메뉴 건너뛰기




Volumn 64, Issue 4, 2009, Pages 819-825

Positive selection of three chitinase genes of the family 18 of glycoside hydrolases in mammals

Author keywords

Chitinase; Glycoside hydrolase family GH18; Positive selection; Protein evolution

Indexed keywords

EUKARYOTA; MAMMALIA; PROKARYOTA;

EID: 70349748467     PISSN: 00063088     EISSN: 13369563     Source Type: Journal    
DOI: 10.2478/s11756-009-0117-4     Document Type: Article
Times cited : (6)

References (54)
  • 7
    • 0028799896 scopus 로고
    • Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages
    • Boot R.G., Renkema G.H., Strijland A., van Zonneveld A.J. & Aerts J.M. 1995. Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J. Biol. Chem. 270: 26252-26256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26252-26256
    • Boot, R.G.1    Renkema, G.H.2    Strijland, A.3    van Zonneveld, A.J.4    Aerts, J.M.5
  • 9
    • 0032975495 scopus 로고    scopus 로고
    • Strong induction of members of the chitinase family of proteins in atherosclerosis: Chitotriosidase and human cartilage gp-39 expressed in lesion macrophages
    • Boot R.G., van Achterberg T.A., van Aken B.E., Renkema G.H., Jacobs M.J., Aerts J.M. & de Vries C.J. 1999. Strong induction of members of the chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilage gp-39 expressed in lesion macrophages. Arterioscler. Thromb. Vasc. Biol. 19: 687-694.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 687-694
    • Boot, R.G.1    van Achterberg, T.A.2    van Aken, B.E.3    Renkema, G.H.4    Jacobs, M.J.5    Aerts, J.M.6    de Vries, C.J.7
  • 10
    • 35548984723 scopus 로고    scopus 로고
    • Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases
    • Bussink A.P., Speijer D., Aerts J.M. & Boot R.G. 2007. Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases. Genetics 177: 959-970.
    • (2007) Genetics , vol.177 , pp. 959-970
    • Bussink, A.P.1    Speijer, D.2    Aerts, J.M.3    Boot, R.G.4
  • 12
    • 40149089819 scopus 로고    scopus 로고
    • A single histidine residue modulates enzymatic activity in acidic mammalian chitinase
    • Bussink A.P., Vreede J., Aerts J.M. & Boot R.G. 2008. A single histidine residue modulates enzymatic activity in acidic mammalian chitinase. FEBS Lett. 582: 931-935.
    • (2008) FEBS Lett. , vol.582 , pp. 931-935
    • Bussink, A.P.1    Vreede, J.2    Aerts, J.M.3    Boot, R.G.4
  • 13
    • 24644465726 scopus 로고    scopus 로고
    • Chitinases and chitinase-like proteins in T(H)2 inflammation and asthma
    • Elias J.A., Homer R.J., Hamid Q. & Lee C.G. 2005. Chitinases and chitinase-like proteins in T(H)2 inflammation and asthma. J. Allergy Clin. Immunol. 116: 497-500.
    • (2005) J. Allergy Clin. Immunol. , vol.116 , pp. 497-500
    • Elias, J.A.1    Homer, R.J.2    Hamid, Q.3    Lee, C.G.4
  • 14
    • 0026709204 scopus 로고
    • What's new in chitinase research?
    • Flach J., Pilet P.E. & Jolles P. 1992. What's new in chitinase research? Experientia 48: 701-716.
    • (1992) Experientia , vol.48 , pp. 701-716
    • Flach, J.1    Pilet, P.E.2    Jolles, P.3
  • 16
    • 0141580438 scopus 로고    scopus 로고
    • Cellular expression of the gut chitinase in the stomach of frogs Xenopus laevis and Rana catesbeiana
    • Fujimoto W., Kimura K. & Iwanaga T. 2002. Cellular expression of the gut chitinase in the stomach of frogs Xenopus laevis and Rana catesbeiana. Biomed. Res. 23: 91-99.
    • (2002) Biomed. Res. , vol.23 , pp. 91-99
    • Fujimoto, W.1    Kimura, K.2    Iwanaga, T.3
  • 17
    • 0034236249 scopus 로고    scopus 로고
    • Chitinolytic enzymes: Catalysis, substrate binding, and their application
    • Fukamizo T. 2000. Chitinolytic enzymes: catalysis, substrate binding, and their application. Curr. Protein Pept. Sci. 1: 105-124.
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 105-124
    • Fukamizo, T.1
  • 18
    • 34547842599 scopus 로고    scopus 로고
    • Chitinase family GH18: Evolutionary insights from the genomic history of a diverse protein family
    • Funkhouser J.D. & Aronson N.N., Jr. 2007. Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family. BMC Evol. Biol. 7: 96.
    • (2007) BMC Evol. Biol. , vol.7 , pp. 96
    • Funkhouser, J.D.1    Aronson Jr., N.N.2
  • 19
    • 0141621106 scopus 로고    scopus 로고
    • Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39
