,776,780,785,786,1411,23910,23911,25119,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16940773$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15892063$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Agrawal, M.K</creatorcontrib><creatorcontrib>Zitt, A</creatorcontrib><creatorcontrib>Bagchi, D</creatorcontrib><creatorcontrib>Weckesser, J</creatorcontrib><creatorcontrib>Bagchi, S.N</creatorcontrib><creatorcontrib>Elert, E. von</creatorcontrib><title>Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806</title><title>Environmental toxicology</title><addtitle>Environ. Toxicol</addtitle><description>Many cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D. magna are trypsins and chymotrypsins, which differ from those of bovine origin in substrate specificity and susceptibility to synthetic inhibitors. An extract from Microcystis aeruginosa strain PCC 7806 inhibited both types of D. magna proteases. Subsequent fractionation of the extract by high-performance liquid chromatography indicated that several inhibitors are produced by M. aeruginosa that differ in their specificity for the trypsins and chymotrypsins of D. magna. Two fractions differed in their inhibitory effect on proteases of D. magna and bovine origin; therefore, assessment of the impact of cyanobacterial protease inhibitors on natural communities requires the use of digestive proteases from ecologically relevant grazers.</description><subject>Animal, plant and microbial ecology</subject><subject>Animals</subject><subject>Applied ecology</subject><subject>Bacterial Toxins - chemistry</subject><subject>Bacterial Toxins - toxicity</subject><subject>Biological and medical sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>chymotrypsin</subject><subject>Chymotrypsin - antagonists & inhibitors</subject><subject>Chymotrypsin - metabolism</subject><subject>Cladocera</subject><subject>cyanobacteria</subject><subject>Daphnia</subject><subject>Daphnia - enzymology</subject><subject>Daphnia magna</subject><subject>Ecotoxicology, biological effects of pollution</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>enzyme activity</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>inhibition</subject><subject>inhibitor</subject><subject>microcystin</subject><subject>microcystins</subject><subject>microcystis</subject><subject>Microcystis - chemistry</subject><subject>Microcystis - pathogenicity</subject><subject>Microcystis aeruginosa</subject><subject>peptide</subject><subject>Peptide Hydrolases - metabolism</subject><subject>peptides</subject><subject>protease</subject><subject>proteinase inhibitors</subject><subject>proteinases</subject><subject>Proteins - metabolism</subject><subject>proteolysis</subject><subject>trypsin</subject><subject>Trypsin - metabolism</subject><issn>1520-4081</issn><issn>1522-7278</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10Mtu1DAUBuAIgegFFrwAeEMlFmnPsWM7WZZAC1JLEdMKdtaJ48wYZpLBTkSHpyczGeiKlS3rOxf_SfIC4RQB-Fnf3Z9yQC4eJYcoOU811_nj3R3SDHI8SI5i_A4AhZLqaXKAMi84KHGYtOWCAtneBf-bet-1rGvYOnS9o-gi8y2bD33cPr6j9aL1xFY0b4lRW7N-4XwYycJXfldabdi1t6Gzm9j7yMiFYe7bLhL7XJZM56CeJU8aWkb3fH8eJ3cX72_LD-nVzeXH8vwqtVmmRCplrStUgDUvhMMMrdJNlana2gpIUFHIWuYu04VDqEHputKY5-gaXmGOQhwnJ1Pf8Ss_Bxd7s_LRuuWSWtcN0XDQAqUqRvhmguPaMQbXmHXwKwobg2C24ZoxXLMLd7Qv902HauXqB7lPcwSv94CipWUTqLU-PjhVZKD11p1N7pdfus3_J5rbm29_R6dThY-9u_9XQeGHUVpoab5-ujTXX3A2g4u3ZutfTb6hztA8jFvczcZWAhCEyCWIP9rkqDs</recordid><startdate>200506</startdate><enddate>200506</enddate><creator>Agrawal, M.K</creator><creator>Zitt, A</creator><creator>Bagchi, D</creator><creator>Weckesser, J</creator><creator>Bagchi, S.N</creator><creator>Elert, E. von</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><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>7QH</scope><scope>7TV</scope><scope>7U7</scope><scope>7UA</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>M7N</scope></search><sort><creationdate>200506</creationdate><title>Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806</title><author>Agrawal, M.K ; Zitt, A ; Bagchi, D ; Weckesser, J ; Bagchi, S.N ; Elert, E. von</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4463-55d7b1601d293e141c67fb46dccb0a3a995d58e479e10d067db71881ef2b18133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animal, plant and