메뉴 건너뛰기




Volumn 41, Issue 2, 2013, Pages 189-199

Comparative genomic and phylogenetic analyses of the intelectin gene family: Implications for their origin and evolution

Author keywords

Comparative genomics; Evolution; FReD; Intelectin

Indexed keywords

CORTICAL GRANULE LECTIN; LECTIN; UNCLASSIFIED DRUG;

EID: 84880166649     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2013.04.016     Document Type: Article
Times cited : (24)

References (41)
  • 1
    • 0033119346 scopus 로고    scopus 로고
    • A unique primary structure, cDNA cloning and function of a galactose-specific lectin from ascidian plasma
    • Abe Y., Tokuda M., Ishimoto R., Azumi K., Yokosawa H. A unique primary structure, cDNA cloning and function of a galactose-specific lectin from ascidian plasma. Eur. J. Biochem. 1999, 261:33-39.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 33-39
    • Abe, Y.1    Tokuda, M.2    Ishimoto, R.3    Azumi, K.4    Yokosawa, H.5
  • 2
    • 0030831258 scopus 로고    scopus 로고
    • A family of fibrinogen related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection
    • Adema C.M., Hertel L.A., Miller R.D., Loker E.S. A family of fibrinogen related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection. Proc. Natl. Acad. Sci. USA 1997, 94:8691-8696.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8691-8696
    • Adema, C.M.1    Hertel, L.A.2    Miller, R.D.3    Loker, E.S.4
  • 3
    • 34247339709 scopus 로고    scopus 로고
    • Intelectin gene from the grass carp Ctenopharyngodon idella: cDNA cloning, tissue expression, and immunohistochemical localization
    • Chang M.X., Nie P. Intelectin gene from the grass carp Ctenopharyngodon idella: cDNA cloning, tissue expression, and immunohistochemical localization. Fish Shellfish Immunol. 2007, 23:128-140.
    • (2007) Fish Shellfish Immunol. , vol.23 , pp. 128-140
    • Chang, M.X.1    Nie, P.2
  • 4
    • 33846653740 scopus 로고    scopus 로고
    • Innate immune defenses in the intestinal tract
    • Dann S.M., Eckmann L. Innate immune defenses in the intestinal tract. Curr. Opin. Gastroenterol. 2007, 23(2):115-120.
    • (2007) Curr. Opin. Gastroenterol. , vol.23 , Issue.2 , pp. 115-120
    • Dann, S.M.1    Eckmann, L.2
  • 5
    • 83555178422 scopus 로고    scopus 로고
    • Isolation and determination of the primary structure of a lectin protein from the serum of the American alligator (Alligator mississippiensis)
    • Darville L.N., Merchant M.E., Maccha V., Siddavarapu V.R., Hasan A., Murray K.K. Isolation and determination of the primary structure of a lectin protein from the serum of the American alligator (Alligator mississippiensis). Comp. Biochem. Physiol. B: Biochem. Mol. Biol. 2012, 161(2):161-169. 10.1016/j.cbpb.2011.11.001.
    • (2012) Comp. Biochem. Physiol. B: Biochem. Mol. Biol. , vol.161 , Issue.2 , pp. 161-169
    • Darville, L.N.1    Merchant, M.E.2    Maccha, V.3    Siddavarapu, V.R.4    Hasan, A.5    Murray, K.K.6
  • 6
    • 37849185741 scopus 로고    scopus 로고
    • Gene transcript changes in individual rainbow trout livers following an inflammatory stimulus
    • Gerwick L., Corley-Smith G., Bayne C.J. Gene transcript changes in individual rainbow trout livers following an inflammatory stimulus. Fish Shellfish Immunol. 2007, 22(3):157-171.
