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Characterization of porcine dentin sialoprotein (DSP) and dentin sialophosphoprotein (DSPP) cDNA clones

dc.contributor.authorYamakoshi, Yasuoen_US
dc.contributor.authorHu, Jan C-C.en_US
dc.contributor.authorLiu, Shengxien_US
dc.contributor.authorZhang, Chuhuaen_US
dc.contributor.authorOida, Shinichiroen_US
dc.contributor.authorFukae, Makotoen_US
dc.contributor.authorSimmer, James P.en_US
dc.date.accessioned2010-06-01T21:40:46Z
dc.date.available2010-06-01T21:40:46Z
dc.date.issued2003-02en_US
dc.identifier.citationYamakoshi, Yasuo; Hu, Jan C.-C.; Liu, Shengxi; Zhang, Chuhua; Oida, Shinichiro; Fukae, Makoto; Simmer, James P. (2003). "Characterization of porcine dentin sialoprotein (DSP) and dentin sialophosphoprotein (DSPP) cDNA clones." European Journal of Oral Sciences 111(1): 60-67. <http://hdl.handle.net/2027.42/74726>en_US
dc.identifier.issn0909-8836en_US
dc.identifier.issn1600-0722en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/74726
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=12558809&dopt=citationen_US
dc.format.extent839060 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherMunksgaard International Publishersen_US
dc.publisherBlackwell Publishing Ltden_US
dc.rights2003 Eur J Oral Scien_US
dc.subject.otherDentin Sialophosphoprotein (DSPP)en_US
dc.subject.otherDentin Sialoprotein (DSP)en_US
dc.subject.otherDentin Phosphophoryn (DPP)en_US
dc.subject.otherOdontogenesisen_US
dc.subject.otherPorcineen_US
dc.titleCharacterization of porcine dentin sialoprotein (DSP) and dentin sialophosphoprotein (DSPP) cDNA clonesen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelDentistryen_US
dc.subject.hlbsecondlevelOtolaryngologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumUniversity of Michigan Dental Research Laboratory, Ann Arbor, MI, USA;en_US
dc.contributor.affiliationotherUniversity of Texas School of Dentistry, Health Science Center at San Antonio, Department of Physiology, TX, USA;en_US
dc.contributor.affiliationotherDepartment of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japanen_US
dc.identifier.pmid12558809en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/74726/1/j.1600-0722.2003.00009.x.pdf
dc.identifier.doi10.1034/j.1600-0722.2003.00009.xen_US
dc.identifier.sourceEuropean Journal of Oral Sciencesen_US
dc.identifier.citedreferenceLinde A. Dentin matrix proteins: composition and possible functions in. Anat Rec 1989; 224: 154 – 166.en_US
dc.identifier.citedreferenceVeis A, Perry A. The phosphoprotein of the dentin matrix. Biochemistry 1967; 6: 2409 – 2416.en_US
dc.identifier.citedreferenceLeaver AG, Triffitt JT, Holbrook IB. Newer knowledge of non-collagenous protein in dentin and cortical bone matrix. Clin Orthop, 1975: 269 – 292.en_US
dc.identifier.citedreferenceDimuzio MT, Veis A. Phosphophoryns – major noncollagenous proteins of rat incisor dentin. Calcif Tissue Res 1978; 25: 169 – 178.en_US
dc.identifier.citedreferenceLinde A, Bhown M, Butler WT. Noncollagenous proteins of dentin. A re-examination of proteins from rat incisor dentin utilizing techniques to avoid artifacts. J Biol Chem 1980; 255: 5931 – 5942.en_US
dc.identifier.citedreferenceRitchie HH, Wang LH. Sequence determination of an extremely acidic rat dentin phosphoprotein. J Biol Chem 1996; 271: 21695 – 21698.en_US
dc.identifier.citedreferenceMacDougall M, Simmons D, Luan X, Nydegger J, Feng J, Gu TT. Dentin phosphoprotein and dentin sialoprotein are cleavage products expressed from a single transcript coded by a gene on human chromosome 4. Dentin phosphoprotein DNA sequence determination. J Biol Chem 1997; 272: 835 – 842.en_US
dc.identifier.citedreferenceTraub W, Jodaikin A, Arad T, Veis A, Sabsay B. Dentin phosphophoryn binding to collagen fibrils. Matrix 1992; 12: 197 – 201.en_US
