A comparative study of pentraxin-like proteins in different fish species
Pentraxins are a family of pentameric serum proteins that have been conserved in evolution and share sequence homology, similar subunit assembly and the capacity for calcium-dependent ligand binding. The classical pentraxins are human C-reactive protein (CRP) and serum amyloid P component (SAP). The...
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Veröffentlicht in: | Developmental and comparative immunology 1998-04, Vol.22 (2), p.185-194 |
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description | Pentraxins are a family of pentameric serum proteins that have been conserved in evolution and share sequence homology, similar subunit assembly and the capacity for calcium-dependent ligand binding. The classical pentraxins are human C-reactive protein (CRP) and serum amyloid P component (SAP). The sequence homology and gene organization indicate that they arose from a gene duplication of an ancestral pentraxin gene. They are usually isolated based on their affinity for phosphorylcholine and agarose, respectively. We have used this method for isolation of pentraxin-like proteins from normal serum of Atlantic salmon (
Salmo salar), common wolffish (
Anarhichas lupus), cod (
Gadus morhua) and halibut (
Hippoglossus hippoglossus). Although pentraxin structures have not been verified, the isolated proteins all appear to be pentraxin-like based on their binding specificity, molecular weight of subunits, cross-reactivity with antibodies to human pentraxins and N-terminal amino acid sequences. However, with the described method only one pentraxin-like protein was detected in each of the fish species. |
doi_str_mv | 10.1016/S0145-305X(97)00051-7 |
format | Article |
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Salmo salar), common wolffish (
Anarhichas lupus), cod (
Gadus morhua) and halibut (
Hippoglossus hippoglossus). Although pentraxin structures have not been verified, the isolated proteins all appear to be pentraxin-like based on their binding specificity, molecular weight of subunits, cross-reactivity with antibodies to human pentraxins and N-terminal amino acid sequences. However, with the described method only one pentraxin-like protein was detected in each of the fish species.</description><identifier>ISSN: 0145-305X</identifier><identifier>EISSN: 1879-0089</identifier><identifier>DOI: 10.1016/S0145-305X(97)00051-7</identifier><identifier>PMID: 9639088</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Acute phase protein ; Amino Acid Sequence ; Anarhichas lupus ; Animals ; Blood Proteins - analysis ; Brackish ; C-reactive protein ; Carrier Proteins - isolation & purification ; Cod ; Common wolffish ; Cross Reactions ; CRP ; Fishes ; Flatfishes ; Freshwater ; Gadus morhua ; Halibut ; Hippoglossus hippoglossus ; Humans ; Marine ; Molecular Sequence Data ; Pentraxin ; Salmo salar ; Salmon ; SAP ; Sepharose - metabolism ; Sequence Homology, Amino Acid ; Serum amyloid P component ; Species Specificity</subject><ispartof>Developmental and comparative immunology, 1998-04, Vol.22 (2), p.185-194</ispartof><rights>1998 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-cbe17deda1b36bea4f210911653f2dde28a79721ac0b9e10a732a8ac1d2153623</citedby><cites>FETCH-LOGICAL-c391t-cbe17deda1b36bea4f210911653f2dde28a79721ac0b9e10a732a8ac1d2153623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0145-305X(97)00051-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9639088$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lund, Vera</creatorcontrib><creatorcontrib>Olafsen, Jan A</creatorcontrib><title>A comparative study of pentraxin-like proteins in different fish species</title><title>Developmental and comparative immunology</title><addtitle>Dev Comp Immunol</addtitle><description>Pentraxins are a family of pentameric serum proteins that have been conserved in evolution and share sequence homology, similar subunit assembly and the capacity for calcium-dependent ligand binding. The classical pentraxins are human C-reactive protein (CRP) and serum amyloid P component (SAP). The sequence homology and gene organization indicate that they arose from a gene duplication of an ancestral pentraxin gene. They are usually isolated based on their affinity for phosphorylcholine and agarose, respectively. We have used this method for isolation of pentraxin-like proteins from normal serum of Atlantic salmon (
Salmo salar), common wolffish (
Anarhichas lupus), cod (
Gadus morhua) and halibut (