    • (2007) Fish Shellfish Immunol. , vol.22 , Issue.3 , pp. 157-171
    • Gerwick, L.1    Corley-Smith, G.2    Bayne, C.J.3
  • 8
    • 0032578849 scopus 로고    scopus 로고
    • Cloning of the novel gene intelectin, which is expressed in intestinal paneth cells in mice
    • Komiya T., Tanigawa Y., Hirohashi S. Cloning of the novel gene intelectin, which is expressed in intestinal paneth cells in mice. Biochem. Biophys. Res. Commun. 1998, 251:759-762.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 759-762
    • Komiya, T.1    Tanigawa, Y.2    Hirohashi, S.3
  • 9
    • 0030895387 scopus 로고    scopus 로고
    • Cloning and expression of a Xenopus laevis oocyte lectin and characterization of its mRNA levels during early development
    • Lee J.K., Buckhaults P., Wilkes C., Teilhet M., King M.L., Moremen K.W., Pierce M. Cloning and expression of a Xenopus laevis oocyte lectin and characterization of its mRNA levels during early development. Glycobiology 1997, 7:367-372.
    • (1997) Glycobiology , vol.7 , pp. 367-372
    • Lee, J.K.1    Buckhaults, P.2    Wilkes, C.3    Teilhet, M.4    King, M.L.5    Moremen, K.W.6    Pierce, M.7
  • 11
    • 17644409070 scopus 로고    scopus 로고
    • The X-lectins: a new family with homology to the Xenopus laevis oocyte lectin XL-35
    • Lee J.K., Baum L.G., Moremen K., Pierce M. The X-lectins: a new family with homology to the Xenopus laevis oocyte lectin XL-35. Glycoconj. J. 2004, 21(8-9):443-450.
    • (2004) Glycoconj. J. , vol.21 , Issue.8-9 , pp. 443-450
    • Lee, J.K.1    Baum, L.G.2    Moremen, K.3    Pierce, M.4
  • 12
    • 67649376348 scopus 로고    scopus 로고
    • The evolutionarily dynamic IFN-inducible GTPase proteins play conserved immune functions in vertebrates and cephalochordates
    • Li G., Zhang J., Sun Y., Wang H., Wang Y. The evolutionarily dynamic IFN-inducible GTPase proteins play conserved immune functions in vertebrates and cephalochordates. Mol. Biol. Evol. 2009, 26(7):1619-1630. 10.1093/molbev/msp074.
    • (2009) Mol. Biol. Evol. , vol.26 , Issue.7 , pp. 1619-1630
    • Li, G.1    Zhang, J.2    Sun, Y.3    Wang, H.4    Wang, Y.5
  • 13
    • 62749176361 scopus 로고    scopus 로고
    • Characterization and comparative analyses of zebrafish intelectins: highly conserved sequences, diversified structures and functions
    • Lin B., Cao Z., Su P., Zhang H., Li M., Lin Y., Zhao D., Shen Y., Jing C., Chen S., Xu A. Characterization and comparative analyses of zebrafish intelectins: highly conserved sequences, diversified structures and functions. Fish Shellfish Immunol. 2009, 26(3):396-405.
    • (2009) Fish Shellfish Immunol. , vol.26 , Issue.3 , pp. 396-405
    • Lin, B.1    Cao, Z.2    Su, P.3    Zhang, H.4    Li, M.5    Lin, Y.6    Zhao, D.7    Shen, Y.8    Jing, C.9    Chen, S.10    Xu, A.11
  • 15
    • 0031697412 scopus 로고    scopus 로고
    • Ficolins and the fibrinogen-like domain
    • Lu J., Le Y. Ficolins and the fibrinogen-like domain. Immunobiology 1998, 199:190-199.
    • (1998) Immunobiology , vol.199 , pp. 190-199
    • Lu, J.1    Le, Y.2
  • 17
    • 63049096659 scopus 로고    scopus 로고
    • Evolution of the multifaceted eukaryotic akirin gene family
    • Macqueen D.J., Johnston I.A. Evolution of the multifaceted eukaryotic akirin gene family. BMC Evol. Biol. 2009, 9:34. 10.1186/1471-2148-9-34.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 34
    • Macqueen, D.J.1    Johnston, I.A.2
  • 18
    • 77953374499 scopus 로고    scopus 로고
    • Ficolins: complement-activating lectins involved in innate immunity
    • Matsushita M. Ficolins: complement-activating lectins involved in innate immunity. J. Innate Immun. 2010, 2:24-32.
