Expression of kallikrein‐related peptidase 4 in dental and non‐dental tissues
dc.contributor.author | Simmer, James P. | en_US |
dc.contributor.author | Richardson, Amelia S. | en_US |
dc.contributor.author | Smith, Charles E. | en_US |
dc.contributor.author | Hu, Yuan Yuan | en_US |
dc.contributor.author | Hu, Jan C‐C. | en_US |
dc.date.accessioned | 2012-03-16T15:54:00Z | |
dc.date.available | 2013-02-01T20:26:21Z | en_US |
dc.date.issued | 2011-12 | en_US |
dc.identifier.citation | Simmer, James P.; Richardson, Amelia S.; Smith, Charles E.; Hu, Yuanyuan; Hu, Jan C‐c. (2011). "Expression of kallikreinâ related peptidase 4 in dental and nonâ dental tissues." European Journal of Oral Sciences 119. <http://hdl.handle.net/2027.42/90082> | en_US |
dc.identifier.issn | 0909-8836 | en_US |
dc.identifier.issn | 1600-0722 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/90082 | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.publisher | Wiley Periodicals, Inc. | en_US |
dc.subject.other | Enamel | en_US |
dc.subject.other | Proteases | en_US |
dc.subject.other | Kallikrein | en_US |
dc.subject.other | Submandibular Salivary Gland | en_US |
dc.subject.other | Amelogenesis Imperfecta | en_US |
dc.title | Expression of kallikrein‐related peptidase 4 in dental and non‐dental tissues | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Otolaryngology | en_US |
dc.subject.hlbsecondlevel | Dentistry | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Facility for Electron Microscopy Research, Department of Anatomy & Cell Biology, and Faculty of Dentistry, McGill University, Montreal, QC, Canada | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/90082/1/j.1600-0722.2011.00834.x.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/90082/2/EOS_834_sm_FigS1-S2.pdf | |
dc.identifier.doi | 10.1111/j.1600-0722.2011.00834.x | en_US |
dc.identifier.source | European Journal of Oral Sciences | en_US |
dc.identifier.citedreference | Meredith RW, Gatesy J, Cheng J, Springer MS. Pseudogenization of the tooth gene enamelysin (MMP20) in the common ancestor of extant baleen whales. Proc Biol Sci 2011; 278 ( 1708 ): 993 – 1002. | en_US |
dc.identifier.citedreference | Simmer JP, Papagerakis P, Smith CE, Fisher DC, Rountrey AN, Zheng L, Hu JC. Regulation of dental enamel shape and hardness. J Dent Res 2010; 89: 1024 – 1038. | en_US |
dc.identifier.citedreference | Hu JC, Ryu OH, Chen JJ, Uchida T, Wakida K, Murakami C, Jiang H, Qian Q, Zhang C, Ottmers V, Bartlett JD, Simmer JP. Localization of EMSP1 expression during tooth formation and cloning of mouse cDNA. J Dent Res 2000; 79: 70 – 76. | en_US |
dc.identifier.citedreference | Hu JC, Zhang C, Sun X, Yang Y, Cao X, Ryu O, Simmer JP. Characterization of the mouse and human PRSS17 genes, their relationship to other serine proteases, and the expression of PRSS17 in developing mouse incisors. Gene 2000; 251: 1 – 8. | en_US |
dc.identifier.citedreference | Hu JC, Sun X, Zhang C, Liu S, Bartlett JD, Simmer JP. Enamelysin and kallikrein‐4 mRNA expression in developing mouse molars. Eur J Oral Sci 2002; 110: 307 – 315. | en_US |
dc.identifier.citedreference | Simmer JP, Sun X, Yamada Y, Zhang CH, Bartlett JD, Hu JC‐C. Enamelysin and kallikrein‐4 expression in the mouse incisor. In: Kobayashi I, Ozawa H, eds. Biomineralization: formation, diversity, evolution and application Proceedings of the 8th International Symposium on Biomineralization, Niigata, Jpn, Sept 25‐28, 2001. Hadano, Japan: Tokai University Press, 2004; 348 – 352. | en_US |
