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Volumn 21, Issue 2, 1999, Pages 193-199

Characterization of the mouse collectin gene locus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 0033172842     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.21.2.3681     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0024324970 scopus 로고
    • Structures and functions associated with the group of mammalian lectins containing collagen-like sequences
    • Thiel, S., and K. B. Reid. 1989. Structures and functions associated with the group of mammalian lectins containing collagen-like sequences. FEBS Lett. 250:78-84.
    • (1989) FEBS Lett. , vol.250 , pp. 78-84
    • Thiel, S.1    Reid, K.B.2
  • 3
    • 0025230703 scopus 로고
    • Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme Clr2Cls2 complex, of the classical pathway of complement, without involvement of Clq
    • Lu, J. H., S. Thiel, H. Wiedemann, T. Timpl, and K. B. Reid. 1990. Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme Clr2Cls2 complex, of the classical pathway of complement, without involvement of Clq. Immunol. 144:2287-2294.
    • (1990) Immunol. , vol.144 , pp. 2287-2294
    • Lu, J.H.1    Thiel, S.2    Wiedemann, H.3    Timpl, T.4    Reid, K.B.5
  • 4
    • 0026445745 scopus 로고
    • Activation of the classical complement pathway by mannose-binding protein in association with a novel Cls-like serine protease
    • Matsushita, M., and T. Fujita. 1992. Activation of the classical complement pathway by mannose-binding protein in association with a novel Cls-like serine protease. J. Exp. Med 176:1497-1502.
    • (1992) J. Exp. Med , vol.176 , pp. 1497-1502
    • Matsushita, M.1    Fujita, T.2
  • 5
    • 0028343828 scopus 로고
    • Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein
    • Sato, T., Y. Endo, M. Matsushita, and T. Fujita. 1994. Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein. Int. Immunol. 6:665-669.
    • (1994) Int. Immunol. , vol.6 , pp. 665-669
    • Sato, T.1    Endo, Y.2    Matsushita, M.3    Fujita, T.4
  • 6
    • 0028146354 scopus 로고
    • Bovine conglutinin binds to an oligosaccharide determinant presented by iC3b, but not by C3, C3b or C3c
    • Laursen, S. B., S. Thiel, B. Teisner, U. Holmskov, Y Wang, R. B. Sim, and J. C. Jensenius. 1994. Bovine conglutinin binds to an oligosaccharide determinant presented by iC3b, but not by C3, C3b or C3c. Immunology 81:648-654.
    • (1994) Immunology , vol.81 , pp. 648-654
    • Laursen, S.B.1    Thiel, S.2    Teisner, B.3    Holmskov, U.4    Wang, Y.5    Sim, R.B.6    Jensenius, J.C.7
  • 7
    • 0030784825 scopus 로고    scopus 로고
    • Immunomodulatory functions of surfactant
    • Wright, J. R. 1997. Immunomodulatory functions of surfactant. Physiol. Rev. 77:931-962.
    • (1997) Physiol. Rev. , vol.77 , pp. 931-962
    • Wright, J.R.1
  • 8
    • 0032033749 scopus 로고    scopus 로고
    • The human ortholog of rhesus mannose-binding protein-A gene is an expressed pseudogene that localizes to chromosome 10
    • Guo, N., T. Mogues, S. Weremowicz, C. C. Morton, and K. N. Sastry. 1998. The human ortholog of rhesus mannose-binding protein-A gene is an expressed pseudogene that localizes to chromosome 10. Mamm. Genome 9:246-249.
    • (1998) Mamm. Genome , vol.9 , pp. 246-249
    • Guo, N.1    Mogues, T.2    Weremowicz, S.3    Morton, C.C.4    Sastry, K.N.5
  • 9
    • 0032015118 scopus 로고    scopus 로고
    • Organization of the human SP-A and SP-D loci at 10q22 q23. Physical and radiation hybrid mapping reveal gene order and orientation
    • Hoover, R. R., and J. Floros. 1998. Organization of the human SP-A and SP-D loci at 10q22 q23. Physical and radiation hybrid mapping reveal gene order and orientation. Am. J. Respir. Cell Mol. Biol. 18:353-362.
    • (1998) Am. J. Respir. Cell Mol. Biol. , vol.18 , pp. 353-362
    • Hoover, R.R.1    Floros, J.2
  • 11
    • 0028971996 scopus 로고
    • Mouse surfactant protein-D. cDNA cloning, characterization, and gene localization to chromosome 14
    • Motwani, M., R. A. White, N. Guo, L. L. Dowler, A. I. Tauber, and K. N. Sastry. 1995. Mouse surfactant protein-D. cDNA cloning, characterization, and gene localization to chromosome 14. J. Immunol. 155:5671-5677.
