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Article: Primary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-D

TitlePrimary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-D
Authors
Issue Date1994
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1994, v. 269 n. 16, p. 11820-11824 How to Cite?
AbstractCollectin-43 (CL-43) is a bovine serum protein that is composed of subunits of three identical chains, each of which contains a collagen region and a C-type carbohydrate recognition domain; thus, CL-43 belongs to the collectins (group III of the C-type lectins). We have derived the complete primary sequence of CL-43 using partial protein sequencing, cDNA cloning, and reverse transcription-polymerase chain reaction techniques. The primary sequence of CL-43 shows that it contains an N-terminal region of 28 residues, followed by a collagenous domain of 38 repeats of Gly-Xaa-Yaa and then a C- terminal section of 159 residues, containing a short 'neck' region and the carbohydrate recognition domain with the conserved residues found in all C- type lectins. The amino acid sequence of CL-43 showed 74% identity to bovine conglutinin and 70% identity to bovine lung surfactant protein D (SP-D), but the collagen region is considerably shorter than the 57 Gly-Xaa-Yaa triplets found in conglutinin and SP-D. Northern blot analysis showed that CL-43 was only synthesized in bovine liver, with no detectable signal in a variety of other bovine tissues, including lung. No cross-hybridizing signals were detected in mRNA from sheep, human, rat, or mouse liver. Since CL-43 and conglutinin have only been detected in members of bovidae, it is probable that an ancestral gene of these two proteins was first derived from a SP-D- like gene, and that this ancestral gene duplicated during evolution.
Persistent Identifierhttp://hdl.handle.net/10722/49436
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLim, BLen_HK
dc.contributor.authorWillis, ACen_HK
dc.contributor.authorReid, KBMen_HK
dc.contributor.authorLu, Jen_HK
dc.contributor.authorLaursen, SBen_HK
dc.contributor.authorJensenius, JCen_HK
dc.contributor.authorHolmskov, Uen_HK
dc.date.accessioned2008-06-12T06:42:35Z-
dc.date.available2008-06-12T06:42:35Z-
dc.date.issued1994en_HK
dc.identifier.citationJournal Of Biological Chemistry, 1994, v. 269 n. 16, p. 11820-11824en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49436-
dc.description.abstractCollectin-43 (CL-43) is a bovine serum protein that is composed of subunits of three identical chains, each of which contains a collagen region and a C-type carbohydrate recognition domain; thus, CL-43 belongs to the collectins (group III of the C-type lectins). We have derived the complete primary sequence of CL-43 using partial protein sequencing, cDNA cloning, and reverse transcription-polymerase chain reaction techniques. The primary sequence of CL-43 shows that it contains an N-terminal region of 28 residues, followed by a collagenous domain of 38 repeats of Gly-Xaa-Yaa and then a C- terminal section of 159 residues, containing a short 'neck' region and the carbohydrate recognition domain with the conserved residues found in all C- type lectins. The amino acid sequence of CL-43 showed 74% identity to bovine conglutinin and 70% identity to bovine lung surfactant protein D (SP-D), but the collagen region is considerably shorter than the 57 Gly-Xaa-Yaa triplets found in conglutinin and SP-D. Northern blot analysis showed that CL-43 was only synthesized in bovine liver, with no detectable signal in a variety of other bovine tissues, including lung. No cross-hybridizing signals were detected in mRNA from sheep, human, rat, or mouse liver. Since CL-43 and conglutinin have only been detected in members of bovidae, it is probable that an ancestral gene of these two proteins was first derived from a SP-D- like gene, and that this ancestral gene duplicated during evolution.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshBlood Proteins - chemistryen_HK
dc.subject.meshCollectinsen_HK
dc.subject.meshGlycoproteins - chemistryen_HK
dc.subject.meshLectins - biosynthesis - chemistry - isolation & purificationen_HK
dc.subject.meshLiver - metabolismen_HK
dc.titlePrimary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-Den_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=269&issue=16&spage=11820&epage=11824&date=1994&atitle=Primary+structure+of+bovine+collectin-43+(CL-43):+comparison+with+conglutinin+and+lung+surfactant+protein-Den_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid8163480-
dc.identifier.scopuseid_2-s2.0-0028200815en_HK
dc.identifier.hkuros9696-
dc.identifier.volume269en_HK
dc.identifier.issue16en_HK
dc.identifier.spage11820en_HK
dc.identifier.epage11824en_HK
dc.identifier.isiWOS:A1994NG37700025-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK
dc.identifier.scopusauthoridWillis, AC=7202176800en_HK
dc.identifier.scopusauthoridReid, KBM=7202780648en_HK
dc.identifier.scopusauthoridLu, J=7601564408en_HK
dc.identifier.scopusauthoridLaursen, SB=7005289302en_HK
dc.identifier.scopusauthoridJensenius, JC=7005603928en_HK
dc.identifier.scopusauthoridHolmskov, U=7004526416en_HK

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