    • (2010) J. Innate Immun. , vol.2 , pp. 24-32
    • Matsushita, M.1
  • 19
    • 14844317340 scopus 로고    scopus 로고
    • Isolation, characterization, and extra-embryonic secretion of the Xenopus laevis embryonic epidermal lectin, XEEL
    • Nagata S. Isolation, characterization, and extra-embryonic secretion of the Xenopus laevis embryonic epidermal lectin, XEEL. Glycobiology 2005, 15(3):281-290.
    • (2005) Glycobiology , vol.15 , Issue.3 , pp. 281-290
    • Nagata, S.1
  • 20
    • 0023044272 scopus 로고
    • Isolation and characterization of a lectin from the cortical granules of Xenopus laevis eggs
    • Nishihara T., Wyrick R.E., Working P.K., Chen Y.H., Hedrick J.L. Isolation and characterization of a lectin from the cortical granules of Xenopus laevis eggs. Biochemistry 1986, 25(20):6013-6020.
    • (1986) Biochemistry , vol.25 , Issue.20 , pp. 6013-6020
    • Nishihara, T.1    Wyrick, R.E.2    Working, P.K.3    Chen, Y.H.4    Hedrick, J.L.5
  • 21
    • 77649232845 scopus 로고    scopus 로고
    • Changes of serum omentin-1 levels in normal subjects and in patients with impaired glucose regulation and with newly diagnosed and untreated type 2 diabetes
    • Pan H.Y., Guo L., Li Q. Changes of serum omentin-1 levels in normal subjects and in patients with impaired glucose regulation and with newly diagnosed and untreated type 2 diabetes. Diabetes Res. Clin. Pract. 2011, 88(1):29-33.
    • (2011) Diabetes Res. Clin. Pract. , vol.88 , Issue.1 , pp. 29-33
    • Pan, H.Y.1    Guo, L.2    Li, Q.3
  • 22
    • 3242811092 scopus 로고    scopus 로고
    • Innate BALB/c enteric epithelial responses to Trichinella spiralis: inducible expression of a novel goblet cell lectin, intelectin-2, and its natural deletion in C57BL/10 mice
    • Pemberton A.D., Knight P.A., Gamble J., Colledge W.H., Lee J.K., Pierce M., Miller H.R. Innate BALB/c enteric epithelial responses to Trichinella spiralis: inducible expression of a novel goblet cell lectin, intelectin-2, and its natural deletion in C57BL/10 mice. J. Immunol. 2004, 173(3):1894-1901.
    • (2004) J. Immunol. , vol.173 , Issue.3 , pp. 1894-1901
    • Pemberton, A.D.1    Knight, P.A.2    Gamble, J.3    Colledge, W.H.4    Lee, J.K.5    Pierce, M.6    Miller, H.R.7
  • 23
    • 0030587536 scopus 로고    scopus 로고
    • The fertilization layer mediated block to polyspermy in Xenopus laevis: isolation of the cortical granule lectin ligand
    • Quill T.A., Hedrick J.L. The fertilization layer mediated block to polyspermy in Xenopus laevis: isolation of the cortical granule lectin ligand. Arch. Biochem. Biophys. 1996, 333(2):326-332.
    • (1996) Arch. Biochem. Biophys. , vol.333 , Issue.2 , pp. 326-332
    • Quill, T.A.1    Hedrick, J.L.2
  • 24
    • 0020479237 scopus 로고
    • Lectin from embryos and oocytes of Xenopus laevis. Purification and properties
    • Roberson M.M., Barondes S.H. Lectin from embryos and oocytes of Xenopus laevis. Purification and properties. J. Biol. Chem. 1982, 257(13):7520-7524.
