Five distinct calcium and phospholipid binding proteins share homology with lipocortin I
We have purified two 35-kDa proteins from rat peritoneal lavages that inhibit phospholipase A2 activity. Both are calcium/phospholipid-dependent membrane binding proteins and share similar structural and biochemical properties with lipocortins I and II. By sequence analysis we confirmed that they ar...
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| Veröffentlicht in: | The Journal of biological chemistry 1988-08, Vol.263 (22), p.10799-10811 |
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| container_title | The Journal of biological chemistry |
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| creator | Pepinsky, R B Tizard, R Mattaliano, R J Sinclair, L K Miller, G T Browning, J L Chow, E P Burne, C Huang, K S Pratt, D |
| description | We have purified two 35-kDa proteins from rat peritoneal lavages that inhibit phospholipase A2 activity. Both are calcium/phospholipid-dependent membrane binding proteins and share similar structural and biochemical properties with lipocortins I and II. By sequence analysis we confirmed that they are lipocortin-related, and we refer to the two inhibitors as lipocortins III and V. Using partial sequence information obtained from the purified rat proteins, full length cDNA clones for both proteins and for their human counterparts were isolated. As with lipocortins I and II, the amino acid sequences of lipocortins III and V which were deduced from the cDNA clones are highly conserved, sharing 50% identity with other family members. Related proteins were also purified from bovine intestinal mucosa and characterized by peptide mapping, sequence, and immunological analyses. In addition to lipocortins III and V the bovine preparation contained a third 35-kDa inhibitor and a 68-kDa inhibitor, extending the number of known lipocortins to six distinct proteins. While the various lipocortins are structurally similar, distinct differences in their cellular distribution indicate specialized roles for the individual proteins. |
| doi_str_mv | 10.1016/S0021-9258(18)38041-4 |
| format | Article |
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Both are calcium/phospholipid-dependent membrane binding proteins and share similar structural and biochemical properties with lipocortins I and II. By sequence analysis we confirmed that they are lipocortin-related, and we refer to the two inhibitors as lipocortins III and V. Using partial sequence information obtained from the purified rat proteins, full length cDNA clones for both proteins and for their human counterparts were isolated. As with lipocortins I and II, the amino acid sequences of lipocortins III and V which were deduced from the cDNA clones are highly conserved, sharing 50% identity with other family members. Related proteins were also purified from bovine intestinal mucosa and characterized by peptide mapping, sequence, and immunological analyses. In addition to lipocortins III and V the bovine preparation contained a third 35-kDa inhibitor and a 68-kDa inhibitor, extending the number of known lipocortins to six distinct proteins. While the various lipocortins are structurally similar, distinct differences in their cellular distribution indicate specialized roles for the individual proteins.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)38041-4</identifier><identifier>PMID: 2968983</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Annexins ; Base Sequence ; Binding and carrier proteins ; Biological and medical sciences ; Calcium-Binding Proteins - genetics ; Cattle ; Cloning, Molecular ; DNA - genetics ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - genetics ; Glycoproteins - isolation & purification ; Humans ; Molecular Sequence Data ; Molecular Weight ; Phospholipases A - antagonists & inhibitors ; Phospholipases A2 ; Proteins ; Rats ; Species Specificity ; Swine</subject><ispartof>The Journal of biological chemistry, 1988-08, Vol.263 (22), p.10799-10811</ispartof><rights>1988 © 1988 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4114-a0b628b294c0dcbdd6c2bf5eac4629fa0829c1df33e6de936b761cbc825586c33</citedby><cites>FETCH-LOGICAL-c4114-a0b628b294c0dcbdd6c2bf5eac4629fa0829c1df33e6de936b761cbc825586c33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7039976$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2968983$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pepinsky, R B</creatorcontrib><creatorcontrib>Tizard, R</creatorcontrib><creatorcontrib>Mattaliano, R J</creatorcontrib><creatorcontrib>Sinclair, L K</creatorcontrib><creatorcontrib>Miller, G T</creatorcontrib><creatorcontrib>Browning, J L</creatorcontrib><creatorcontrib>Chow, E P</creatorcontrib><creatorcontrib>Burne, C</creatorcontrib><creatorcontrib>Huang, K S</creatorcontrib><creatorcontrib>Pratt, D</creatorcontrib><title>Five distinct calcium and phospholipid binding proteins share homology with lipocortin I</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have purified two 35-kDa proteins from rat peritoneal lavages that inhibit phospholipase A2 activity. Both are calcium/phospholipid-dependent membrane binding proteins and share similar structural and biochemical properties with lipocortins I and II. By sequence analysis we confirmed that they are lipocortin-related, and we refer to the two inhibitors as lipocortins III and V. Using partial sequence information obtained from the purified rat proteins, full length cDNA clones for both proteins and for their human counterparts were isolated. As with lipocortins I and II, the amino acid sequences of lipocortins III and V which were deduced from the cDNA clones are highly conserved, sharing 50% identity with other family members. Related proteins were also purified from bovine intestinal mucosa and characterized by peptide mapping, sequence, and immunological analyses. In addition to lipocortins III and V the bovine preparation contained a third 35-kDa inhibitor and a 68-kDa inhibitor, extending the number of known lipocortins to six distinct proteins. While the various lipocortins are structurally similar, distinct differences in their cellular distribution indicate specialized roles for the individual proteins.