메뉴 건너뛰기




Volumn 1491, Issue 1-3, 2000, Pages 93-106

Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization

Author keywords

Cathepsin Z; cDNA cloning; Cysteine protease; Expressed sequence tag database search; Genomic PAC clone; Primer extension

Indexed keywords

CATHEPSIN; COMPLEMENTARY DNA; CYSTEINE PROTEINASE;

EID: 0034712886     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4781(00)00021-X     Document Type: Article
Times cited : (27)

References (53)
  • 2
    • 0024312845 scopus 로고
    • Biosynthesis of lysosomal endopeptidases
    • Erickson A.H. Biosynthesis of lysosomal endopeptidases. J. Cell Biochem. 40:1989;31-41.
    • (1989) J. Cell Biochem. , vol.40 , pp. 31-41
    • Erickson, A.H.1
  • 3
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti P.J., Storer A.C. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246:1995;273-283.
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 4
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles of cysteine proteases in human biology
    • Chapman H.A., Riese R.J., Shi G.P. Emerging roles of cysteine proteases in human biology. Annu. Rev. Physiol. 58:1997;63-88.
    • (1997) Annu. Rev. Physiol. , vol.58 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 6
    • 0000249898 scopus 로고
    • Nucleotide and predicted amino acid sequence of cloned human and mouse preprocathepsin B cDNAs
    • Chan S.J., San Segundo B.S., McCormick M.B., Steiner D.F. Nucleotide and predicted amino acid sequence of cloned human and mouse preprocathepsin B cDNAs. Proc. Natl. Acad. Sci. USA. 83:1986;7721-7725.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7721-7725
    • Chan, S.J.1    San Segundo, B.S.2    McCormick, M.B.3    Steiner, D.F.4
  • 9
    • 0024310890 scopus 로고
    • Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase
    • Fuchs R., Gassen H.G. Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase. Nucleic Acids Res. 17:1989;9471.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9471
    • Fuchs, R.1    Gassen, H.G.2
  • 10
    • 0023656232 scopus 로고
    • Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin
    • Troen B.R., Gal S., Gottesmann M.M. Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. Biochem. J. 246:1987;731-735.
    • (1987) Biochem. J. , vol.246 , pp. 731-735
    • Troen, B.R.1    Gal, S.2    Gottesmann, M.M.3
  • 12
    • 0032479144 scopus 로고    scopus 로고
    • Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location
    • Santamaria I., Velasco G., Pendás A.M., Fueyo A., López-Otin C. Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location. J. Biol. Chem. 273:1998;16816-16823.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16816-16823
    • Santamaria, I.1    Velasco, G.2    Pendás, A.M.3    Fueyo, A.4    López-Otin, C.5
  • 13
    • 0040234054 scopus 로고    scopus 로고
    • Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions
    • Nägler D.K., Ménard R. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. FEBS Lett. 434:1998;135-139.
    • (1998) FEBS Lett. , vol.434 , pp. 135-139
    • Nägler, D.K.1    Ménard, R.2
  • 14
    • 0032835452 scopus 로고    scopus 로고
    • Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression
    • Tisljar K., Deussing J., Peters C. Cathepsin J, a novel murine cysteine protease of the papain family with a placenta-restricted expression. FEBS Lett. 459:1999;299-304.
    • (1999) FEBS Lett. , vol.459 , pp. 299-304
    • Tisljar, K.1    Deussing, J.2    Peters, C.3
  • 16
    • 0032522413 scopus 로고    scopus 로고
    • Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
    • Santamaria I., Velasco G., Cazorla M., Fueyo A., Campo E., López-Otin C. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 58:1998;1624-1630.
    • (1998) Cancer Res. , vol.58 , pp. 1624-1630