    • Fusetti F., Pijning T., Kalk K.H., Bos E. & Dijkstra B.W. 2003. Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39. J. Biol. Chem. 278: 37753-37760.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37753-37760
    • Fusetti, F.1    Pijning, T.2    Kalk, K.H.3    Bos, E.4    Dijkstra, B.W.5
  • 20
  • 21
    • 0027505001 scopus 로고
    • Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family
    • Hakala B.E., White C. & Recklies A.D. 1993. Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. J. Biol. Chem. 268: 25803-25810.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25803-25810
    • Hakala, B.E.1    White, C.2    Recklies, A.D.3
  • 22
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280: 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 23
    • 0033291773 scopus 로고    scopus 로고
    • Classification of chitinases modules
    • Henrissat B. 1999. Classification of chitinases modules. EXS 87: 137-156.
    • (1999) EXS , vol.87 , pp. 137-156
    • Henrissat, B.1
  • 24
    • 0043031435 scopus 로고    scopus 로고
    • Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes
    • Houston D.R., Recklies A.D., Krupa J.C. & van Aalten D.M. 2003. Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes. J. Biol. Chem. 278: 30206-30212.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30206-30212
    • Houston, D.R.1    Recklies, A.D.2    Krupa, J.C.3    van Aalten, D.M.4
  • 25
    • 0037373324 scopus 로고    scopus 로고
    • Tests for positive selection on immune and reproductive genes in closely related species of the murine genus mus
    • Jansa S.A., Lundrigan B.L. & Tucker P.K. 2003. Tests for positive selection on immune and reproductive genes in closely related species of the murine genus mus. J. Mol. Evol. 56: 294-307.
    • (2003) J. Mol. Evol. , vol.56 , pp. 294-307
    • Jansa, S.A.1    Lundrigan, B.L.2    Tucker, P.K.3
  • 29
    • 17044374400 scopus 로고    scopus 로고
    • Expression of YKL-40 by peritumoral macrophages in human small cell lung cancer
    • Junker N., Johansen J.S., Andersen C.B. & Kristjansen P.E. 2005. Expression of YKL-40 by peritumoral macrophages in human small cell lung cancer. Lung Cancer 48: 223-231.
    • (2005) Lung Cancer , vol.48 , pp. 223-231
    • Junker, N.1    Johansen, J.S.2    Andersen, C.B.3    Kristjansen, P.E.4
  • 30
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases - regulation and function
    • Kasprzewska A. 2003. Plant chitinases - regulation and function. Cell. Mol. Biol. Lett. 8: 809-824.
    • (2003) Cell. Mol. Biol. Lett. , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 31
    • 0035112853 scopus 로고    scopus 로고
    • Concentration and localization of YKL-40 in hip joint diseases
    • Kawasaki M., Hasegawa Y., Kondo S. & Iwata H. 2001. Concentration and localization of YKL-40 in hip joint diseases. J. Rheumatol. 28: 341-345.
    • (2001) J. Rheumatol. , vol.28 , pp. 341-345
    • Kawasaki, M.1    Hasegawa, Y.2    Kondo, S.3    Iwata, H.4
  • 32
    • 0031586597 scopus 로고    scopus 로고
    • Induction and expression of human cartilage glycoprotein 39 in rheumatoid inflammatory and peripheral blood monocyte-derived macrophages
    • Kirkpatrick R.B., Emery J.G., Connor J.R., Dodds R., Lysko P.G. & Rosenberg M. 1997. Induction and expression of human cartilage glycoprotein 39 in rheumatoid inflammatory and peripheral blood monocyte-derived macrophages. Exp. Cell. Res. 237: 46-54.
    • (1997) Exp. Cell. Res. , vol.237 , pp. 46-54
    • Kirkpatrick, R.B.1    Emery, J.G.2    Connor, J.R.3    Dodds, R.4    Lysko, P.G.5    Rosenberg, M.6
  • 33
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S., Tamura K. & Nei M. 2004. MEGA3: integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief. Bioinform. 5: 150-163.
    • (2004) Brief. Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 35
    • 0030791307 scopus 로고    scopus 로고
    • Evolution by the birth-and-death process in multigene families of the vertebrate immune system
    • Nei M., Gu X. & Sitnikova T. 1997. Evolution by the birth-and-death process in multigene families of the vertebrate immune system. Proc. Natl. Acad. Sci. USA 94: 7799-7806.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7799-7806
    • Nei, M.1    Gu, X.2    Sitnikova, T.3
  • 36
    • 0031571093 scopus 로고    scopus 로고
    • Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation
    • Rehli M., Krause S.W. & Andreesen R. 1997. Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation. Genomics 43: 221-225.
