메뉴 건너뛰기




Volumn 20, Issue 5, 1999, Pages 953-963

Genomic organization of the mouse gene for lung surfactant protein D

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIBIA; AVES; BOVINAE; MAMMALIA; RODENTIA;

EID: 0033126694     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.20.5.3343     Document Type: Article
Times cited : (18)

References (48)
  • 1
    • 0028049687 scopus 로고
    • Molecular and cellular processing of lung surfactant
    • Rooney, S. A., S. L. Young, and C. R. Mendelson. 1994. Molecular and cellular processing of lung surfactant. FASEB J. 8:957-967.
    • (1994) FASEB J. , vol.8 , pp. 957-967
    • Rooney, S.A.1    Young, S.L.2    Mendelson, C.R.3
  • 2
    • 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
  • 3
    • 0027976024 scopus 로고
    • Collectins: Collagenous C-type lectins of the innate immune defense system
    • Holmskov, U., R. Malhotra, R. B. Sim, and J. C. Jensenius. 1994. Collectins: collagenous C-type lectins of the innate immune defense system. Immunol. Today 15:67-74.
    • (1994) Immunol. Today , vol.15 , pp. 67-74
    • Holmskov, U.1    Malhotra, R.2    Sim, R.B.3    Jensenius, J.C.4
  • 4
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R., and C. A. Janeway, Jr. 1997. Innate immunity: the virtues of a nonclonal system of recognition. Cell 91:295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 7
    • 0030925434 scopus 로고    scopus 로고
    • Isolation and characterization of a new member of the scavenger receptor superfamily. Glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule
    • Holmskov, U., P. Lawson, B. Teisner, I. Tornoe, A. C. Willis, C. Morgan, C. Koch, and K. B. Reid. 1997. Isolation and characterization of a new member of the scavenger receptor superfamily. glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule. J. Biol. Chem. 272:13743-13749.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13743-13749
    • Holmskov, U.1    Lawson, P.2    Teisner, B.3    Tornoe, I.4    Willis, A.C.5    Morgan, C.6    Koch, C.7    Reid, K.B.8
  • 8
    • 0029086053 scopus 로고
    • Opsonic activities of surfactant proteins A and D in phagocytosis of gram-negative bacteria by alveolar macrophages
    • Pikaar, J. C., W. F. Voorhout, L. M. van Golde, J. Verhoef, J. A. Van Strijp, and J. F. van Iwaarden. 1995. Opsonic activities of surfactant proteins A and D in phagocytosis of gram-negative bacteria by alveolar macrophages. J. Infect. Dis. 172:481-489.
    • (1995) J. Infect. Dis. , vol.172 , pp. 481-489
    • Pikaar, J.C.1    Voorhout, W.F.2    Van Golde, L.M.3    Verhoef, J.4    Van Strijp, J.A.5    Van Iwaarden, J.F.6
  • 9
    • 0026646154 scopus 로고
    • Immunocytochemical localization of surfactant protein D (SP-D) in type II cells, Clara cells, and alveolar macrophages of rat lung
    • Voorhout, W. F., T. Veenendaal, Y. Kuroki, Y. Ogasawara, L. M. van Golde, and H. J. Geuze. 1992. Immunocytochemical localization of surfactant protein D (SP-D) in type II cells, Clara cells, and alveolar macrophages of rat lung. J. Histochem. Cytochem. 40:1589-1597.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1589-1597
    • Voorhout, W.F.1    Veenendaal, T.2    Kuroki, Y.3    Ogasawara, Y.4    Van Golde, L.M.5    Geuze, H.J.6
  • 10
    • 0026659644 scopus 로고
    • Surfactant protein D; subcellular localization in nonciliated bronchiolar epithelial cells
    • Crouch, E., D. Parghi, S. F. Kuan, and A. Persson. 1992. Surfactant protein D; subcellular localization in nonciliated bronchiolar epithelial cells. Am. J. Physiol. 263:L60-L66.