dc.identifier.citedreferenceZhang X, Zhao J, Li C, Gao S, Qiu C, Liu P, Wu G, Qiang B, Lo WH, Shen Y. DSPP mutation in dentinogenesis imperfecta Shields type II. Nature Genet 2001; 27: 151 – 152.en_US
dc.identifier.citedreferenceXiao S, Yu C, Chou X, Yuan W, Wang Y, Bu L, Fu G, Qian M, Yang J, Shi Y, Hu L, Han B, Wang Z, Huang W, Liu J, Chen Z, Zhao G, Kong X. Dentinogenesis imperfecta 1 with or without progressive hearing loss is associated with distinct mutations in DSPP. [erratum appears in Nat Genet 2001 March; 27 (3): 345]. Nature Genet 2001; 27: 201 – 204.en_US
dc.identifier.citedreferencePallos D, Hart PS, Cortelli JR, Vian S, Wright JT, Korkko J, Brunoni D, Hart TC. Novel COL1A1 mutation (G599C) associated with mild osteogenesis imperfecta and dentinogenesis imperfecta. Arch Oral Biol 2001; 46: 459 – 470.en_US
dc.identifier.citedreferenceKinney JH, Pople JA, Driessen CH, Breunig TM, Marshall GW, Marshall SJ. Intrafibrillar mineral may be absent in dentinogenesis imperfecta type II (DI-II). J Dent Res 2001; 80: 1555 – 1559.en_US
dc.identifier.citedreferenceButler WT, Bhown M, Dimuzio MT, Linde A. Nonocollagenous proteins of dentin. Isolation and partial characterization of rat dentin proteins and proteoglycans using a three-step preparative method. Coll Relat Res 1981; 1: 187 – 199.en_US
dc.identifier.citedreferenceButler WT, Bhown M, Brunn JC, D'souza RN, Farach-Carson MC, Happonen R-P, Schrohenloher RE, Seyer JM, Somerman MJ, Foster RA, Tomana M, van Dijk S. Isolation, characterization and immunolocalization of a 53-kDa Dentin Sialoprotein (DSP). Matrix 1992; 12: 343 – 351.en_US
dc.identifier.citedreferenceQin C, Cook RG, Orkiszewski RS, Butler WT. Identification and characterization of the carboxyl-terminal region of rat dentin sialoprotein. J Biol Chem 2001; 276: 904 – 909.en_US
dc.identifier.citedreferenceButler WT, Ritchie H. The nature and functional significance of dentin extracellular matrix proteins. Int J Dev Biol 1995; 39: 343 – 351.en_US
dc.identifier.citedreferenceJonsson M, Fredriksson S, Jontell M, Linde A. Isoelectric focusing of the phosphoprotein of rat-incisor dentin in ampholine and acid pH gradients. Evidence for carrier ampholyte-protein complexes. J Chromatogr 1978; 157: 234 – 242.en_US
dc.identifier.citedreferenceButler WT, Bhown M, Dimuzio MT, Cothran WC, Linde A. Multiple forms of rat dentin phosphoproteins. Arch Biochem Biophys 1983; 225: 178 – 186.en_US
dc.identifier.citedreferenceHuq NL, Cross KJ, Talbo GH, Riley PF, Loganathan A, Crossley MA, Perich JW, Reynolds EC. N -terminal sequence analysis of bovine dentin phosphophoryn after conversion of phosphoseryl to S -propylcysteinyl residues. J Dent Res 2000; 79: 1914 – 1919.en_US
dc.identifier.citedreferenceRitchie HH, Wang LH, Knudtson K. A novel rat 523 amino acid phosphophoryn: nucleotide sequence and genomic organization. Biochim Biophys Acta 2001; 1520: 212 – 222.en_US
dc.identifier.citedreferenceRitchie HH, Hou H, Veis A, Butler WT. Cloning and sequence determination of rat dentin sialoprotein, a novel dentin protein. J Biol Chem 1994; 269: 3698 – 3702.en_US
dc.identifier.citedreferenceGeorge A, Bannon L, Sabsay B, Dillon JW, Malone J, Veis A, Jenkins NA, Gilbert DJ, Copeland NG. The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl–phosphate interaction ridges that may be essential in the biomineralization process. J Biol Chem 1996; 271: 32869 – 32873.en_US
dc.identifier.citedreferenceGeorge A, Srinivasan R, Thotakura S, Veis A. The phosphophoryn gene family: identical domain structures at the carboxyl end. Eur J Oral Sci 1998; 106: 221 – 226.en_US
dc.identifier.citedreferenceGeorge A, Srinivasan RSR, Liu K, Veis A. Rat dentin matrix protein 3 is a compound protein of rat dentin sialoprotein and phosphophoryn. Connect Tissue Res 1999; 40: 49 – 57.en_US
