메뉴 건너뛰기




Volumn 4, Issue DECEMBER2015, 2015, Pages

The serine protease hepsin mediates urinary secretion and polymerisation of zona pellucida domain protein uromodulin

Author keywords

[No Author keywords available]

Indexed keywords

HEPSIN; PROSTASIN; TAMM HORSFALL GLYCOPROTEIN; SERINE PROTEINASE;

EID: 84956957059     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.08887     Document Type: Article
Times cited : (87)

References (61)
  • 2
    • 77951764114 scopus 로고    scopus 로고
    • Establishment of an in vivo model facilitates B2 receptor protein maturation and heterodimerization
    • Abd Alla J, Pohl A, Reeck K, Streichert T, Quitterer U. 2010. Establishment of an in vivo model facilitates B2 receptor protein maturation and heterodimerization. Integrative Biology 2:209-217. doi: 10.1039/b922592g.
    • (2010) Integrative Biology , vol.2 , pp. 209-217
    • Abd Alla, J.1    Pohl, A.2    Reeck, K.3    Streichert, T.4    Quitterer, U.5
  • 4
    • 0141557578 scopus 로고    scopus 로고
    • Structural characterization of native mouse zona pellucida proteins using mass spectrometry
    • Boja ES, Hoodbhoy T, Fales HM, Dean J. 2003. Structural characterization of native mouse zona pellucida proteins using mass spectrometry. Journal of Biological Chemistry 278:34189-34202. doi: 10.1074/jbc.M304026200.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Dean, J.4
  • 5
    • 63049086099 scopus 로고    scopus 로고
    • Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
    • Béliveau F, Désilets A, Leduc R. 2009. Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides. FEBS Journal 276:2213-2226. doi: 10.1111/j.1742-4658.2009.06950.x.
    • (2009) FEBS Journal , vol.276 , pp. 2213-2226
    • Béliveau, F.1    Désilets, A.2    Leduc, R.3
  • 7
    • 33748415333 scopus 로고    scopus 로고
    • Prostasin attenuates inducible nitric oxide synthase expression in lipopolysaccharide-induced urinary bladder inflammation
    • Chen L-M, et al. 2006. Prostasin attenuates inducible nitric oxide synthase expression in lipopolysaccharide-induced urinary bladder inflammation. AJP: Renal Physiology 291:F567-F577. doi: 10.1152/ajprenal.00047.2006.
    • (2006) AJP: Renal Physiology , vol.291
    • Chen, L.-M.1
  • 8
    • 77949657431 scopus 로고    scopus 로고
    • Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor
    • Chen M, Chen L-M, Lin C-Y, Chai KX. 2010. Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor. Molecular and Cellular Biochemistry 337:259-266. doi: 10.1007/s11010-009-0307-y.
    • (2010) Molecular and Cellular Biochemistry , vol.337 , pp. 259-266
    • Chen, M.1    Chen, L.-M.2    Lin, C.-Y.3    Chai, K.X.4
  • 12
    • 23944482310 scopus 로고    scopus 로고
    • Dissection of a DNA-damage-induced transcriptional network using a combination of microarrays, RNA interference and computational promoter analysis
    • Elkon R, Rashi-Elkeles S, Lerenthal Y, Linhart C, Tenne T, Amariglio N, Rechavi G, Shamir R, Shiloh Y. 2005. Dissection of a DNA-damage-induced transcriptional network using a combination of microarrays, RNA interference and computational promoter analysis. Genome Biology 6:R43 doi: 10.1186/gb-2005-6-5-r43.
    • (2005) Genome Biology , vol.6
    • Elkon, R.1    Rashi-Elkeles, S.2    Lerenthal, Y.3    Linhart, C.4    Tenne, T.5    Amariglio, N.6    Rechavi, G.7    Shamir, R.8    Shiloh, Y.9
  • 13
    • 27144432513 scopus 로고    scopus 로고