    • (1992) Am. J. Physiol. , vol.263
    • Crouch, E.1    Parghi, D.2    Kuan, S.F.3    Persson, A.4
  • 11
    • 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
  • 13
    • 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
  • 14
    • 0028415231 scopus 로고
    • Modulation of surfactant protein D expression by glucocorticoids in fetal rat lung
    • Mariencheck, W., and E. Crouch. 1994. Modulation of surfactant protein D expression by glucocorticoids in fetal rat lung. Am. J. Respir. Cell Mol. Biol. 10;419-429.
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.10 , pp. 419-429
    • Mariencheck, W.1    Crouch, E.2
  • 15
    • 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
  • 16
    • 0024415548 scopus 로고
    • The human mannose-binding 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-binding 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
  • 17
    • 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
  • 18
    • 0029240468 scopus 로고
    • Characterization of murine mannose-binding protein genes Mb11 and Mb12 reveals features common to other collectin genes
    • Sastry, R., J. S. Wang, D. C. Brown, R. A. Ezckowitz, A. T. Tauber, and K. N. Sastry. 1995. Characterization of murine mannose-binding protein genes Mb11 and Mb12 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.T.5    Sastry, K.N.6
  • 21
    • 0027466290 scopus 로고
    • Genomic organization of human surfactant protein D (SP-D): SP-D is encoded on chromosome 10q22.2-23.1
    • Crouch, F., 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, F.1    Rust, K.2    Veile, R.3    Donis Keller, H.4    Grosso, L.5
  • 22
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 23
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman, M. A., M. K. Dush, and G. R. Martin. 1988. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85:8998-9002.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 25
    • 0027174559 scopus 로고
    • Identification of a new, abundant superfamily of mammalian LTR-transposons
    • Smit, A. F. 1993. Identification of a new, abundant superfamily of mammalian LTR-transposons. Nucleic Acids Res. 21:1863-1872.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1863-1872
    • Smit, A.F.1
  • 26
    • 0028364621 scopus 로고
    • Gene organization and 5′-flanking region sequence of conglutinin: A C-type mammalian lectin containing a collagen-like domain
    • Kawasaki, N., N. Itoh, and T. Kawasaki. 1994. Gene organization and 5′-flanking region sequence of conglutinin: a C-type mammalian lectin containing a collagen-like domain. Biochem. Biophys. Res. Commun. 198: 597-604.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 597-604
    • Kawasaki, N.1    Itoh, N.2    Kawasaki, T.3
  • 27
    • 0019363396 scopus 로고
    • Organization and expression of eucaryote split genes coding for proteins
    • Breathnach, R., and P. Chambon. 1981. Organization and expression of eucaryote split genes coding for proteins. Annu. Rev. Biochem. 50:344-383.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 344-383
    • Breathnach, R.1    Chambon, P.2
  • 28
    • 0028080881 scopus 로고
    • A homeodomain protein related to caudal regulates intestine-specific gene transcription
    • Suh, E., L. Chen, J. Taylor, and P. G. Traber. 1994. A homeodomain protein related to caudal regulates intestine-specific gene transcription. Mol. Cell Biol. 14:7340-7351.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7340-7351
    • Suh, E.1    Chen, L.2    Taylor, J.3    Traber, P.G.4
  • 29
    • 0028353904 scopus 로고
    • The DNA-binding specificity of the hepatocyte nuclear factor 3/forkhead domain is influenced by amino-acid residues adjacent to the recognition helix
    • Overdier, D. G., A. Porcella, and R. H. Costa. 1994. The DNA-binding specificity of the hepatocyte nuclear factor 3/forkhead domain is influenced by amino-acid residues adjacent to the recognition helix. Mol. Cell. Biol. 14:2755-2766.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2755-2766
    • Overdier, D.G.1    Porcella, A.2    Costa, R.H.3
  • 30
    • 0028024585 scopus 로고
    • The lung-specific surfactant protein B gene promoter is a target for thyroid transcription factor I and hepatocyte nuclear factor 3, indicating common factors for organ-specific gene expression along the foregut axis
    • Bohinski, R. J., R. Di Lauro, and J. A. Whitsett. 1994. The lung-specific surfactant protein B gene promoter is a target for thyroid transcription factor I and hepatocyte nuclear factor 3, indicating common factors for organ-specific gene expression along the foregut axis. Mol Cell. Biol. 14:5671-5681.