    • (1982) J. Biol. Chem. , vol.257 , Issue.13 , pp. 7520-7524
    • Roberson, M.M.1    Barondes, S.H.2
  • 25
    • 0021073706 scopus 로고
    • Xenopus laevis lectin is localized at several sites in Xenopus oocytes, eggs, and embryos
    • Roberson M.M., Barondes S.H. Xenopus laevis lectin is localized at several sites in Xenopus oocytes, eggs, and embryos. J. Cell Biol. 1983, 97(6):1875-1881.
    • (1983) J. Cell Biol. , vol.97 , Issue.6 , pp. 1875-1881
    • Roberson, M.M.1    Barondes, S.H.2
  • 26
    • 44749084233 scopus 로고    scopus 로고
    • Identification, cloning and tissue localization of a rainbow trout (Oncorhynchus mykiss) intelectin like protein that binds bacteria and chitin
    • Russell S., Young K.M., Smith M., Hayes M.A., Lumsden J.S. Identification, cloning and tissue localization of a rainbow trout (Oncorhynchus mykiss) intelectin like protein that binds bacteria and chitin. Fish Shellfish Immunol. 2008, 25:91-105.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 91-105
    • Russell, S.1    Young, K.M.2    Smith, M.3    Hayes, M.A.4    Lumsden, J.S.5
  • 27
  • 29
    • 0035951070 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a human intestinal lactoferrin receptor
    • Suzuki Y.A., Shin K., Lönnerdal B. Molecular cloning and functional expression of a human intestinal lactoferrin receptor. Biochemistry 2001, 40(51):15771-15779.
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15771-15779
    • Suzuki, Y.A.1    Shin, K.2    Lönnerdal, B.3
  • 30
    • 28344453346 scopus 로고    scopus 로고
    • Mammalian lactoferrin receptors: structure and function
    • Suzuki Y.A., Lopez V., Lönnerdal B. Mammalian lactoferrin receptors: structure and function. Cell. Mol. Life Sci. 2005, 62(22):2560-2575.
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.22 , pp. 2560-2575
    • Suzuki, Y.A.1    Lopez, V.2    Lönnerdal, B.3
  • 31
    • 39149133136 scopus 로고    scopus 로고
    • The two channel catfish intelectin genes exhibit highly differential patterns of tissue expression and regulation after infection with Edwardsiella ictaluri
    • Takano T., Sha Z., Peatman E., Terhune J., Liu H., Kucuktas H., Li P., Edholm E.S., Wilson M., Liu Z. The two channel catfish intelectin genes exhibit highly differential patterns of tissue expression and regulation after infection with Edwardsiella ictaluri. Dev. Comp. Immunol. 2008, 32:693-705.
    • (2008) Dev. Comp. Immunol. , vol.32 , pp. 693-705
    • Takano, T.1    Sha, Z.2    Peatman, E.3    Terhune, J.4    Liu, H.5    Kucuktas, H.6    Li, P.7    Edholm, E.S.8    Wilson, M.9    Liu, Z.10
  • 32
    • 0035968315 scopus 로고    scopus 로고
    • Human intelectin is a novel soluble lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall
    • Tsuji S., Uehori J., Matsumoto M., Suzuki Y., Matsuhisa A., Toyoshima K., Seya T. Human intelectin is a novel soluble lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall. J. Biol. Chem. 2001, 276:23456-23463.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23456-23463
    • Tsuji, S.1    Uehori, J.2    Matsumoto, M.3    Suzuki, Y.4    Matsuhisa, A.5    Toyoshima, K.6    Seya, T.7
  • 33
    • 35148882483 scopus 로고    scopus 로고
    • Differential structure and activity between human and mouse intelectin-1: human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer
    • Tsuji S., Yamashita M., Nishiyama A., Shinohara T., Li Z., Myrvik Q.N., Hoffman D.R., Henriksen R.A., Shibata Y. Differential structure and activity between human and mouse intelectin-1: human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer. Glycobiology 2007, 17(10):1045-1051.