dc.identifier.citedreference | Ryu O, Hu JC, Yamakoshi Y, Villemain JL, Cao X, Zhang C, Bartlett JD, Simmer JP. Porcine kallikrein‐4 activation, glycosylation, activity, and expression in prokaryotic and eukaryotic hosts. Eur J Oral Sci 2002; 110: 358 – 365. | en_US |
dc.identifier.citedreference | Smith CE, Richardson AS, Hu Y, Bartlett JD, Hu JC‐C, Simmer JP. Effects of loss of function of kallikrein 4 on mineralization of enamel: comparison to mice lacking matrix metalloproteinase 20. J Biol Chem 2011; 286 ( 20 ): 18149 – 18160. | en_US |
dc.identifier.citedreference | Simmer JP, Hu Y, Lertlam R, Yamakoshi Y, Hu JC. Hypomaturation enamel defects in Klk4 knockout/LacZ knockin mice. J Biol Chem 2009; 284: 19110 – 19121. | en_US |
dc.identifier.citedreference | Hart PS, Hart TC, Michalec MD, Ryu OH, Simmons D, Hong S, Wright JT. Mutation in kallikrein 4 causes autosomal recessive hypomaturation amelogenesis imperfecta. J Med Genet 2004; 41: 545 – 549. | en_US |
dc.identifier.citedreference | Lu Y, Papagerakis P, Yamakoshi Y, Hu JC, Bartlett JD, Simmer JP. Functions of KLK4 and MMP‐20 in dental enamel formation. Biol Chem 2008; 389: 695 – 700. | en_US |
dc.identifier.citedreference | Obiezu CV, Shan SJ, Soosaipillai A, Luo LY, Grass L, Sotiropoulou G, Petraki CD, Papanastasiou PA, Levesque MA, Diamandis EP. Human kallikrein 4: quantitative study in tissues and evidence for Its secretion into biological fluids. Clin Chem 2005; 51: 1432 – 1442. | en_US |
dc.identifier.citedreference | Shaw JL, Diamandis EP. Distribution of 15 human kallikreins in tissues and biological fluids. Clin Chem 2007; 53: 1423 – 1432. | en_US |
dc.identifier.citedreference | Seiz L, Kotzsch M, Grebenchtchikov NI, Geurts‐Moespot AJ, Fuessel S, Goettig P, Gkazepis A, Wirth MP, Schmitt M, Lossnitzer A, Sweep FC, Magdolen V. Polyclonal antibodies against kallikrein‐related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer. Biol chem 2010; 391: 391 – 401. | en_US |
dc.identifier.citedreference | Day CH, Fanger GR, Retter MW, Hylander BL, Penetrante RB, Houghton RL, Zhang X, Mcneill PD, Filho AM, Nolasco M, Badaro R, Cheever MA, Reed SG, Dillon DC, Watanabe Y. Characterization of KLK4 expression and detection of KLK4‐specific antibody in prostate cancer patient sera. Oncogene 2002; 21: 7114 – 7120. | en_US |
dc.identifier.citedreference | Nelson PS, Gan L, Ferguson C, Moss P, Gelinas R, Hood L, Wang K. Molecular cloning and characterization of prostase, an androgen‐regulated serine protease with prostate‐restricted expression. Proc Natl Acad Sci USA 1999; 96: 3114 – 3119. | en_US |
dc.identifier.citedreference | Takayama TK, Mcmullen BA, Nelson PS, Matsumura M, Fujikawa K. Characterization of hK4 (prostase), a prostate‐specific serine protease: activation of the precursor of prostate specific antigen (pro‐PSA) and single‐chain urokinase‐type plasminogen activator and degradation of prostatic acid phosphatase. Biochemistry 2001; 40: 15341 – 15348. | en_US |
dc.identifier.citedreference | Williams SA, Xu Y, De Marzo AM, Isaacs JT, Denmeade SR. Prostate‐specific antigen (PSA) is activated by KLK2 in prostate cancer ex vivo models and in prostate‐targeted PSA/KLK2 double transgenic mice. Prostate 2010; 70: 788 – 796. | en_US |