    • (1994) Mol Cell. Biol. , vol.14 , pp. 5671-5681
    • Bohinski, R.J.1    Di Lauro, R.2    Whitsett, J.A.3
  • 31
    • 0028844735 scopus 로고
    • Upstream enhancer activity in the human surfactant protein B gene is mediated by thyroid transcription factor I
    • Yan, C., Z. Sever, and J. A. Whitsett. 1995. Upstream enhancer activity in the human surfactant protein B gene is mediated by thyroid transcription factor I. J. Biol. Chem. 270:24852-24857.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24852-24857
    • Yan, C.1    Sever, Z.2    Whitsett, J.A.3
  • 32
    • 0029785710 scopus 로고    scopus 로고
    • Biosynthesis of surfactant protein D. Contributions of conserved NH2-terminal cysteine residues and collagen helix formation to assembly and secretion
    • Brown Augsburger, P., D. Chang, K. Rust, and E. C. Crouch. 1996. Biosynthesis of surfactant protein D. Contributions of conserved NH2-terminal cysteine residues and collagen helix formation to assembly and secretion. J. Biol. Chem. 271:18912-18919.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18912-18919
    • Brown Augsburger, P.1    Chang, D.2    Rust, K.3    Crouch, E.C.4
  • 33
    • 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
  • 34
    • 0025016078 scopus 로고
    • Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families
    • Exposito, J. Y., and R. Garrone. 1990. Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families. Proc. Natl. Acad. Sci. USA 87:6669-6673.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6669-6673
    • Exposito, J.Y.1    Garrone, R.2
  • 35
    • 0030587494 scopus 로고    scopus 로고
    • Cloning and characterization of the human lectin P35 gene and its related gene
    • Endo, Y., Y. Sato, M. Matsushita, and T. Fujita. 1996. Cloning and characterization of the human lectin P35 gene and its related gene. Genotics 36:515-521.
    • (1996) Genotics , vol.36 , pp. 515-521
    • Endo, Y.1    Sato, Y.2    Matsushita, M.3    Fujita, T.4
  • 36
    • 0025719055 scopus 로고
    • Short chain collagens in sponges are encoded by a family of closely related genes
    • Exposito, J. Y., D. Le Guellec, Q. Lu, and R. Garronc. 1991. Short chain collagens in sponges are encoded by a family of closely related genes. J. Biol. Chem. 266:21923-21928.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21923-21928
    • Exposito, J.Y.1    Le Guellec, D.2    Lu, Q.3    Garronc, R.4
  • 37
    • 0023646322 scopus 로고
    • Intron-dependent evolution: Preferred types of exons and introns
    • Patthy, L. 1987. Intron-dependent evolution: preferred types of exons and introns. FEBS Lett. 214:1-7.
    • (1987) FEBS Lett. , vol.214 , pp. 1-7
    • Patthy, L.1
  • 38
    • 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
  • 39
    • 0031081111 scopus 로고    scopus 로고
    • Simple sequence repeats as a source of quantitative genetic variation
    • Kashi, Y., D. King, and M. Soller. 1997. Simple sequence repeats as a source of quantitative genetic variation. Trends Genet. 13:74-78.
    • (1997) Trends Genet. , vol.13 , pp. 74-78
    • Kashi, Y.1    King, D.2    Soller, M.3
  • 40
    • 0025744589 scopus 로고
    • Spontaneous mutation at the hypervariable mouse minisatellite locus Ms6-hm: Flanking DNA sequence and analysis of germline and early somatic mutation events
    • Kelly, R., M. Gibbs, A. Collick, and A. J. Jeffreys. 1991. Spontaneous mutation at the hypervariable mouse minisatellite locus Ms6-hm: flanking DNA sequence and analysis of germline and early somatic mutation events, Proc. R. Soc. Lond. B. Biol. Sci. 245:235-245.