dc.identifier.citedreferenceRitchie HH, Wang L. The presence of multiple rat DSP-PP transcripts. Biochim Biophys Acta 2000; 1493: 27 – 32.en_US
dc.identifier.citedreferenceRitchie HH, Li X. A novel rat dentin mRNA coding only for dentin sialoprotein. Eur J Oral Sci 2001; 109: 342 – 347.en_US
dc.identifier.citedreferenceAltschul S, Madden T, SchÄffer A, Zhang J, Zhang Z, Miller W, Lipman D. Gapped blast and psi-blast: a new generation of protein database search programs. Nucl Acids Res 1997; 25: 3389 – 3402.en_US
dc.identifier.citedreferenceHiggins DG, Thompson JD, Gibson TJ. Using CLUSTAL for multiple sequence alignments. Methods Enzymol 1996; 266: 383 – 402.en_US
dc.identifier.citedreferenceHansen JE, Lund O, Tolstrup N, Gooley AA, Williams KL, Brunak S. NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility. Glycoconjugate J 1998; 15: 115 – 130.en_US
dc.identifier.citedreferenceBlom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999; 294: 1351 – 1362.en_US
dc.identifier.citedreferenceGu K, Chang S, Ritchie HH, Clarkson BH, Rutherford RB. Molecular cloning of a human dentin sialophosphoprotein gene. Eur J Oral Sci 2000; 108: 35 – 42.en_US
dc.identifier.citedreferenceFeng JQ, Luan X, Wallace J, Jing D, Ohshima T, Kulkarni AB, D'Souza RN, Kozak CA, MacDougall M. Genomic organization, chromosomal mapping, and promoter analysis of the mouse dentin sialophosphoprotein (Dspp) gene, which codes for both dentin sialoprotein and dentin phosphoprotein. J Biol Chem 1998; 273: 9457 – 9464.en_US
dc.identifier.citedreferencevon Heijne G. Signal sequences. The limits of variation. J Mol Biol 1985; 184: 99 – 105.en_US
dc.identifier.citedreferenceOida S, Nagano T, Yamakoshi Y, Ando H, Yamada M, Fukae M. Amelogenin gene expression in porcine odontoblasts. J Dent Res 2002; 81: 103 – 108.en_US
dc.identifier.citedreferenceFukae M, Ijiri H, Tanabe T, Shimizu M. Partial amino acid sequences of two proteins in developing porcine enamel. J Dent Res 1979; 58: 1000 – 1001.en_US
dc.identifier.citedreferenceFukae M, Tanabe T, Ijiri H, Shimizu M. Studies on porcine enamel proteins: a possible original enamel protein. Tsurumi U Dent J 1980; 6: 87 – 94.en_US
dc.identifier.citedreferenceYamakoshi Y, Tanabe T, Fukae M, Shimizu M. Porcine amelogenins. Calcif Tissue Int 1994; 54: 69 – 75.en_US
dc.identifier.citedreferenceFukae M, Tanabe T, Murakami C, Dohi N, Uchida T, Shimizu M. Primary structure of porcine 89 kDa enamelin. Adv Dent Res 1996; 10: 111 – 118.en_US
dc.identifier.citedreferenceSimmer JP, Fukae M, Tanabe T, Yamakoshi Y, Uchida T, Xue J, Margolis HC, Shimizu M, Dehart BC, Hu CC, Bartlett JD. Purification, characterization, and cloning of enamel matrix serine proteinase 1. J Dent Res 1998; 77: 377 – 386.en_US
dc.identifier.citedreferenceGu K, Chang SR, Slaven MS, Clarkson BH, Rutherford RB, Ritchie HH. Human dentin phosphophoryn nucleotide and amino acid sequence. Eur J Oral Sci 1998; 106: 1043 – 1047.en_US
dc.identifier.citedreferenceRitchie H, Wang LH. A mammalian bicistronic transcript encoding two dentin-specific proteins. Biochem Biophys Res Comms 1997; 231: 425 – 428.en_US
dc.identifier.citedreferenceShapiro MB, Senapathy P. RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucl Acids Res 1987; 15: 7155 – 7174.en_US
dc.identifier.citedreferenceWatakabe A, Tanaka K, Shimura Y. The role of exon sequences in splice site selection. Genes Dev 1993; 7: 407 – 418.en_US
dc.identifier.citedreferenceBurset M, Seledtsov IA, Solovyev VV. Analysis of canonical and non-canonical splice sites in mammalian genomes. Nucl Acids Res 2000; 28: 4364 – 4375.en_US
dc.identifier.citedreferenceModrek B, Lee C. A genomic view of alternative splicing. Nature Genet 2002; 30: 13 – 19.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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