Molecular cloning of pancreatic group I phospholipase A2 receptor
We have recently reported that mammalian pancreatic group I phospholipase A2 (PLA2-I) has its specific receptor (PLA2 receptor) on a variety of mammalian cells and that various biological responses are elicited by PLA2-I via this receptor. In this study, we cloned cDNAs encoding a protein correspond...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-02, Vol.269 (8), p.5897-5904 |
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| container_title | The Journal of biological chemistry |
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| creator | ISHIZAKI, J HANASAKI, K HIGASHINO, K.-I KISHINO, J KIKUCHI, N OHARA, O ARITA, H |
| description | We have recently reported that mammalian pancreatic group I phospholipase A2 (PLA2-I) has its specific receptor (PLA2 receptor)
on a variety of mammalian cells and that various biological responses are elicited by PLA2-I via this receptor. In this study,
we cloned cDNAs encoding a protein corresponding to the bovine PLA2 receptor purified from the corpora lutea on the basis
of its partial amino acid sequences. The identity of a protein encoded by the cloned cDNA with the bovine PLA2 receptor was
verified by a transient expression experiment using COS-7 cells. Interestingly, the deduced primary structure of the PLA2
receptor (1,463 amino acid residues) exhibits a close relatedness throughout the molecule to that of the macrophage mannose
receptor, a unique member of Ca(2+)-dependent (C-type) animal lectin family, in spite of their functional diversity. Based
on this sequence similarity between these two receptors, the domain organization of the PLA2 receptor could be tentatively
assigned as follows; 10 extracellular domains including 8 tandem repeats homologous to C-type carbohydrate-recognition domains
(CRDs) and a single transmembrane region followed by a short cytoplasmic tail. The results of transient expression experiments
for mutant PLA2 receptors supported this assignment and furthermore suggested the region responsible for PLA2-I binding corresponds
to CRDs in the mannose receptor. |
| doi_str_mv | 10.1016/s0021-9258(17)37546-4 |
| format | Article |
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on a variety of mammalian cells and that various biological responses are elicited by PLA2-I via this receptor. In this study,
we cloned cDNAs encoding a protein corresponding to the bovine PLA2 receptor purified from the corpora lutea on the basis
of its partial amino acid sequences. The identity of a protein encoded by the cloned cDNA with the bovine PLA2 receptor was
verified by a transient expression experiment using COS-7 cells. Interestingly, the deduced primary structure of the PLA2
receptor (1,463 amino acid residues) exhibits a close relatedness throughout the molecule to that of the macrophage mannose
receptor, a unique member of Ca(2+)-dependent (C-type) animal lectin family, in spite of their functional diversity. Based
on this sequence similarity between these two receptors, the domain organization of the PLA2 receptor could be tentatively
assigned as follows; 10 extracellular domains including 8 tandem repeats homologous to C-type carbohydrate-recognition domains
(CRDs) and a single transmembrane region followed by a short cytoplasmic tail. The results of transient expression experiments
for mutant PLA2 receptors supported this assignment and furthermore suggested the region responsible for PLA2-I binding corresponds
to CRDs in the mannose receptor.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(17)37546-4</identifier><identifier>PMID: 7509792</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Cattle ; Cell receptors ; Cell structures and functions ; Cloning, Molecular ; DNA, Complementary ; Fundamental and applied biological sciences. Psychology ; Lectins, C-Type ; Mannose-Binding Lectins ; Miscellaneous ; Molecular and cellular biology ; Molecular Sequence Data ; Mutation ; Pancreas - metabolism ; Receptors, Cell Surface - genetics ; Receptors, Phospholipase A2 ; Recombinant Proteins - genetics ; RNA - analysis ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of biological chemistry, 1994-02, Vol.269 (8), p.5897-5904</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3884-1bb8813e9609a6997989dd8ec20505b3080edf0151596f080071db554a2654023</citedby><cites>FETCH-LOGICAL-c3884-1bb8813e9609a6997989dd8ec20505b3080edf0151596f080071db554a2654023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27931,27932</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4055620$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7509792$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ISHIZAKI, J</creatorcontrib><creatorcontrib>HANASAKI, K</creatorcontrib><creatorcontrib>HIGASHINO, K.-I</creatorcontrib><creatorcontrib>KISHINO, J</creatorcontrib><creatorcontrib>KIKUCHI, N</creatorcontrib><creatorcontrib>OHARA, O</creatorcontrib><creatorcontrib>ARITA, H</creatorcontrib><title>Molecular cloning of pancreatic group I phospholipase A2 receptor</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have recently reported that mammalian pancreatic group I phospholipase A2 (PLA2-I) has its specific receptor (PLA2 receptor)
on a variety of mammalian cells and that various biological responses are elicited by PLA2-I via this receptor. In this study,
we cloned cDNAs encoding a protein corresponding to the bovine PLA2 receptor purified from the corpora lutea on the basis
of its partial amino acid sequences. The identity of a protein encoded by the cloned cDNA with the bovine PLA2 receptor was
verified by a transient expression experiment using COS-7 cells. Interestingly, the deduced primary structure of the PLA2
