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Article: Structure, function and regulation of BP-3, a member of the CD38/ADP-ribosyl cyclase family

TitleStructure, function and regulation of BP-3, a member of the CD38/ADP-ribosyl cyclase family
Authors
Issue Date1996
PublisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/
Citation
Faseb Journal, 1996, v. 10 n. 6, p. A1462 How to Cite?
AbstractThe murine BP-3 gene encodes a variably glycosylated phosphatidylinositollinkcd cell surface glycoprotein that is expressed on early B and T lineage cells, myeloid cells, intestinal epithelial cells and a discrete population of reticular cells in peripheral lymphoid tissues. The deduced amino acid sequence of BP-3 cDNA shares significant homology with human and mouse CD38 and molluscan ADPribosyl cyclase, enzymes that generate the calcium mobilizing agent, cyclic ADPribose, from NAD. However, our studies indicate that the recombinant BP-3 molecule has relatively low ADP-ribosyl cyclase enzyme activity, measurable only at pH 4.0. The BP-3 gene was mapped to mouse chromosome 5 very near the CD38 locus, suggesting that this family arose by gene duplication. Analysis of genomic clones indicates that the BP-3 gene consists of 9 exons and spans approximately 27 Kb. The overall exon organization of the BP-3 gene is very similar to that reported for the ADP-ribosyl cyclase gene in the mollusc, Aplysta turodal. As a first step to gain insight into the BP-3 gene regulatory elements, we determined the transcriptions! start sites of the BP-3 gene in a pro-B cell line. The major transcription! start site (-19 from the ATO start codon) contains a weak initiator sequence. The upstream region lacks a TATA box, but consensus recognition sequences for the Pu.l. Ikaros/LvF-1. E2A and TCF-1 transcriptional factors may regulate BP-3 transcription in lymphoid and myeloid cells.
Persistent Identifierhttp://hdl.handle.net/10722/132576
ISSN
2015 Impact Factor: 5.299
2015 SCImago Journal Rankings: 2.775

 

DC FieldValueLanguage
dc.contributor.authorWillerfbrd, DDen_HK
dc.contributor.authorGraeff, RMen_HK
dc.contributor.authorLee, HCen_HK
dc.contributor.authorAlt, Fen_HK
dc.contributor.authorCooper, MDen_HK
dc.date.accessioned2011-03-28T09:26:28Z-
dc.date.available2011-03-28T09:26:28Z-
dc.date.issued1996en_HK
dc.identifier.citationFaseb Journal, 1996, v. 10 n. 6, p. A1462en_HK
dc.identifier.issn0892-6638en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132576-
dc.description.abstractThe murine BP-3 gene encodes a variably glycosylated phosphatidylinositollinkcd cell surface glycoprotein that is expressed on early B and T lineage cells, myeloid cells, intestinal epithelial cells and a discrete population of reticular cells in peripheral lymphoid tissues. The deduced amino acid sequence of BP-3 cDNA shares significant homology with human and mouse CD38 and molluscan ADPribosyl cyclase, enzymes that generate the calcium mobilizing agent, cyclic ADPribose, from NAD. However, our studies indicate that the recombinant BP-3 molecule has relatively low ADP-ribosyl cyclase enzyme activity, measurable only at pH 4.0. The BP-3 gene was mapped to mouse chromosome 5 very near the CD38 locus, suggesting that this family arose by gene duplication. Analysis of genomic clones indicates that the BP-3 gene consists of 9 exons and spans approximately 27 Kb. The overall exon organization of the BP-3 gene is very similar to that reported for the ADP-ribosyl cyclase gene in the mollusc, Aplysta turodal. As a first step to gain insight into the BP-3 gene regulatory elements, we determined the transcriptions! start sites of the BP-3 gene in a pro-B cell line. The major transcription! start site (-19 from the ATO start codon) contains a weak initiator sequence. The upstream region lacks a TATA box, but consensus recognition sequences for the Pu.l. Ikaros/LvF-1. E2A and TCF-1 transcriptional factors may regulate BP-3 transcription in lymphoid and myeloid cells.en_HK
dc.languageengen_US
dc.publisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/en_HK
dc.relation.ispartofFASEB Journalen_HK
dc.titleStructure, function and regulation of BP-3, a member of the CD38/ADP-ribosyl cyclase familyen_HK
dc.typeArticleen_HK
dc.identifier.emailGraeff, RM: graeffr@hku.hken_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.authorityGraeff, RM=rp01464en_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-33749124134en_HK
dc.identifier.volume10en_HK
dc.identifier.issue6en_HK
dc.identifier.spageA1462en_HK
dc.identifier.epageA1462en_HK
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWillerfbrd, DD=14720452600en_HK
dc.identifier.scopusauthoridGraeff, RM=7003614053en_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK
dc.identifier.scopusauthoridAlt, F=35428755500en_HK
dc.identifier.scopusauthoridCooper, MD=35414231200en_HK

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