    • Santamaria, I.1    Velasco, G.2    Cazorla, M.3    Fueyo, A.4    Campo, E.5    López-Otin, C.6
  • 17
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • Shi G.P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J. Biol. Chem. 267:1992;7258-7262.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7258-7262
    • Shi, G.P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 19
    • 0022004518 scopus 로고
    • Molecular cloning of a bovine cathepsin
    • Gay N.J., Walker J.E. Molecular cloning of a bovine cathepsin. Biochem. J. 225:1985;707-712.
    • (1985) Biochem. J. , vol.225 , pp. 707-712
    • Gay, N.J.1    Walker, J.E.2
  • 20
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Pfeiffer S.L., DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. USA. 90:1993;3063-3067.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Pfeiffer, S.L.2    Ditomas, M.E.3
  • 21
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12:1996;697-715.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 23
    • 0032410105 scopus 로고    scopus 로고
    • Napsins: New human aspartic proteinases. Distinction between two closely related genes
    • Tatnell P.J., Powell D.J., Hill J., Smith T.S., Tew D.G., Kay J. Napsins: new human aspartic proteinases. Distinction between two closely related genes. FEBS Lett. 441:1998;43-48.
    • (1998) FEBS Lett. , vol.441 , pp. 43-48
    • Tatnell, P.J.1    Powell, D.J.2    Hill, J.3    Smith, T.S.4    Tew, D.G.5    Kay, J.6
  • 24
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • Nägler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Ménard R. Human cathepsin X: a cysteine protease with unique carboxypeptidase activity. Biochemistry. 38:1999;12648-12654.
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nägler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Ménard, R.6
  • 25
    • 0029973555 scopus 로고    scopus 로고
    • Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae
    • Lustigman S., McKerrow J.H., Shah K., Lui J., Huima T., Hough M., Brotman B. Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae. J. Biol. Chem. 271:1996;30181-30189.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30181-30189
    • Lustigman, S.1    McKerrow, J.H.2    Shah, K.3    Lui, J.4    Huima, T.5    Hough, M.6    Brotman, B.7
  • 26
    • 0027730590 scopus 로고
    • Sequence analysis of translationally controlled maternal mRNAs from Urechis caupo
    • Rosenthal E. Sequence analysis of translationally controlled maternal mRNAs from Urechis caupo. Dev. Genet. 14:1993;485-491.
    • (1993) Dev. Genet. , vol.14 , pp. 485-491
    • Rosenthal, E.1
  • 28
  • 29
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:1997;4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 31
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonucleases
    • Chirgwin J.M., Przybla A.E., MacDonald R.J., Rutter W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonucleases. Biochemistry. 18:1979;241-245.
    • (1979) Biochemistry , vol.18 , pp. 241-245
    • Chirgwin, J.M.1    Przybla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 32
    • 0031109750 scopus 로고    scopus 로고
    • The genes of the lysosomal cysteine proteinases cathepsin B, H, L, and S map to different mouse chromosomes
    • Deussing J., Roth W., Rommerskirch W., Wiederanders B., von Figura K., Peters C. The genes of the lysosomal cysteine proteinases cathepsin B, H, L, and S map to different mouse chromosomes. Mamm. Genome. 8:1997;241-245.
    • (1997) Mamm. Genome , vol.8 , pp. 241-245
    • Deussing, J.1    Roth, W.2    Rommerskirch, W.3    Wiederanders, B.4    Von Figura, K.5    Peters, C.6
  • 33
    • 0022446621 scopus 로고
    • Comparison of three actin-coding sequences in the mouse: Evolutionary relationships between the actin genes of warm-blooded vertebrates