    • (1997) Genomics , vol.43 , pp. 221-225
    • Rehli, M.1    Krause, S.W.2    Andreesen, R.3
  • 38
    • 0032518453 scopus 로고    scopus 로고
    • Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages
    • Renkema G.H., Boot R.G., Au F.L., Donker-Koopman W.E., Strijland A., Muijsers A.O., Hrebicek M. & Aerts J.M. 1998. Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. Eur. J. Biochem. 251: 504-509.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 504-509
    • Renkema, G.H.1    Boot, R.G.2    Au, F.L.3    Donker-Koopman, W.E.4    Strijland, A.5    Muijsers, A.O.6    Hrebicek, M.7    Aerts, J.M.8
  • 39
    • 0032735186 scopus 로고    scopus 로고
    • Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member
    • Saito A., Ozaki K., Fujiwara T., Nakamura Y. & Tanigami A. 1999. Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member. Gene 239: 325-331.
    • (1999) Gene , vol.239 , pp. 325-331
    • Saito, A.1    Ozaki, K.2    Fujiwara, T.3    Nakamura, Y.4    Tanigami, A.5
  • 40
    • 28444469149 scopus 로고    scopus 로고
    • Evolutionary and mechanistic relationships between glycosidases acting on α- and β-bonds
    • Stam M.R., Blanc E., Coutinho P.M. & Henrissat B. 2005. Evolutionary and mechanistic relationships between glycosidases acting on α- and β-bonds. Carbohydr. Res. 340: 2728-2734.
    • (2005) Carbohydr. Res. , vol.340 , pp. 2728-2734
    • Stam, M.R.1    Blanc, E.2    Coutinho, P.M.3    Henrissat, B.4
  • 41
    • 0036321175 scopus 로고    scopus 로고
    • Cellular expression of gut chitinase mRNA in the gastrointestinal tract of mice and chickens
    • Suzuki M., Fujimoto W., Goto M., Morimatsu M., Syuto B. & Iwanaga T. 2002. Cellular expression of gut chitinase mRNA in the gastrointestinal tract of mice and chickens. J. Histochem. Cytochem. 50: 1081-1089.
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 1081-1089
    • Suzuki, M.1    Fujimoto, W.2    Goto, M.3    Morimatsu, M.4    Syuto, B.5    Iwanaga, T.6
  • 42
    • 0035957018 scopus 로고    scopus 로고
    • Positive Darwinian selection drives the evolution of several female reproductive proteins in mammals
    • Swanson W.J., Yang Z., Wolfner M.F. & Aquadro C.F. 2001. Positive Darwinian selection drives the evolution of several female reproductive proteins in mammals. Proc. Natl. Acad. Sci. USA 98: 2509-2514.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2509-2514
    • Swanson, W.J.1    Yang, Z.2    Wolfner, M.F.3    Aquadro, C.F.4
  • 43
    • 0038386053 scopus 로고    scopus 로고
    • Chitin - the undisputed biomolecule of great potential
    • Tharanathan R.N. & Kittur F.S. 2003. Chitin - the undisputed biomolecule of great potential. Crit. Rev. Food Sci. Nutr. 43: 61-87.
    • (2003) Crit. Rev. Food Sci. Nutr. , vol.43 , pp. 61-87
    • Tharanathan, R.N.1    Kittur, F.S.2
  • 50
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang Z. 1997. PAML: a program package for phylogenetic analysis by maximum likelihood. Comput. Appl. Biosci. 13: 555-556.
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 555-556
    • Yang, Z.1
  • 51
    • 16344378246 scopus 로고    scopus 로고
    • Bayes empirical bayes inference of amino acid sites under positive selection
    • Yang Z., Wong W.S. & Nielsen R. 2005. Bayes empirical bayes inference of amino acid sites under positive selection. Mol. Biol. Evol. 22: 1107-1118.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1107-1118
    • Yang, Z.1    Wong, W.S.2    Nielsen, R.3
  • 53
    • 24644445672 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of mouse chitotriosidase
    • Zheng T., Rabach M., Chen N.Y., Rabach L., Hu X., Elias J.A. & Zhu Z. 2005. Molecular cloning and functional characterization of mouse chitotriosidase. Gene 357: 37-46.
    • (2005) Gene , vol.357 , pp. 37-46
    • Zheng, T.1    Rabach, M.2    Chen, N.Y.3    Rabach, L.4    Hu, X.5    Elias, J.A.6    Zhu, Z.7
  • 54
    • 2942668626 scopus 로고    scopus 로고
    • Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation
    • Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q. & Elias J.A. 2004. Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science 304: 1678-1682.
    • (2004) Science , vol.304 , pp. 1678-1682
    • Zhu, Z.1    Zheng, T.2    Homer, R.J.3    Kim, Y.K.4    Chen, N.Y.5    Cohn, L.6    Hamid, Q.7    Elias, J.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.