dc.identifier.citedreference | Hu JC, Sun X, Zhang C, Simmer JP. A comparison of enamelin and amelogenin expression in developing mouse molars. Eur J Oral Sci 2001; 109: 125 – 132. | en_US |
dc.identifier.citedreference | Dong Y, Kaushal A, Bui L, Chu S, Fuller PJ, Nicklin J, Samaratunga H, Clements JA. Human kallikrein 4 (KLK4) is highly expressed in serous ovarian carcinomas. Clin Cancer Res 2001; 7: 2363 – 2371. | en_US |
dc.identifier.citedreference | Obiezu CV, Soosaipillai A, Jung K, Stephan C, Scorilas A, Howarth DH, Diamandis EP. Detection of human kallikrein 4 in healthy and cancerous prostatic tissues by immunofluorometry and immunohistochemistry. Clin Chem 2002; 48: 1232 – 1240. | en_US |
dc.identifier.citedreference | Kita M, Okumura Y, Ohdachi SD, Oba Y, Yoshikuni M, Nakamura Y, Kido H, Uemura D. Purification and characterisation of blarinasin, a new tissue kallikrein‐like protease from the short‐tailed shrew Blarina brevicauda: comparative studies with blarina toxin. Biol Chem 2005; 386: 177 – 182. | en_US |
dc.identifier.citedreference | Aminetzach YT, Srouji JR, Kong CY, Hoekstra HE. Convergent evolution of novel protein function in shrew and lizard venom. Curr Biol 2009; 19: 1925 – 1931. | en_US |
dc.identifier.citedreference | Ramsay AJ, Dong Y, Hunt ML, Linn M, Samaratunga H, Clements JA, Hooper JD. Kallikrein‐related peptidase 4 (KLK4) initiates intracellular signaling via protease‐activated receptors (PARs). KLK4 and PAR‐2 are co‐expressed during prostate cancer progression. J Biol Chem 2008; 283: 12293 – 12304. | en_US |
dc.identifier.citedreference | Mize GJ, Wang W, Takayama TK. Prostate‐specific kallikreins‐2 and ‐4 enhance the proliferation of DU‐145 prostate cancer cells through protease‐activated receptors‐1 and ‐2. Mol Cancer Res 2008; 6: 1043 – 1051. | en_US |
dc.identifier.citedreference | Ossovskaya VS, Bunnett NW. Protease‐activated receptors: contribution to physiology and disease. Physiol Rev 2004; 84: 579 – 621. | en_US |
dc.identifier.citedreference | Gratio V, Beaufort N, Seiz L, Maier J, Virca GD, Debela M, Grebenchtchikov N, Magdolen V, Darmoul D. Kallikrein‐related peptidase 4: a new activator of the aberrantly expressed protease‐activated receptor 1 in colon cancer cells. Am J Pathol 2010; 176: 1452 – 1461. | en_US |
dc.identifier.citedreference | Fincham AG, Moradian‐Oldak J, Simmer JP. The structural biology of the developing dental enamel matrix. J Struct Biol 1999; 126: 270 – 299. | en_US |
dc.identifier.citedreference | Smith CE, Pompura JR, Borenstein S, Fazel A, Nanci A. Degradation and loss of matrix proteins from developing enamel. Anat Rec 1989; 224: 292 – 316. | en_US |
dc.identifier.citedreference | Uchida T, Tanabe T, Fukae M, Shimizu M, Yamada M, Miake K, Kobayashi S. Immunochemical and immunohistochemical studies, using antisera against porcine 25 kDa amelogenin, 89 kDa enamelin and the 13‐17 kDa nonamelogenins, on immature enamel of the pig and rat. Histochemistry 1991; 96: 129 – 138. | en_US |
dc.identifier.citedreference | Fukae M, Tanabe T, Uchida T, Yamakoshi Y, Shimizu M. Enamelins in the newly formed bovine enamel. Calcif Tissue Int 1993; 53: 257 – 261. | en_US |
dc.identifier.citedreference | Fincham AG, Belcourt AB, Termine JD, Butler WT, Cothran WC. Dental enamel matrix: sequences of two amelogenin polypeptides. Biosci Rep 1981; 1: 771 – 778. | en_US |
dc.identifier.citedreference | Fincham AG, Moradian‐Oldak J. Amelogenin post‐translational modifications: carboxy‐terminal processing and the phosphorylation of bovine and porcine “TRAP” and “LRAP” amelogenins. Biochem Biophys Res Commun 1993; 197: 248 – 255. | en_US |