    • Identification of hepatocyte growth factor activator inhibitor-1B as a potential physiological inhibitor of prostasin
    • Fan B, Wu TD, Li W, Kirchhofer D. 2005. Identification of hepatocyte growth factor activator inhibitor-1B as a potential physiological inhibitor of prostasin. Journal of Biological Chemistry 280:34513-34520. doi: 10.1074/jbc.M502119200.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 34513-34520
    • Fan, B.1    Wu, T.D.2    Li, W.3    Kirchhofer, D.4
  • 14
    • 0030062155 scopus 로고    scopus 로고
    • Polarized GP2 secretion in MDCK cells via GPI targeting and apical membrane- restricted proteolysis
    • Fritz BA, Lowe AW. 1996. Polarized GP2 secretion in MDCK cells via GPI targeting and apical membrane- restricted proteolysis. American Journal of Physiology 270:176-183.
    • (1996) American Journal of Physiology , vol.270 , pp. 176-183
    • Fritz, B.A.1    Lowe, A.W.2
  • 18
    • 0020198526 scopus 로고
    • The primary structure of high molecular mass urokinase from human urine. The complete amino arid sequence of the a chain
    • Gu¨ nzler WA, Steffens GJ, Otting F, Kim SM, Frankus E, Flohe´ L. 1982. The primary structure of high molecular mass urokinase from human urine. the complete amino arid sequence of the a chain. Hoppe-Seyler´S Zeitschrift Fu¨r Physiologische Chemie 363:1155-1166. doi: 10.1515/bchm2.1982.363.2.1155.
    • (1982) Hoppe-Seyler´S Zeitschrift Fu¨r Physiologische Chemie , vol.363 , pp. 1155-1166
    • Nzler, G.1    Wa, S.G.2    Otting, F.3    Kim, S.M.4    Frankus, E.5    Flohe´, L.6
  • 19
    • 77958473336 scopus 로고    scopus 로고
    • Insights into egg coat assembly and egg-sperm interaction from the x-ray structure of full-length ZP3
    • Han L, Monne´ M, Okumura H, Schwend T, Cherry AL, Flot D, Matsuda T, Jovine L. 2010. Insights into egg coat assembly and egg-sperm interaction from the x-ray structure of full-length ZP3. Cell 143:404-415. doi: 10.1016/j.cell.2010.09.041.
    • (2010) Cell , vol.143 , pp. 404-415
    • Han, L.1    Monne´, M.2    Okumura, H.3    Schwend, T.4    Cherry, A.L.5    Flot, D.6    Matsuda, T.7    Jovine, L.8
  • 20
    • 0036914069 scopus 로고    scopus 로고
    • Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy
    • Hart TC. 2002. Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy. Journal of Medical Genetics 39:882-892. doi: 10.1136/jmg.39.12.882.
    • (2002) Journal of Medical Genetics , vol.39 , pp. 882-892
    • Hart, T.C.1
  • 21
    • 42949151580 scopus 로고    scopus 로고
    • Matrix metalloproteinase 13 (MMP13) and tissue inhibitor of matrix metalloproteinase 1 (TIMP1), regulated by the MAPK pathway, are both necessary for madin-darby canine kidney tubulogenesis
    • Hellman NE, Spector J, Robinson J, Zuo X, Saunier S, Antignac C, Tobias JW, Lipschutz JH. 2008. Matrix metalloproteinase 13 (mMP13) and tissue inhibitor of matrix metalloproteinase 1 (TIMP1), regulated by the MAPK pathway, are both necessary for madin-darby canine kidney tubulogenesis. Journal of Biological Chemistry 283:4272-4282. doi: 10.1074/jbc.M708027200.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 4272-4282
    • Hellman, N.E.1    Spector, J.2    Robinson, J.3    Zuo, X.4    Saunier, S.5    Antignac, C.6    Tobias, J.W.7    Lipschutz, J.H.8
  • 25
    • 0036307181 scopus 로고    scopus 로고
    • The ZP domain is a conserved module for polymerization of extracellular proteins
    • Jovine L, Qi H, Williams Z, Litscher E, Wassarman PM. 2002. The ZP domain is a conserved module for polymerization of extracellular proteins. Nature Cell Biology 4:457-461. doi: 10.1038/ncb802.