    • (1991) Proc. R. Soc. Lond. B. Biol. Sci. , vol.245 , pp. 235-245
    • Kelly, R.1    Gibbs, M.2    Collick, A.3    Jeffreys, A.J.4
  • 41
    • 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
  • 42
    • 0026508808 scopus 로고
    • Compilation of vertebrate-encoded transcription factors
    • Faisst, S., and S. Meyer. 1992. Compilation of vertebrate-encoded transcription factors. Nucleic Acids Res. 20:3-26.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3-26
    • Faisst, S.1    Meyer, S.2
  • 43
    • 0030070192 scopus 로고    scopus 로고
    • Differential activation of lung-specific genes by two forkhead proteins, FREAC-1 and FREAC-2
    • Hellqvist, M., M. Mahlapuu, L. Samuelsson, S. Enerback, and P. Carlsson. 1996. Differential activation of lung-specific genes by two forkhead proteins, FREAC-1 and FREAC-2. J. Biol. Chem. 271:4482-4490.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4482-4490
    • Hellqvist, M.1    Mahlapuu, M.2    Samuelsson, L.3    Enerback, S.4    Carlsson, P.5
  • 44
    • 0028934922 scopus 로고
    • Lung cell-specific expression of the murine surfactant protein A (SP-A) gene is mediated by interactions between the SP-A promoter and thyroid transcription factor-1
    • published erratum appears in J. Biol. Chem. 270(27): 16482
    • Bruno, M. D., R. J. Bohinski, K. M. Huclsman, J. A. Whitsett, and T. R. Korfhagen. 1995.Lung cell-specific expression of the murine surfactant protein A (SP-A) gene is mediated by interactions between the SP-A promoter and thyroid transcription factor-1. J. Biol. Chem. 270:6531-6536 [published erratum appears in J. Biol. Chem. 270(27): 16482].
    • (1995) J. Biol. Chem. , vol.270 , pp. 6531-6536
    • Bruno, M.D.1    Bohinski, R.J.2    Huclsman, K.M.3    Whitsett, J.A.4    Korfhagen, T.R.5
  • 45
    • 0029962808 scopus 로고    scopus 로고
    • Transcription of the lung-specific surfactant protein C gene is mediated by thyroid transcription factor 1
    • Kelly, S. E., C. J. Bachurski, M. S. Burhans, and S. W. Glasser. 1996. Transcription of the lung-specific surfactant protein C gene is mediated by thyroid transcription factor 1. J. Biol. Chem. 271:6881-6888.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6881-6888
    • Kelly, S.E.1    Bachurski, C.J.2    Burhans, M.S.3    Glasser, S.W.4
  • 46
    • 0029999397 scopus 로고    scopus 로고
    • The lung enriched transcription factor TTF-1 and the ubiquitously expressed proteins Sp1 and Sp3 interact with elements located in the minimal promoter of the rat Clara cell secretory protein gene
    • Toonen, R. F., S. Gowan, and C. D. Bingle. 1996. The lung enriched transcription factor TTF-1 and the ubiquitously expressed proteins Sp1 and Sp3 interact with elements located in the minimal promoter of the rat Clara cell secretory protein gene. Biochem. J. 316:467-473.
    • (1996) Biochem. J. , vol.316 , pp. 467-473
    • Toonen, R.F.1    Gowan, S.2    Bingle, C.D.3
  • 47
    • 0027166263 scopus 로고
    • Identification of enhancers in the 5′-flanking region of the rabbit surfactant protein A (SP-A) gene and characterization of their binding proteins
    • Gao, E., J. L. Alcorn, and C. R. Mendelson. 1993. Identification of enhancers in the 5′-flanking region of the rabbit surfactant protein A (SP-A) gene and characterization of their binding proteins. J. Biol. Chem. 268:19697-19709.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19697-19709
    • Gao, E.1    Alcorn, J.L.2    Mendelson, C.R.3
  • 48
    • 0030267045 scopus 로고    scopus 로고
    • Surfactant proteins A and D increase in response to intratracheal lipopolysaccharide
    • McIntosh, J. C., A. H. Swyers, J. H. Fisher, and J. R. Wright. 1996. Surfactant proteins A and D increase in response to intratracheal lipopolysaccharide. Am. J. Respir. Cell Mol. Biol. 15:509-519.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , pp. 509-519
    • McIntosh, J.C.1    Swyers, A.H.2    Fisher, J.H.3    Wright, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.