    • (2007) Glycobiology , vol.17 , Issue.10 , pp. 1045-1051
    • Tsuji, S.1    Yamashita, M.2    Nishiyama, A.3    Shinohara, T.4    Li, Z.5    Myrvik, Q.N.6    Hoffman, D.R.7    Henriksen, R.A.8    Shibata, Y.9
  • 34
    • 64549117342 scopus 로고    scopus 로고
    • Capture of heat-killed Mycobacterium bovis bacillus Calmette-Guérin by intelectin-1 deposited on cell surfaces
    • Tsuji S., Yamashita M., Hoffman D.R., Nishiyama A., Shinohara T., Ohtsu T., Shibata Y. Capture of heat-killed Mycobacterium bovis bacillus Calmette-Guérin by intelectin-1 deposited on cell surfaces. Glycobiology 2009, 19(5):518-526.
    • (2009) Glycobiology , vol.19 , Issue.5 , pp. 518-526
    • Tsuji, S.1    Yamashita, M.2    Hoffman, D.R.3    Nishiyama, A.4    Shinohara, T.5    Ohtsu, T.6    Shibata, Y.7
  • 36
    • 80455178899 scopus 로고    scopus 로고
    • A unique epidermal mucus lectin identified from catfish (Silurus asotus): first evidence of intelectin in fish skin slime
    • Tsutsui S., Komatsu Y., Sugiura T., Araki K., Nakamura O. A unique epidermal mucus lectin identified from catfish (Silurus asotus): first evidence of intelectin in fish skin slime. J. Biochem. 2011, 150(5):501-514.
    • (2011) J. Biochem. , vol.150 , Issue.5 , pp. 501-514
    • Tsutsui, S.1    Komatsu, Y.2    Sugiura, T.3    Araki, K.4    Nakamura, O.5
  • 38
    • 33746658999 scopus 로고    scopus 로고
    • Intelectin: a novel lipid raft-associated protein in the enterocyte brush border
    • Wrackmeyer U., Hansen G.H., Seya T., Danielsen E.M. Intelectin: a novel lipid raft-associated protein in the enterocyte brush border. Biochemistry 2006, 45:9188-9197.
    • (2006) Biochemistry , vol.45 , pp. 9188-9197
    • Wrackmeyer, U.1    Hansen, G.H.2    Seya, T.3    Danielsen, E.M.4
  • 39
    • 84861478693 scopus 로고    scopus 로고
    • Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN
    • Yan J., Wang J., Zhao Y., Zhang J., Bai C., Zhang C., Zhang C., Li K., Zhang H., Du X., Feng L. Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN. Fish Shellfish Immunol. 2012, 33(1):11-20.
    • (2012) Fish Shellfish Immunol. , vol.33 , Issue.1 , pp. 11-20
    • Yan, J.1    Wang, J.2    Zhao, Y.3    Zhang, J.4    Bai, C.5    Zhang, C.6    Zhang, C.7    Li, K.8    Zhang, H.9    Du, X.10    Feng, L.11
  • 41
    • 0022532747 scopus 로고
    • Galactose-specific lectin in the hemolymph of solitary ascidian, Halocynthia roretzi. Molecular, binding and functional properties
    • Yokosawa H., Harada K., Igarashi K., Abe Y., Takahashi K., Ishii S. Galactose-specific lectin in the hemolymph of solitary ascidian, Halocynthia roretzi. Molecular, binding and functional properties. Biochim. Biophys. Acta 1986, 870(2):242-247.
    • (1986) Biochim. Biophys. Acta , vol.870 , Issue.2 , pp. 242-247
    • Yokosawa, H.1    Harada, K.2    Igarashi, K.3    Abe, Y.4    Takahashi, K.5    Ishii, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.