    • (2002) Nature Cell Biology , vol.4 , pp. 457-461
    • Jovine, L.1    Qi, H.2    Williams, Z.3    Litscher, E.4    Wassarman, P.M.5
  • 28
    • 84888389812 scopus 로고    scopus 로고
    • Role of hepsin in factor VII activation in zebrafish. Blood Cells
    • Khandekar G, Jagadeeswaran P. 2014. Role of hepsin in factor VII activation in zebrafish. Blood Cells, Molecules, and Diseases 52:76-81. doi: 10.1016/j.bcmd.2013.07.014.
    • (2014) Molecules, and Diseases , vol.52 , pp. 76-81
    • Khandekar, G.1    Jagadeeswaran, P.2
  • 29
    • 0032818491 scopus 로고    scopus 로고
    • Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins ofXenopus egg envelopes
    • Kubo H, Matsushita M, Kotani M, Kawasaki H, Saido TC, Kawashima S, Katagiri C, Suzuki A. 1999. Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins ofXenopus egg envelopes. Developmental Genetics 25:123-129. doi: 10.1002/(SICI)1520-6408(1999)25:2<123::AID-DVG6>3.0.CO;2-3.
    • (1999) Developmental Genetics , vol.25 , pp. 123-129
    • Kubo, H.1    Matsushita, M.2    Kotani, M.3    Kawasaki, H.4    Saido, T.C.5    Kawashima, S.6    Katagiri, C.7    Suzuki, A.8
  • 33
    • 77956458124 scopus 로고    scopus 로고
    • Progressive renal papillary calcification and ureteral stone formation in mice deficient for tamm-horsfall protein
    • Liu Y, Mo L, Goldfarb DS, Evan AP, Liang F, Khan SR, Lieske JC, Wu X-R, et al. 2010. Progressive renal papillary calcification and ureteral stone formation in mice deficient for tamm-horsfall protein. AJP: Renal Physiology 299:F469-F478. doi: 10.1152/ajprenal.00243.2010.
    • (2010) AJP: Renal Physiology , vol.299 , pp. 469-478
    • Liu, Y.1    Mo, L.2    Goldfarb, D.S.3    Evan, A.P.4    Liang, F.5    Khan, S.R.6    Lieske, J.C.7    Wu, X.-R.8
  • 36
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • Mentlein R. 1999. Dipeptidyl-peptidase IV (cD26)-role in the inactivation of regulatory peptides. Regulatory Peptides 85:9-24. doi: 10.1016/S0167-0115(99)00089-0.
    • (1999) Regulatory Peptides , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 40
    • 76549122581 scopus 로고    scopus 로고
    • Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA
    • Owen KA, Qiu D, Alves J, Schumacher AM, Kilpatrick LM, Li J, Harris JL, Ellis V. 2010. Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA. Biochemical Journal 426:219-228. doi: 10.1042/BJ20091448.
    • (2010) Biochemical Journal , vol.426 , pp. 219-228
    • Owen, K.A.1    Qiu, D.2    Alves, J.3    Schumacher, A.M.4    Kilpatrick, L.M.5    Li, J.6    Harris, J.L.7    Ellis, V.8
  • 42
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Research 29:45e-45. doi: 10.1093/nar/29.9.e45.
    • (2001) Nucleic Acids Research , vol.29 , pp. 45-46
    • Pfaffl, M.W.1
  • 43
    • 80052264182 scopus 로고    scopus 로고
    • The rediscovery of uromodulin (Tamm-horsfall protein): From tubulointerstitial nephropathy to chronic kidney disease
    • Rampoldi L, Scolari F, Amoroso A, Ghiggeri G, Devuyst O. 2011. The rediscovery of uromodulin (tamm-horsfall protein): from tubulointerstitial nephropathy to chronic kidney disease. Kidney International 80:338-347. doi: 10.1038/ki.2011.134.
    • (2011) Kidney International , vol.80 , pp. 338-347
    • Rampoldi, L.1    Scolari, F.2    Amoroso, A.3    Ghiggeri, G.4    Devuyst, O.5
  • 44