    • Alonso S., Minty A., Bourlet Y., Buckingham M.E. Comparison of three actin-coding sequences in the mouse: evolutionary relationships between the actin genes of warm-blooded vertebrates. J. Mol. Evol. 23:1986;11-22.
    • (1986) J. Mol. Evol. , vol.23 , pp. 11-22
    • Alonso, S.1    Minty, A.2    Bourlet, Y.3    Buckingham, M.E.4
  • 35
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulated translation by eukaryotic ribosomes
    • Kozack M. Point mutations define a sequence flanking the AUG initiator codon that modulated translation by eukaryotic ribosomes. Cell. 44:1986;283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozack, M.1
  • 36
    • 0023046815 scopus 로고
    • An new method for predicting signal sequence cleavage sites
    • von Heijne G. An new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:1986;4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 38
    • 0027102589 scopus 로고
    • The genes coding for phosphoenolpyruvate carboxykinase-1 (PCK1) and neuronal nicotinic acetylcholine receptor alpha-4 subunit (CHRNA4) map to human chromosome 20, extending the known region of homology with mouse chromosome 2
    • Pilz A.J., Willer E., Povey S., Abbott C.M. The genes coding for phosphoenolpyruvate carboxykinase-1 (PCK1) and neuronal nicotinic acetylcholine receptor alpha-4 subunit (CHRNA4) map to human chromosome 20, extending the known region of homology with mouse chromosome 2. Ann. Hum. Genet. 56:1992;289-293.
    • (1992) Ann. Hum. Genet. , vol.56 , pp. 289-293
    • Pilz, A.J.1    Willer, E.2    Povey, S.3    Abbott, C.M.4
  • 39
    • 0019363396 scopus 로고
    • Organization and expression of eukaryotic split genes coding for proteins
    • Breathnach R., Chambon P. Organization and expression of eukaryotic split genes coding for proteins. Annu. Rev. Biochem. 50:1981;349-383.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 40
    • 0021683084 scopus 로고
    • Characterization of the expressed gene and several processed pseudogenes for the mouse ribosomal protein L30 gene family
    • Wiedemann L.M., Perry R.P. Characterization of the expressed gene and several processed pseudogenes for the mouse ribosomal protein L30 gene family. Mol. Cell Biol. 4:1984;2518-2528.
    • (1984) Mol. Cell Biol. , vol.4 , pp. 2518-2528
    • Wiedemann, L.M.1    Perry, R.P.2
  • 41
    • 0029089618 scopus 로고
    • The mei-41 gne of D. melanogaster is a structural and functional homolog of the human ataxia telangiectasia gene
    • Hari K.L., Santerre A., Sekelsky J.J., McKim K.S., Boyd J.B., Hawley R.S. The mei-41 gne of D. melanogaster is a structural and functional homolog of the human ataxia telangiectasia gene. Cell. 82:1995;815-821.
    • (1995) Cell , vol.82 , pp. 815-821
    • Hari, K.L.1    Santerre, A.2    Sekelsky, J.J.3    McKim, K.S.4    Boyd, J.B.5    Hawley, R.S.6
  • 42
    • 0030754723 scopus 로고    scopus 로고
    • The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking
    • Lusson J., Benjannet S., Hamelin J., Savaria D., Chretien M., Seidah N.G. The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking. Biochem. J. 326:1997;737-744.
    • (1997) Biochem. J. , vol.326 , pp. 737-744
    • Lusson, J.1    Benjannet, S.2    Hamelin, J.3    Savaria, D.4    Chretien, M.5    Seidah, N.G.6
  • 43
    • 0025922703 scopus 로고
    • G protein Gs-alpha (GNAS1), the probable candidate gene for Albright hereditary osteodystrophy, is assigned to human chromosome 20q12-q13.2
    • Gopal Rao V.V.N., Schnittger S., Hansmann I. G protein Gs-alpha (GNAS1), the probable candidate gene for Albright hereditary osteodystrophy, is assigned to human chromosome 20q12-q13.2. Genomics. 10:1991;257-261.
    • (1991) Genomics , vol.10 , pp. 257-261