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Annexins</subject><subject>Base Sequence</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Cattle</subject><subject>Cloning, Molecular</subject><subject>DNA - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - isolation & purification</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Phospholipases A - antagonists & inhibitors</subject><subject>Phospholipases A2</subject><subject>Proteins</subject><subject>Rats</subject><subject>Species Specificity</subject><subject>Swine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1q3DAURkVpSSdpHyGgRSntwol-bFlalRKaNBDoIi1kJ-QreXyLbU0lT0LePkpmmC4jEFrc8119HEJOOTvjjKvzW8YEr4xo9Beuv0rNal7Vb8iKMy0r2fC7t2R1QN6T45z_snJqw4_IkTBKGy1X5O4S7wP1mBecYaHgRsDtRN3s6WaIudwRN-hph7PHeU03KS4B50zz4FKgQ5ziGNeP9AGXgRY0QkxlFb3-QN71bszh4_49IX8uf_y--Fnd_Lq6vvh-U0HNeV051imhO2FqYB467xWIrm-Cg1oJ0zumhQHueymD8sFI1bWKQwdaNI1WIOUJ-bzbW5r924a82AkzhHF0c4jbbFstuVK8eRUsCGt12xaw2YGQYs4p9HaTcHLp0XJmn9XbF_X22avl2r6ot3XJne4_2HZT8IfU3nWZf9rPXS6e--RmwHzAWiaNadV_bMD18IAp2A4jDGGyQkkrRKnQGlOwbzssFLn3GJLNgGGG4EsEFusjvtL3CbQ7rMI</recordid><startdate>19880805</startdate><enddate>19880805</enddate><creator>Pepinsky, R B</creator><creator>Tizard, R</creator><creator>Mattaliano, R J</creator><creator>Sinclair, L K</creator><creator>Miller, G T</creator><creator>Browning, J L</creator><creator>Chow, E P</creator><creator>Burne, C</creator><creator>Huang, K S</creator><creator>Pratt, D</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19880805</creationdate><title>Five distinct calcium and phospholipid binding proteins share homology with lipocortin I</title><author>Pepinsky, R B ; Tizard, R ; Mattaliano, R J ; Sinclair, L K ; Miller, G T ; Browning, J L ; Chow, E P ; Burne, C ; Huang, K S ; Pratt, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4114-a0b628b294c0dcbdd6c2bf5eac4629fa0829c1df33e6de936b761cbc825586c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Annexins</topic><topic>Base Sequence</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Cattle</topic><topic>Cloning, Molecular</topic><topic>DNA - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - isolation & purification</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Phospholipases A - antagonists & inhibitors</topic><topic>Phospholipases A2</topic><topic>Proteins</topic><topic>Rats</topic><topic>Species Specificity</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pepinsky, R B</creatorcontrib><creatorcontrib>Tizard, R</creatorcontrib><creatorcontrib>Mattaliano, R J</creatorcontrib><creatorcontrib>Sinclair, L K</creatorcontrib><creatorcontrib>Miller, G T</creatorcontrib><creatorcontrib>Browning, J L</creatorcontrib><creatorcontrib>Chow, E P</creatorcontrib><creatorcontrib>Burne, C</creatorcontrib><creatorcontrib>Huang, K S</creatorcontrib><creatorcontrib>Pratt, D</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pepinsky, R B</au><au>Tizard, R</au><au>Mattaliano, R J</au><au>Sinclair, L K</au><au>Miller, G T</au><au>Browning, J L</au><au>Chow, E P</au><au>Burne, C</au><au>Huang, K S</au><au>Pratt, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Five distinct calcium and phospholipid binding proteins share homology with lipocortin I</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-08-05</date><risdate>1988</risdate><volume>263</volume><issue>22</issue><spage>10799</spage><epage>10811</epage><pages>10799-10811</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have purified two 35-kDa proteins from rat peritoneal lavages that inhibit phospholipase A2 activity. Both are calcium/phospholipid-dependent membrane binding proteins and share similar structural and biochemical properties with lipocortins I and II. By sequence analysis we confirmed that they are lipocortin-related, and we refer to the two inhibitors as lipocortins III and V. Using partial sequence information obtained from the purified rat proteins, full length cDNA clones for both proteins and for their human counterparts were isolated. As with lipocortins I and II, the amino acid sequences of lipocortins III and V which were deduced from the cDNA clones are highly conserved, sharing 50% identity with other family members. Related proteins were also purified from bovine intestinal mucosa and characterized by peptide mapping, sequence, and immunological analyses. In addition to lipocortins III and V the bovine preparation contained a third 35-kDa inhibitor and a 68-kDa inhibitor, extending the number of known lipocortins to six distinct proteins. 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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Annexins Base Sequence Binding and carrier proteins Biological and medical sciences Calcium-Binding Proteins - genetics Cattle Cloning, Molecular DNA - genetics Fundamental and applied biological sciences. Psychology Glycoproteins - genetics Glycoproteins - isolation & purification Humans Molecular Sequence Data Molecular Weight Phospholipases A - antagonists & inhibitors Phospholipases A2 Proteins Rats Species Specificity Swine |
| title | Five distinct calcium and phospholipid binding proteins share homology with lipocortin I |
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