Hippoglossus hippoglossus). Although pentraxin structures have not been verified, the isolated proteins all appear to be pentraxin-like based on their binding specificity, molecular weight of subunits, cross-reactivity with antibodies to human pentraxins and N-terminal amino acid sequences. However, with the described method only one pentraxin-like protein was detected in each of the fish species.</description><subject>Acute phase protein</subject><subject>Amino Acid Sequence</subject><subject>Anarhichas lupus</subject><subject>Animals</subject><subject>Blood Proteins - analysis</subject><subject>Brackish</subject><subject>C-reactive protein</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Cod</subject><subject>Common wolffish</subject><subject>Cross Reactions</subject><subject>CRP</subject><subject>Fishes</subject><subject>Flatfishes</subject><subject>Freshwater</subject><subject>Gadus morhua</subject><subject>Halibut</subject><subject>Hippoglossus hippoglossus</subject><subject>Humans</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Pentraxin</subject><subject>Salmo salar</subject><subject>Salmon</subject><subject>SAP</subject><subject>Sepharose - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serum amyloid P component</subject><subject>Species Specificity</subject><issn>0145-305X</issn><issn>1879-0089</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotVZ_QiEn0cNqZre72ZykFLVCwYMK3kI2mcXofplsi_33ph_02tMc3mfmHR5CxsDugEF2_8ZgkkYJSz9vBL9ljKUQ8RMyhJyLiLFcnJLhATknF95_B4jlwAZkILJEsDwfkvmU6rbulFO9XSH1_dKsaVvSDpveqT_bRJX9Qdq5tkfbeGobamxZogs5La3_or5DbdFfkrNSVR6v9nNEPp4e32fzaPH6_DKbLiKdCOgjXSBwg0ZBkWQFqkkZAxMAWZqUsTEY54oLHoPSrBAITPEkVrnSYGJIkyxORuR6dze89LtE38vaeo1VpRpsl15yIVIBaXYUhGzCQ9EkgOkO1K713mEpO2dr5dYSmNyollvVcuNRCi63qiUPe-N9wbKo0Ry29m5D_rDLMehYWXTSB1GNRmMd6l6a1h5p-Ad27o5l</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>Lund, Vera</creator><creator>Olafsen, Jan A</creator><general>Elsevier Ltd</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19980401</creationdate><title>A comparative study of pentraxin-like proteins in different fish species</title><author>Lund, Vera ; Olafsen, Jan A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-cbe17deda1b36bea4f210911653f2dde28a79721ac0b9e10a732a8ac1d2153623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Acute phase protein</topic><topic>Amino Acid Sequence</topic><topic>Anarhichas lupus</topic><topic>Animals</topic><topic>Blood Proteins - analysis</topic><topic>Brackish</topic><topic>C-reactive protein</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Cod</topic><topic>Common wolffish</topic><topic>Cross Reactions</topic><topic>CRP</topic><topic>Fishes</topic><topic>Flatfishes</topic><topic>Freshwater</topic><topic>Gadus morhua</topic><topic>Halibut</topic><topic>Hippoglossus hippoglossus</topic><topic>Humans</topic><topic>Marine</topic><topic>Molecular Sequence Data</topic><topic>Pentraxin</topic><topic>Salmo salar</topic><topic>Salmon</topic><topic>SAP</topic><topic>Sepharose - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serum amyloid P component</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lund, Vera</creatorcontrib><creatorcontrib>Olafsen, Jan A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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><collection>MEDLINE - Academic</collection><jtitle>Developmental and comparative immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lund, Vera</au><au>Olafsen, Jan A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A comparative study of pentraxin-like proteins in different fish species</atitle><jtitle>Developmental and comparative immunology</jtitle><addtitle>Dev Comp Immunol</addtitle><date>1998-04-01</date><risdate>1998</risdate><volume>22</volume><issue>2</issue><spage>185</spage><epage>194</epage><pages>185-194</pages><issn>0145-305X</issn><eissn>1879-0089</eissn><abstract>Pentraxins are a family of pentameric serum proteins that have been conserved in evolution and share sequence homology, similar subunit assembly and the capacity for calcium-dependent ligand binding. The classical pentraxins are human C-reactive protein (CRP) and serum amyloid P component (SAP). The sequence homology and gene organization indicate that they arose from a gene duplication of an ancestral pentraxin gene. They are usually isolated based on their affinity for phosphorylcholine and agarose, respectively. We have used this method for isolation of pentraxin-like proteins from normal serum of Atlantic salmon (
Salmo salar), common wolffish (
Anarhichas lupus), cod (
Gadus morhua) and halibut (
Hippoglossus hippoglossus). Although pentraxin structures have not been verified, the isolated proteins all appear to be pentraxin-like based on their binding specificity, molecular weight of subunits, cross-reactivity with antibodies to human pentraxins and N-terminal amino acid sequences. However, with the described method only one pentraxin-like protein was detected in each of the fish species.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>9639088</pmid><doi>10.1016/S0145-305X(97)00051-7</doi><tpages>10</tpages></addata></record> |
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subjects | Acute phase protein Amino Acid Sequence Anarhichas lupus Animals Blood Proteins - analysis Brackish C-reactive protein Carrier Proteins - isolation & purification Cod Common wolffish Cross Reactions CRP Fishes Flatfishes Freshwater Gadus morhua Halibut Hippoglossus hippoglossus Humans Marine Molecular Sequence Data Pentraxin Salmo salar Salmon SAP Sepharose - metabolism Sequence Homology, Amino Acid Serum amyloid P component Species Specificity |
title | A comparative study of pentraxin-like proteins in different fish species |
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