microbial ecology</topic><topic>Animals</topic><topic>Applied ecology</topic><topic>Bacterial Toxins - chemistry</topic><topic>Bacterial Toxins - toxicity</topic><topic>Biological and medical sciences</topic><topic>Chromatography, High Pressure Liquid</topic><topic>chymotrypsin</topic><topic>Chymotrypsin - antagonists & inhibitors</topic><topic>Chymotrypsin - metabolism</topic><topic>Cladocera</topic><topic>cyanobacteria</topic><topic>Daphnia</topic><topic>Daphnia - enzymology</topic><topic>Daphnia magna</topic><topic>Ecotoxicology, biological effects of pollution</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>enzyme activity</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>inhibition</topic><topic>inhibitor</topic><topic>microcystin</topic><topic>microcystins</topic><topic>microcystis</topic><topic>Microcystis - chemistry</topic><topic>Microcystis - pathogenicity</topic><topic>Microcystis aeruginosa</topic><topic>peptide</topic><topic>Peptide Hydrolases - metabolism</topic><topic>peptides</topic><topic>protease</topic><topic>proteinase inhibitors</topic><topic>proteinases</topic><topic>Proteins - metabolism</topic><topic>proteolysis</topic><topic>trypsin</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Agrawal, M.K</creatorcontrib><creatorcontrib>Zitt, A</creatorcontrib><creatorcontrib>Bagchi, D</creatorcontrib><creatorcontrib>Weckesser, J</creatorcontrib><creatorcontrib>Bagchi, S.N</creatorcontrib><creatorcontrib>Elert, E. von</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aqualine</collection><collection>Pollution Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Water Resources Abstracts</collection><collection>Environmental Sciences and Pollution Management</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) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Environmental toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Agrawal, M.K</au><au>Zitt, A</au><au>Bagchi, D</au><au>Weckesser, J</au><au>Bagchi, S.N</au><au>Elert, E. von</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806</atitle><jtitle>Environmental toxicology</jtitle><addtitle>Environ. Toxicol</addtitle><date>2005-06</date><risdate>2005</risdate><volume>20</volume><issue>3</issue><spage>314</spage><epage>322</epage><pages>314-322</pages><issn>1520-4081</issn><eissn>1522-7278</eissn><abstract>Many cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D. magna are trypsins and chymotrypsins, which differ from those of bovine origin in substrate specificity and susceptibility to synthetic inhibitors. An extract from Microcystis aeruginosa strain PCC 7806 inhibited both types of D. magna proteases. Subsequent fractionation of the extract by high-performance liquid chromatography indicated that several inhibitors are produced by M. aeruginosa that differ in their specificity for the trypsins and chymotrypsins of D. magna. Two fractions differed in their inhibitory effect on proteases of D. magna and bovine origin; therefore, assessment of the impact of cyanobacterial protease inhibitors on natural communities requires the use of digestive proteases from ecologically relevant grazers.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>15892063</pmid><doi>10.1002/tox.20123</doi><tpages>9</tpages></addata></record> |
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| subjects | Animal, plant and microbial ecology Animals Applied ecology Bacterial Toxins - chemistry Bacterial Toxins - toxicity Biological and medical sciences Chromatography, High Pressure Liquid chymotrypsin Chymotrypsin - antagonists & inhibitors Chymotrypsin - metabolism Cladocera cyanobacteria Daphnia Daphnia - enzymology Daphnia magna Ecotoxicology, biological effects of pollution Electrophoresis, Polyacrylamide Gel enzyme activity Enzyme Inhibitors - pharmacology Freshwater Fundamental and applied biological sciences. Psychology General aspects inhibition inhibitor microcystin microcystins microcystis Microcystis - chemistry Microcystis - pathogenicity Microcystis aeruginosa peptide Peptide Hydrolases - metabolism peptides protease proteinase inhibitors proteinases Proteins - metabolism proteolysis trypsin Trypsin - metabolism |
| title | Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806 |
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