dc.identifier.citedreference | Yamakoshi Y, Tanabe T, Fukae M, Shimizu M. Porcine amelogenins. Calcif Tissue Int 1994; 54: 69 – 75. | en_US |
dc.identifier.citedreference | Fincham AG, Moradian‐Oldak J. Comparative mass spectrometric analyses of enamel matrix proteins from five species suggest a common pathway of post‐secretory proteolytic processing. Connect Tissue Res 1996; 35: 151 – 156. | en_US |
dc.identifier.citedreference | Yamakoshi Y, Hu JC‐C, Ryu OH, Tanabe T, Oida S, Fukae M, Simmer JP. A comprehensive strategy for purifying pig enamel proteins. In: Kobayashi I, Ozawa H, eds. Biomineralization: formation, diversity, evolution and application Proceedings of the 8th International Symposium on Biomineralization, Niigata, Jpn, Sept 25–28, 2001. Hadano, Japan: Tokai University Press, 2003; 326 – 332. | en_US |
dc.identifier.citedreference | Begue‐Kirn C, Krebsbach PH, Bartlett JD, Butler WT. Dentin sialoprotein, dentin phosphoprotein, enamelysin and ameloblastin: tooth‐specific molecules that are distinctively expressed during murine dental differentiation. Eur J Oral Sci 1998; 106: 963 – 970. | en_US |
dc.identifier.citedreference | Ryu OH, Fincham AG, Hu CC, Zhang C, Qian Q, Bartlett JD, Simmer JP. Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins. J Dent Res 1999; 78: 743 – 750. | en_US |
dc.identifier.citedreference | Nagano T, Kakegawa A, Yamakoshi Y, Tsuchiya S, Hu JC, Gomi K, Arai T, Bartlett JD, Simmer JP. Mmp‐20 and Klk4 cleavage site preferences for amelogenin sequences. J Dent Res 2009; 88: 823 – 828. | en_US |
dc.identifier.citedreference | Iwata T, Yamakoshi Y, Hu JC, Ishikawa I, Bartlett JD, Krebsbach PH, Simmer JP. Processing of ameloblastin by MMP‐20. J Dent Res 2007; 86: 153 – 157. | en_US |
dc.identifier.citedreference | Chun YH, Yamakoshi Y, Yamakoshi F, Fukae M, Hu JC, Bartlett JD, Simmer JP. Cleavage Site Specificity of MMP‐20 for Secretory‐stage Ameloblastin. J Dent Res 2010; 89: 785 – 790. | en_US |
dc.identifier.citedreference | Caterina JJ, Skobe Z, Shi J, Ding Y, Simmer JP, Birkedal‐Hansen H, Bartlett JD. Enamelysin (matrix metalloproteinase 20)‐deficient mice display an amelogenesis imperfecta phenotype. J Biol Chem 2002; 277: 49598 – 49604. | en_US |
dc.identifier.citedreference | Kim JW, Simmer JP, Hart TC, Hart PS, Ramaswami MD, Bartlett JD, Hu JC. MMP‐20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. J Med Genet 2005; 42: 271 – 275. | en_US |
dc.identifier.citedreference | Papagerakis P, Lin HK, Lee KY, Hu Y, Simmer JP, Bartlett JD, Hu JC. Premature stop codon in MMP20 causing amelogenesis imperfecta. J Dent Res 2008; 87: 56 – 59. | en_US |
dc.identifier.citedreference | Ozdemir D, Hart PS, Ryu OH, Choi SJ, Ozdemir‐Karatas M, Firatli E, Piesco N, Hart TC. MMP20 active‐site mutation in hypomaturation amelogenesis imperfecta. J Dent Res 2005; 84: 1031 – 1035. | en_US |
dc.identifier.citedreference | Lee SK, Seymen F, Kang HY, Lee KE, Gencay K, Tuna B, Kim JW. MMP20 hemopexin domain mutation in amelogenesis imperfecta. J Dent Res 2010; 89: 46 – 50. | en_US |
dc.identifier.citedreference | Smith CE. Cellular and chemical events during enamel maturation. Crit Rev Oral Biol Med 1998; 9: 128 – 161. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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