    • (1995) J. Immunol. , vol.155 , pp. 5671-5677
    • Motwani, M.1    White, R.A.2    Guo, N.3    Dowler, L.L.4    Tauber, A.I.5    Sastry, K.N.6
  • 12
    • 0029240468 scopus 로고
    • Characterization of murine mannose-binding protein genes Mbl1 and Mbl2 reveals features common to other collectin genes
    • Sastry, R., J. S. Wang, D. C. Brown, R. A. Ezckowitz, A. I. Tauber, and K. N. Sastry. 1995. Characterization of murine mannose-binding protein genes Mbl1 and Mbl2 reveals features common to other collectin genes. Mamm. Genome 6:103-110.
    • (1995) Mamm. Genome , vol.6 , pp. 103-110
    • Sastry, R.1    Wang, J.S.2    Brown, D.C.3    Ezckowitz, R.A.4    Tauber, A.I.5    Sastry, K.N.6
  • 13
    • 0029973090 scopus 로고    scopus 로고
    • Localization and developmental expression of surfactant proteins A and D in the respiratory tract of the mouse
    • Wong, C. J., J. Akiyama, L. Allen, and S. Hawgood. 1996. Localization and developmental expression of surfactant proteins A and D in the respiratory tract of the mouse Pediatr. Res. 39:930-937.
    • (1996) Pediatr. Res. , vol.39 , pp. 930-937
    • Wong, C.J.1    Akiyama, J.2    Allen, L.3    Hawgood, S.4
  • 15
    • 0027466290 scopus 로고
    • Genomic organization of human surfactant protein D (SP-D): SP-D is encoded on chromosome 10q22.2-23.1
    • Crouch, E. C., K. Rust, R. Veile, H. Donis-Keller, and L. Grosso. 1993. Genomic organization of human surfactant protein D (SP-D): SP-D is encoded on chromosome 10q22.2-23.1. J. Biol. Chem. 268:2976-2983.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2976-2983
    • Crouch, E.C.1    Rust, K.2    Veile, R.3    Donis-Keller, H.4    Grosso, L.5
  • 16
    • 0028446014 scopus 로고
    • The mapping of transgenes by fluorescence in situ hybridization on G-banded mouse chromosomes
    • Shi, Y. P., T. T. Huang, E. J. Carlson, and C. J. Epstein. 1994. The mapping of transgenes by fluorescence in situ hybridization on G-banded mouse chromosomes. Mamm. Genome 5:337-341.
    • (1994) Mamm. Genome , vol.5 , pp. 337-341
    • Shi, Y.P.1    Huang, T.T.2    Carlson, E.J.3    Epstein, C.J.4
  • 19
    • 0028942724 scopus 로고
    • Rapid physical mapping of the human trk protooncogene (NTRK1) to human chromosome 1q21-q22 by P1 clone selection, fluorescence in situ hybridization (FISH), and computer-assisted microscopy
    • Weier, H. U., A. P. Rhein, F. Shadravan, C. Collins, and D. Polikoff. 1995. Rapid physical mapping of the human trk protooncogene (NTRK1) to human chromosome 1q21-q22 by P1 clone selection, fluorescence in situ hybridization (FISH), and computer-assisted microscopy. Genomics 26:390-393.
    • (1995) Genomics , vol.26 , pp. 390-393
    • Weier, H.U.1    Rhein, A.P.2    Shadravan, F.3    Collins, C.4    Polikoff, D.5
  • 20
    • 0030077032 scopus 로고    scopus 로고
    • Characterization of the human surfactant protein D promoter: Transcriptional regulation of SP-D gene expression by glucocorticoids
    • Rust, K., L. Bingle, W. Mariencheck, A. Persson, and E. C. Crouch. 1996. Characterization of the human surfactant protein D promoter: transcriptional regulation of SP-D gene expression by glucocorticoids. Am. J. Respir. Cell Mol. Biol. 14:121-130.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.14 , pp. 121-130
    • Rust, K.1    Bingle, L.2    Mariencheck, W.3    Persson, A.4    Crouch, E.C.5
  • 21
    • 0028277807 scopus 로고
    • Bovine conglutinin gene exon structure reveals its evolutionary relationship in surfactant protein-D
    • Liou, L. S., R. Sastry, K. L. Hartshorn, Y. M. Lee, T. B. Okarma, A. I. Tauber, and K. N. Sastry. 1994. Bovine conglutinin gene exon structure reveals its evolutionary relationship in surfactant protein-D. J. Immunol. 153:173-180.