receptor (1,463 amino acid residues) exhibits a close relatedness throughout the molecule to that of the macrophage mannose
receptor, a unique member of Ca(2+)-dependent (C-type) animal lectin family, in spite of their functional diversity. Based
on this sequence similarity between these two receptors, the domain organization of the PLA2 receptor could be tentatively
assigned as follows; 10 extracellular domains including 8 tandem repeats homologous to C-type carbohydrate-recognition domains
(CRDs) and a single transmembrane region followed by a short cytoplasmic tail. The results of transient expression experiments
for mutant PLA2 receptors supported this assignment and furthermore suggested the region responsible for PLA2-I binding corresponds
to CRDs in the mannose receptor.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lectins, C-Type</subject><subject>Mannose-Binding Lectins</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Pancreas - metabolism</subject><subject>Receptors, Cell Surface - genetics</subject><subject>Receptors, Phospholipase A2</subject><subject>Recombinant Proteins - genetics</subject><subject>RNA - analysis</subject><subject>Sequence Homology, Amino Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kNtKAzEQQIMotV4-obCIiD6sTpLN7bGIN1B8UMG3kM1m28i2WZMu4t-b2tKBYRjmzAwchCYYrjFgfpMACC4VYfISiysqWMXLag-NMUhaUoY_99F4hxyio5S-IEel8AiNBAMlFBmj6UvonB06EwvbhaVfzorQFr1Z2ujMyttiFsPQF09FPw8pZ-d7k1wxJUV01vWrEE_QQWu65E639Rh93N-93z6Wz68PT7fT59JSKasS17WUmDrFQRmu8nepmkY6S4ABqylIcE0LmGGmeJs7ELipGasM4awCQo_RxeZuH8P34NJKL3yyruvM0oUhacGpkETQDLINaGNIKbpW99EvTPzVGPRanX5be9FrLxoL_a9OV3lvsn0w1AvX7La2rvL8fDs3yZqujVmSTzusAsY4gYydbbC5n81_fHS69sHO3UITrrTUTCpB_wBh63-d</recordid><startdate>19940225</startdate><enddate>19940225</enddate><creator>ISHIZAKI, J</creator><creator>HANASAKI, K</creator><creator>HIGASHINO, K.-I</creator><creator>KISHINO, J</creator><creator>KIKUCHI, N</creator><creator>OHARA, O</creator><creator>ARITA, H</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19940225</creationdate><title>Molecular cloning of pancreatic group I phospholipase A2 receptor</title><author>ISHIZAKI, J ; HANASAKI, K ; HIGASHINO, K.-I ; KISHINO, J ; KIKUCHI, N ; OHARA, O ; ARITA, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3884-1bb8813e9609a6997989dd8ec20505b3080edf0151596f080071db554a2654023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lectins, C-Type</topic><topic>Mannose-Binding Lectins</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Pancreas - metabolism</topic><topic>Receptors, Cell Surface - genetics</topic><topic>Receptors, Phospholipase A2</topic><topic>Recombinant Proteins - genetics</topic><topic>RNA - analysis</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ISHIZAKI, J</creatorcontrib><creatorcontrib>HANASAKI, K</creatorcontrib><creatorcontrib>HIGASHINO, K.-I</creatorcontrib><creatorcontrib>KISHINO, J</creatorcontrib><creatorcontrib>KIKUCHI, N</creatorcontrib><creatorcontrib>OHARA, O</creatorcontrib><creatorcontrib>ARITA, H</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ISHIZAKI, J</au><au>HANASAKI, K</au><au>HIGASHINO, K.-I</au><au>KISHINO, J</au><au>KIKUCHI, N</au><au>OHARA, O</au><au>ARITA, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning of pancreatic group I phospholipase A2 receptor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-02-25</date><risdate>1994</risdate><volume>269</volume><issue>8</issue><spage>5897</spage><epage>5904</epage><pages>5897-5904</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have recently reported that mammalian pancreatic group I phospholipase A2 (PLA2-I) has its specific receptor (PLA2 receptor)
on a variety of mammalian cells and that various biological responses are elicited by PLA2-I via this receptor. In this study,
we cloned cDNAs encoding a protein corresponding to the bovine PLA2 receptor purified from the corpora lutea on the basis
of its partial amino acid sequences. The identity of a protein encoded by the cloned cDNA with the bovine PLA2 receptor was
verified by a transient expression experiment using COS-7 cells. Interestingly, the deduced primary structure of the PLA2
receptor (1,463 amino acid residues) exhibits a close relatedness throughout the molecule to that of the macrophage mannose
receptor, a unique member of Ca(2+)-dependent (C-type) animal lectin family, in spite of their functional diversity. Based
on this sequence similarity between these two receptors, the domain organization of the PLA2 receptor could be tentatively
assigned as follows; 10 extracellular domains including 8 tandem repeats homologous to C-type carbohydrate-recognition domains
(CRDs) and a single transmembrane region followed by a short cytoplasmic tail. The results of transient expression experiments
for mutant PLA2 receptors supported this assignment and furthermore suggested the region responsible for PLA2-I binding corresponds
to CRDs in the mannose receptor.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7509792</pmid><doi>10.1016/s0021-9258(17)37546-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1994-02, Vol.269 (8), p.5897-5904 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76378273 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Cattle Cell receptors Cell structures and functions Cloning, Molecular DNA, Complementary Fundamental and applied biological sciences. Psychology Lectins, C-Type Mannose-Binding Lectins Miscellaneous Molecular and cellular biology Molecular Sequence Data Mutation Pancreas - metabolism Receptors, Cell Surface - genetics Receptors, Phospholipase A2 Recombinant Proteins - genetics RNA - analysis Sequence Homology, Amino Acid |
| title | Molecular cloning of pancreatic group I phospholipase A2 receptor |
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