    • Gopal Rao, V.V.N.1    Schnittger, S.2    Hansmann, I.3
  • 45
    • 0023318626 scopus 로고
    • Non-methylated CpG-rich islands at the human alpha-globin locus: Implications for evolution of the alpha-globin pseudogene
    • Bird A.P., Taggart M.H., Nicholls R.D., Higgs D.R. Non-methylated CpG-rich islands at the human alpha-globin locus: implications for evolution of the alpha-globin pseudogene. EMBO J. 4:1987;999-1004.
    • (1987) EMBO J. , vol.4 , pp. 999-1004
    • Bird, A.P.1    Taggart, M.H.2    Nicholls, R.D.3    Higgs, D.R.4
  • 46
    • 0025728140 scopus 로고
    • The structure of the mouse cathepsin B gene and its putative promoter
    • Qian F., Frankfater A., Chan S.J., Steiner D.F. The structure of the mouse cathepsin B gene and its putative promoter. DNA and Cell Biol. 10:1991;159-168.
    • (1991) DNA and Cell Biol. , vol.10 , pp. 159-168
    • Qian, F.1    Frankfater, A.2    Chan, S.J.3    Steiner, D.F.4
  • 48
    • 0025343071 scopus 로고
    • Identification of positive and negative reulatory elements governing cell-type-specific expression of the neural cell adhesion molecule gene
    • Hirsch M.R., Gaugler L., Deagostini-Bazin H., Bally-Cuif L., Goridis C. Identification of positive and negative reulatory elements governing cell-type-specific expression of the neural cell adhesion molecule gene. Mol. Cell Biol. 10:1990;1959-1968.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1959-1968
    • Hirsch, M.R.1    Gaugler, L.2    Deagostini-Bazin, H.3    Bally-Cuif, L.4    Goridis, C.5
  • 49
    • 0025025394 scopus 로고
    • Transcription factor PEA3 participates in the induction of urokinase plasminogen activator transcription in murine keratinocytes stimulated with epidermal growth factor or phorbol-ester
    • Rorth P., Nerlov C., Blasi F., Johnsen M. Transcription factor PEA3 participates in the induction of urokinase plasminogen activator transcription in murine keratinocytes stimulated with epidermal growth factor or phorbol-ester. Nucleic Acids Res. 18:1990;5009-5017.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5009-5017
    • Rorth, P.1    Nerlov, C.2    Blasi, F.3    Johnsen, M.4
  • 50
    • 0025915612 scopus 로고
    • A nuclear factor binds to metal regulatory elements of the mouse encoding metallothionein-I gene
    • Labbe S., Prevost J., Remondelli P., Leone A., Seguin C. A nuclear factor binds to metal regulatory elements of the mouse encoding metallothionein-I gene. Nucleic Acids Res. 19:1991;4225-4231.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4225-4231
    • Labbe, S.1    Prevost, J.2    Remondelli, P.3    Leone, A.4    Seguin, C.5
  • 51
    • 0024437214 scopus 로고
    • Muscle-specific gene expression controlled by a regulatory element lacking a MyoD1-binding site
    • Baldwin T.J., Burden S.J. Muscle-specific gene expression controlled by a regulatory element lacking a MyoD1-binding site. Nature. 341:1989;716-720.
    • (1989) Nature , vol.341 , pp. 716-720
    • Baldwin, T.J.1    Burden, S.J.2
  • 52
    • 0025823908 scopus 로고
    • Characterization of hypersensitive sites, protein-binding motifs, and regulatory elements in both promoters of the mouse porphobilinogen deaminase gene
    • Porcher C., Pitiot G., Plumb M., Lowe S., de Verneuil H., Grandchamp N. Characterization of hypersensitive sites, protein-binding motifs, and regulatory elements in both promoters of the mouse porphobilinogen deaminase gene. J. Biol. Chem. 226:1991;10562-10569.
    • (1991) J. Biol. Chem. , vol.226 , pp. 10562-10569
    • Porcher, C.1    Pitiot, G.2    Plumb, M.3    Lowe, S.4    De Verneuil, H.5    Grandchamp, N.6
  • 53
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman S.B., Wunsch C.D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:1970;443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.