Prophenoloxidase system activation in the crayfish Procambarus clarki
The prophenoloxidase system (proPO) was studied in primary cultures of hemocytes of the crayfish Procambarus clarki. Both zymosan and lipopolysaccharide (LPS) separately induced rapid degranulation and lysis of semigranular hemocytes, with concurrent release of proPO. ProPO could be demonstrated in...
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Veröffentlicht in: | Developmental and comparative immunology 1993-09, Vol.17 (5), p.399-406 |
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creator | Lanz, Humberto Hernández, Salvador Garrido-Guerrero, Efraín Tsutsumi, Víctor Aréchiga, Hugo |
description | The prophenoloxidase system (proPO) was studied in primary cultures of hemocytes of the crayfish
Procambarus clarki. Both zymosan and lipopolysaccharide (LPS) separately induced rapid degranulation and lysis of semigranular hemocytes, with concurrent release of proPO. ProPO could be demonstrated in the hemocyte lysate supernatant (HLS) obtained by a freeze/thaw method, and was specifically activated by LPS and zymosan. Phenoloxidase activity was blocked by serine protease inhibitors, such as soybean trypsin inhibitor (STI), leupeptin, and phenylmethyl-sulphonylfluoride (PMSF), and substantially increased by cystein protease inhibitors (
N-methylmaleimide,
N-ethylmaleimide, and iodoacetamide). This enhancement was observed only when the proPO system was activated. Incubation without activators or preincubation with STI prevented the induced enhancement. Electrophoretic analyses of HLS treated with zymosan or LPS showed that three bands at 41, 39, and 37 kDa were specifically modified when the system was activated. These results suggest that a serine protease is involved in the activation of the proPO system in
P. clarki, and a mechanism susceptible to cystein protease inhibitors could be related to its regulation. |
doi_str_mv | 10.1016/0145-305X(93)90031-K |
format | Article |
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Procambarus clarki. Both zymosan and lipopolysaccharide (LPS) separately induced rapid degranulation and lysis of semigranular hemocytes, with concurrent release of proPO. ProPO could be demonstrated in the hemocyte lysate supernatant (HLS) obtained by a freeze/thaw method, and was specifically activated by LPS and zymosan. Phenoloxidase activity was blocked by serine protease inhibitors, such as soybean trypsin inhibitor (STI), leupeptin, and phenylmethyl-sulphonylfluoride (PMSF), and substantially increased by cystein protease inhibitors (
N-methylmaleimide,
N-ethylmaleimide, and iodoacetamide). This enhancement was observed only when the proPO system was activated. Incubation without activators or preincubation with STI prevented the induced enhancement. Electrophoretic analyses of HLS treated with zymosan or LPS showed that three bands at 41, 39, and 37 kDa were specifically modified when the system was activated. These results suggest that a serine protease is involved in the activation of the proPO system in
P. clarki, and a mechanism susceptible to cystein protease inhibitors could be related to its regulation.</description><identifier>ISSN: 0145-305X</identifier><identifier>EISSN: 1879-0089</identifier><identifier>DOI: 10.1016/0145-305X(93)90031-K</identifier><identifier>PMID: 8270092</identifier><identifier>CODEN: DCIMDQ</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Animals ; Arthropod immunity ; Astacoidea - metabolism ; Biochemistry. Physiology. Immunology ; Biological and medical sciences ; Carbohydrates - pharmacology ; Catechol Oxidase - antagonists & inhibitors ; Catechol Oxidase - blood ; Cells, Cultured ; Cellular crustacean immunity ; Cellular immunology ; Crayfish ; Crustacea ; Crustacean immunity ; Cysteine Proteinase Inhibitors - pharmacology ; Enzyme Activation - drug effects ; Enzyme Precursors - antagonists & inhibitors ; Enzyme Precursors - blood ; Freshwater ; Fundamental and applied biological sciences. Psychology ; Hemocytes ; Hemocytes - enzymology ; Invertebrates ; Lipopolysaccharides - pharmacology ; Physiology. Development ; Procambarus clarki ; Procambarus clarkii ; Prophenoloxidase system ; Serine Proteinase Inhibitors - pharmacology ; Zymosan - pharmacology</subject><ispartof>Developmental and comparative immunology, 1993-09, Vol.17 (5), p.399-406</ispartof><rights>1993</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-e0cdc37fb03e3a88a8fd2488f2137a294730b93844deafd53a29b5077795d613</citedby><cites>FETCH-LOGICAL-c446t-e0cdc37fb03e3a88a8fd2488f2137a294730b93844deafd53a29b5077795d613</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0145305X9390031K$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3773260$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8270092$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lanz, Humberto</creatorcontrib><creatorcontrib>Hernández, Salvador</creatorcontrib><creatorcontrib>Garrido-Guerrero, Efraín</creatorcontrib><creatorcontrib>Tsutsumi, Víctor</creatorcontrib><creatorcontrib>Aréchiga, Hugo</creatorcontrib><title>Prophenoloxidase system activation in the crayfish Procambarus clarki</title><title>Developmental and comparative immunology</title><addtitle>Dev Comp Immunol</addtitle><description>The prophenoloxidase system (proPO) was studied in primary cultures of hemocytes of the crayfish
Procambarus clarki. Both zymosan and lipopolysaccharide (LPS) separately induced rapid degranulation and lysis of semigranular hemocytes, with concurrent release of proPO. ProPO could be demonstrated in the hemocyte lysate supernatant (HLS) obtained by a freeze/thaw method, and was specifically activated by LPS and zymosan. Phenoloxidase activity was blocked by serine protease inhibitors, such as soybean trypsin inhibitor (STI), leupeptin, and phenylmethyl-sulphonylfluoride (PMSF), and substantially increased by cystein protease inhibitors (
N-methylmaleimide,
N-ethylmaleimide, and iodoacetamide). This enhancement was observed only when the proPO system was activated. Incubation without activators or preincubation with STI prevented the induced enhancement. Electrophoretic analyses of HLS treated with zymosan or LPS showed that three bands at 41, 39, and 37 kDa were specifically modified when the system was activated. These results suggest that a serine protease is involved in the activation of the proPO system in
P. clarki, and a mechanism susceptible to cystein protease inhibitors could be related to its regulation.</description><subject>Animals</subject><subject>Arthropod immunity</subject><subject>Astacoidea - metabolism</subject><subject>Biochemistry. Physiology. Immunology</subject><subject>Biological and medical sciences</subject><subject>Carbohydrates - pharmacology</subject><subject>Catechol Oxidase - antagonists & inhibitors</subject><subject>Catechol Oxidase - blood</subject><subject>Cells, Cultured</subject><subject>Cellular crustacean immunity</subject><subject>Cellular immunology</subject><subject>Crayfish</subject><subject>Crustacea</subject><subject>Crustacean immunity</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme Precursors - antagonists & inhibitors</subject><subject>Enzyme Precursors - blood</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemocytes</subject><subject>Hemocytes - enzymology</subject><subject>Invertebrates</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>Physiology. Development</subject><subject>Procambarus clarki</subject><subject>Procambarus clarkii</subject><subject>Prophenoloxidase system</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><subject>Zymosan - pharmacology</subject><issn>0145-305X</issn><issn>1879-0089</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhi1EVZbSfwBSDgjRQ2CcSWL7UqmqSqlaCQ49cLMm9kRryMdiZyv235N0V3sEX0byPO-r0SPEWwmfJMj6M8iyyhGqHx8NXhgAlPn9C7GSWpkcQJuXYnVEXonXKf2E-WkJp-JUFwrAFCtx8z2OmzUPYzf-CZ4SZ2mXJu4zclN4oimMQxaGbFpz5iLt2pDW2Rxx1DcUtylzHcVf4Y04aalLfH6YZ-Lxy83j9df84dvt3fXVQ-7Ksp5yBucdqrYBZCStSbe-KLVuC4mKClMqhMagLkvP1PoK57-mAqWUqXwt8Ux82Ndu4vh7y2myfUiOu44GHrfJqpnRBuG_oKxroxGXxnIPujimFLm1mxh6ijsrwS6W7aLQLgqtQfts2d7PsXeH_m3Tsz-GDlrn_fvDnpKjro00uJCOGCqFRb2cebnHeHb2FDja5AIPjn2I7Cbrx_DvO_4CHj2YvA</recordid><startdate>19930901</startdate><enddate>19930901</enddate><creator>Lanz, Humberto</creator><creator>Hernández, Salvador</creator><creator>Garrido-Guerrero, Efraín</creator><creator>Tsutsumi, Víctor</creator><creator>Aréchiga, Hugo</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><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>7T5</scope><scope>F1W</scope><scope>H94</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19930901</creationdate><title>Prophenoloxidase system activation in the crayfish Procambarus clarki</title><author>Lanz, Humberto ; Hernández, Salvador ; Garrido-Guerrero, Efraín ; Tsutsumi, Víctor ; Aréchiga, Hugo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-e0cdc37fb03e3a88a8fd2488f2137a294730b93844deafd53a29b5077795d613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Arthropod