    • (1994) J. Immunol. , vol.153 , pp. 173-180
    • Liou, L.S.1    Sastry, R.2    Hartshorn, K.L.3    Lee, Y.M.4    Okarma, T.B.5    Tauber, A.I.6    Sastry, K.N.7
  • 22
    • 0028169837 scopus 로고
    • Collectins - Soluble proteins containing collagenous regions and lectin domains - And their roles in innate immunity
    • Hoppe, H. J., and K. B. Reid. 1994. Collectins - soluble proteins containing collagenous regions and lectin domains - and their roles in innate immunity. Protein Sci. 3:1143-1158.
    • (1994) Protein Sci. , vol.3 , pp. 1143-1158
    • Hoppe, H.J.1    Reid, K.B.2
  • 23
    • 0023177034 scopus 로고
    • The 35 kd pulmonary surfactant-associated protein is encoded on chromosome 10
    • Bruns, G., H. Stroh, G. M. Veldman, S. A. Latt, and J. Floros. 1987. The 35 kd pulmonary surfactant-associated protein is encoded on chromosome 10. Hum. Genet. 76:58-62.
    • (1987) Hum. Genet. , vol.76 , pp. 58-62
    • Bruns, G.1    Stroh, H.2    Veldman, G.M.3    Latt, S.A.4    Floros, J.5
  • 24
    • 0027296942 scopus 로고
    • Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster
    • Kolble, K., J. Lu, S. E. Mole, S. Kaluz, and K. B. Reid. 1993. Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster. Genomics 17:294-298.
    • (1993) Genomics , vol.17 , pp. 294-298
    • Kolble, K.1    Lu, J.2    Mole, S.E.3    Kaluz, S.4    Reid, K.B.5
  • 25
    • 0024415548 scopus 로고
    • The human mannose-hinding protein gene: Exon structure reveals its evolutionary relationship to a human pulmonary surfactant gene and localization to chromosome 10
    • Sastry, K., G. A. Herman, L. Day, E. Deignan, G. Bruns, C. C. Morton, and R. A. Ezckowitz. 1989. The human mannose-hinding protein gene: exon structure reveals its evolutionary relationship to a human pulmonary surfactant gene and Localization to chromosome 10. J. Exp. Med. 170:1175-1189.
    • (1989) J. Exp. Med. , vol.170 , pp. 1175-1189
    • Sastry, K.1    Herman, G.A.2    Day, L.3    Deignan, E.4    Bruns, G.5    Morton, C.C.6    Ezckowitz, R.A.7
  • 26
    • 0028675629 scopus 로고
    • The murine mannose-binding protein genes (Mbl 1 and Mbl 2) localize to chromosomes 14 and 19
    • White, R. A., L. L. Dowler, L. R. Adkison, R. A. Ezekowitz, and K. N. Sastry. 1994. The murine mannose-binding protein genes (Mbl 1 and Mbl 2) localize to chromosomes 14 and 19. Mamm. Genome 5:807-809.
    • (1994) Mamm. Genome , vol.5 , pp. 807-809
    • White, R.A.1    Dowler, L.L.2    Adkison, L.R.3    Ezekowitz, R.A.4    Sastry, K.N.5
  • 27
    • 0029840182 scopus 로고    scopus 로고
    • Characteriztion of two mannose-bnding protein cDNAs from rhesus monkey (Macaca mulatta): Structure and evolutionary implications
    • Mogues, T., T. Ota, A. I. Taubr, and K. N. Sasty. 1996. Characteriztion of two mannose-bnding protein cDNAs from rhesus monkey (Macaca mulatta): structure and evolutionary implications. Glycobiology 6:543-550.
    • (1996) Glycobiology , vol.6 , pp. 543-550
    • Mogues, T.1    Ota, T.2    Taubr, A.I.3    Sasty, K.N.4
  • 29
    • 0028175514 scopus 로고
    • A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation
    • Hoppe, H. J., P. N. Barlow, and K. B. Reid. 1994. A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation. FEBS Lett. 344:191-195.
    • (1994) FEBS Lett. , vol.344 , pp. 191-195
    • Hoppe, H.J.1    Barlow, P.N.2    Reid, K.B.3
  • 30
    • 0030600144 scopus 로고    scopus 로고
    • Genomic simple repetitive dnas are targets for differential binding of nuclear proteins
    • Epplen, J. T., A. Kyas, and W. Maueler. 1996. Genomic simple repetitive DNAs are targets for differential binding of nuclear proteins. FEBS Lett. 389:92-95.