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber J, Mann M, Ishihama Y. 2007. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nature Protocols 2:1896-1906. doi: 10.1038/nprot.2007.261.
    • (2007) Nature Protocols , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 45
    • 78751528090 scopus 로고    scopus 로고
    • Tamm-horsfall glycoprotein interacts with renal outer medullary potassium channel ROMK2 and regulates its function
    • Renigunta A, Renigunta V, Saritas T, Decher N, Mutig K, Waldegger S. 2011. Tamm-horsfall glycoprotein interacts with renal outer medullary potassium channel ROMK2 and regulates its function. Journal of Biological Chemistry 286:2224-2235. doi: 10.1074/jbc.M110.149880.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 2224-2235
    • Renigunta, A.1    Renigunta, V.2    Saritas, T.3    Decher, N.4    Mutig, K.5    Waldegger, S.6
  • 47
    • 0036200908 scopus 로고    scopus 로고
    • A conditional allele at the mouse channel activating protease 1 (Prss8) gene locus
    • Rubera I, Meier E, Vuagniaux Grégoire, Mérillat A-M, Beermann F, Rossier BC, Hummler E. 2002. A conditional allele at the mouse channel activating protease 1 (prss8) gene locus. Genesis 32:173-176. doi: 10.1002/gene.10040.
    • (2002) Genesis , vol.32 , pp. 173-176
    • Rubera, I.1    Meier, E.2    Grégoire, Mérillat, V.A.3    Beermann, F.4    Rossier, B.C.5    Hummler, E.6
  • 49
    • 61949278337 scopus 로고    scopus 로고
    • Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly
    • Schaeffer C, Santambrogio S, Perucca S, Casari G, Rampoldi L. 2009. Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly. Molecular Biology of the Cell 20:589-599. doi: 10.1091/mbc.E08-08-0876.
    • (2009) Molecular Biology of the Cell , vol.20 , pp. 589-599
    • Schaeffer, C.1    Santambrogio, S.2    Perucca, S.3    Casari, G.4    Rampoldi, L.5
  • 51
    • 84863205849 scopus 로고    scopus 로고
    • NIH image to ImageJ: 25 years of image analysis
    • Schneider CA, Rasband WS, Eliceiri KW. 2012. NIH image to ImageJ: 25 years of image analysis. Nature Methods 9:671-675. doi: 10.1038/nmeth.2089.
    • (2012) Nature Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 54
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Analytical Chemistry 68:850-858. doi: 10.1021/ac950914h.
    • (1996) Analytical Chemistry , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 59
    • 0032518561 scopus 로고    scopus 로고
    • Generation and characterization of mice deficient in hepsin, a hepatic transmembrane serine protease
    • Wu Q, Yu D, Post J, Halks-Miller M, Sadler JE, Morser J. 1998. Generation and characterization of mice deficient in hepsin, a hepatic transmembrane serine protease. Journal of Clinical Investigation 101:321-326. doi: 10.1172/JCI1617.
    • (1998) Journal of Clinical Investigation , vol.101 , pp. 321-326
    • Wu, Q.1    Yu, D.2    Post, J.3    Halks-Miller, M.4    Sadler, J.E.5    Morser, J.6
  • 61
    • 21244467119 scopus 로고    scopus 로고
    • Gene expression profiles in HEK-293 cells with low or high store-operated calcium entry: Can regulatory as well as regulated genes be identified?
    • Zagranichnaya TK. 2005. Gene expression profiles in HEK-293 cells with low or high store-operated calcium entry: can regulatory as well as regulated genes be identified? Physiological Genomics 21:14-33. doi: 10.1152/physiolgenomics.00099.2004.
    • (2005) Physiological Genomics , vol.21 , pp. 14-33
    • Zagranichnaya, T.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.