immunity</topic><topic>Astacoidea - metabolism</topic><topic>Biochemistry. Physiology. Immunology</topic><topic>Biological and medical sciences</topic><topic>Carbohydrates - pharmacology</topic><topic>Catechol Oxidase - antagonists & inhibitors</topic><topic>Catechol Oxidase - blood</topic><topic>Cells, Cultured</topic><topic>Cellular crustacean immunity</topic><topic>Cellular immunology</topic><topic>Crayfish</topic><topic>Crustacea</topic><topic>Crustacean immunity</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzyme Precursors - antagonists & inhibitors</topic><topic>Enzyme Precursors - blood</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemocytes</topic><topic>Hemocytes - enzymology</topic><topic>Invertebrates</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>Physiology. Development</topic><topic>Procambarus clarki</topic><topic>Procambarus clarkii</topic><topic>Prophenoloxidase system</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Zymosan - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lanz, Humberto</creatorcontrib><creatorcontrib>Hernández, Salvador</creatorcontrib><creatorcontrib>Garrido-Guerrero, Efraín</creatorcontrib><creatorcontrib>Tsutsumi, Víctor</creatorcontrib><creatorcontrib>Aréchiga, Hugo</creatorcontrib><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>Immunology Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Developmental and comparative immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lanz, Humberto</au><au>Hernández, Salvador</au><au>Garrido-Guerrero, Efraín</au><au>Tsutsumi, Víctor</au><au>Aréchiga, Hugo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prophenoloxidase system activation in the crayfish Procambarus clarki</atitle><jtitle>Developmental and comparative immunology</jtitle><addtitle>Dev Comp Immunol</addtitle><date>1993-09-01</date><risdate>1993</risdate><volume>17</volume><issue>5</issue><spage>399</spage><epage>406</epage><pages>399-406</pages><issn>0145-305X</issn><eissn>1879-0089</eissn><coden>DCIMDQ</coden><abstract>The prophenoloxidase system (proPO) was studied in primary cultures of hemocytes of the crayfish
Procambarus clarki. Both zymosan and lipopolysaccharide (LPS) separately induced rapid degranulation and lysis of semigranular hemocytes, with concurrent release of proPO. ProPO could be demonstrated in the hemocyte lysate supernatant (HLS) obtained by a freeze/thaw method, and was specifically activated by LPS and zymosan. Phenoloxidase activity was blocked by serine protease inhibitors, such as soybean trypsin inhibitor (STI), leupeptin, and phenylmethyl-sulphonylfluoride (PMSF), and substantially increased by cystein protease inhibitors (
N-methylmaleimide,
N-ethylmaleimide, and iodoacetamide). This enhancement was observed only when the proPO system was activated. Incubation without activators or preincubation with STI prevented the induced enhancement. Electrophoretic analyses of HLS treated with zymosan or LPS showed that three bands at 41, 39, and 37 kDa were specifically modified when the system was activated. These results suggest that a serine protease is involved in the activation of the proPO system in
P. clarki, and a mechanism susceptible to cystein protease inhibitors could be related to its regulation.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>8270092</pmid><doi>10.1016/0145-305X(93)90031-K</doi><tpages>8</tpages></addata></record> |
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subjects | Animals Arthropod immunity Astacoidea - metabolism Biochemistry. Physiology. Immunology Biological and medical sciences Carbohydrates - pharmacology Catechol Oxidase - antagonists & inhibitors Catechol Oxidase - blood Cells, Cultured Cellular crustacean immunity Cellular immunology Crayfish Crustacea Crustacean immunity Cysteine Proteinase Inhibitors - pharmacology Enzyme Activation - drug effects Enzyme Precursors - antagonists & inhibitors Enzyme Precursors - blood Freshwater Fundamental and applied biological sciences. Psychology Hemocytes Hemocytes - enzymology Invertebrates Lipopolysaccharides - pharmacology Physiology. Development Procambarus clarki Procambarus clarkii Prophenoloxidase system Serine Proteinase Inhibitors - pharmacology Zymosan - pharmacology |
title | Prophenoloxidase system activation in the crayfish Procambarus clarki |
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