    • (1996) FEBS Lett. , vol.389 , pp. 92-95
    • Epplen, J.T.1    Kyas, A.2    Maueler, W.3
  • 31
    • 0023664021 scopus 로고
    • Exon structure of a mannose-binding protein gene reflects its evolutionary relationship to the asialoglycoprotein receptor and nonfibrillar collagens
    • Drickamer, K., and V. McCreary. 1987. Exon structure of a mannose-binding protein gene reflects its evolutionary relationship to the asialoglycoprotein receptor and nonfibrillar collagens. J. Biol. Chem. 262:2582-2589.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2582-2589
    • Drickamer, K.1    McCreary, V.2
  • 32
    • 0031913586 scopus 로고    scopus 로고
    • Conservation of surfactant protein A: Evidence for a single origin for vertebrate pulmonary surfactant
    • Sullivan, L. C., C. B. Daniels, I. D. Phillips, S. Orgeig, and J. A. Whitsett. 1998. Conservation of surfactant protein A: evidence for a single origin for vertebrate pulmonary surfactant. J. Mol. Evol. 46:131-138.
    • (1998) J. Mol. Evol. , vol.46 , pp. 131-138
    • Sullivan, L.C.1    Daniels, C.B.2    Phillips, I.D.3    Orgeig, S.4    Whitsett, J.A.5
  • 33
    • 0001473574 scopus 로고    scopus 로고
    • Ancient origin of the complement lectin pathway revealed by molecular cloning of mannan binding protein-associated serine protease from a urochordate, the Japanese ascidian, Halocynthia roretzi
    • Ji, X., K. Azumi, M. Sasaki, and M. Nonaka. 1997. Ancient origin of the complement lectin pathway revealed by molecular cloning of mannan binding protein-associated serine protease from a urochordate, the Japanese ascidian, Halocynthia roretzi. Proc. Natl. Acad. Sci. USA 94:6340-6345.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6340-6345
    • Ji, X.1    Azumi, K.2    Sasaki, M.3    Nonaka, M.4
  • 34
    • 0023645042 scopus 로고
    • Serum lectin with known structure activates complement through the classical pathway
    • Ikedo, K., T. Sannoh, N. Kawasaki, T. Kawasaki, and I. Yamashina. 1987. Serum lectin with known structure activates complement through the classical pathway. J. Biol. Chem. 262:7451-7454.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7451-7454
    • Ikedo, K.1    Sannoh, T.2    Kawasaki, N.3    Kawasaki, T.4    Yamashina, I.5
  • 35
    • 0028114821 scopus 로고
    • Elevated surfactant protein A in bronchoalveolar lavage fluids from sarcoidosis and hypersensitivity pneumonitis patients
    • Hamm, H., J. Luhrs, J. Guzman y Rotaeche, U. Costavel, H. Fabel, and W. Barsch. 1994. Elevated surfactant protein A in bronchoalveolar lavage fluids from sarcoidosis and hypersensitivity pneumonitis patients. Chest 106: 1766-1770.
    • (1994) Chest , vol.106 , pp. 1766-1770
    • Hamm, H.1    Luhrs, J.2    Guzman Y Rotaeche, J.3    Costavel, U.4    Fabel, H.5    Barsch, W.6
  • 36
    • 0030788625 scopus 로고    scopus 로고
    • Surfactant composition in infants and young children with cystic fibrosis
    • Hull, J., M. South, P. Phelan, and K. Grimwood. 1997. Surfactant composition in infants and young children with cystic fibrosis. Am. J. Respir. Crit. Care Med. 156:161-165.
    • (1997) Am. J. Respir. Crit. Care Med. , vol.156 , pp. 161-165
    • Hull, J.1    South, M.2    Phelan, P.3    Grimwood, K.4
  • 37
    • 0031132583 scopus 로고    scopus 로고
    • Surfactant protein A-deficient mice are susceptible to group B streptococcal infection
    • LeVine, A. M., M. D. Bruno, K. M. Huelsman, G. F. Ross, J. A. Whitsett, and T. R. Korfhagen. 1997. Surfactant protein A-deficient mice are susceptible to group B streptococcal infection. J. Immunol. 158:4336-4340.
    • (1997) J. Immunol. , vol.158 , pp. 4336-4340
    • LeVine, A.M.1    Bruno, M.D.2    Huelsman, K.M.3    Ross, G.F.4    Whitsett, J.A.5    Korfhagen, T.R.6
  • 38
    • 0024992486 scopus 로고
    • Clearance and recycling of pulmonary surfactant
    • Lung Cell. Mol. Physiol. 3
    • Wright, J. R. 1990. Clearance and recycling of pulmonary surfactant. Am. J. Physiol. 259(Lung Cell. Mol. Physiol. 3):L1-L12.
    • (1990) Am. J. Physiol. , vol.259
    • Wright, J.R.1


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