메뉴 건너뛰기




Volumn 46, Issue 15, 2009, Pages 3060-3069

Multimeric and trimeric subunit SP-D are interconvertible structures with distinct ligand interaction

Author keywords

HDL; LDL; Lipopolysaccharide; Lipoteichoic acid; Mannan; Multimers; N acetyl mannoseamine; oxLDL; Peptidoglycan; Surfactant protein D; Trimers

Indexed keywords

SURFACTANT PROTEIN D;

EID: 68749113721     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.06.005     Document Type: Article
Times cited : (30)

References (28)
  • 1
    • 0033045721 scopus 로고    scopus 로고
    • Mannan-binding lectin deficiency is associated with unexplained recurrent miscarriage
    • Christiansen O.B., Kilpatrick D.C., Souter V., et al. Mannan-binding lectin deficiency is associated with unexplained recurrent miscarriage. Scand. J. Immunol. 49 (1999) 193-196
    • (1999) Scand. J. Immunol. , vol.49 , pp. 193-196
    • Christiansen, O.B.1    Kilpatrick, D.C.2    Souter, V.3
  • 2
    • 0036749283 scopus 로고    scopus 로고
    • Structural requirements for SP-D function in vitro and in vivo: therapeutic potential of recombinant SP-D
    • Clark H., and Reid K.B. Structural requirements for SP-D function in vitro and in vivo: therapeutic potential of recombinant SP-D. Immunobiology 205 (2002) 619-631
    • (2002) Immunobiology , vol.205 , pp. 619-631
    • Clark, H.1    Reid, K.B.2
  • 3
    • 0027523921 scopus 로고
    • Accumulation of surfactant protein D in human pulmonary alveolar proteinosis
    • Crouch E., Persson A., and Chang D. Accumulation of surfactant protein D in human pulmonary alveolar proteinosis. Am. J. Pathol. 142 (1993) 241-248
    • (1993) Am. J. Pathol. , vol.142 , pp. 241-248
    • Crouch, E.1    Persson, A.2    Chang, D.3
  • 4
    • 0028233879 scopus 로고
    • Molecular structure of pulmonary surfactant protein D (SP-D)
    • Crouch E., Persson A., Chang D., and Heuser J. Molecular structure of pulmonary surfactant protein D (SP-D). J. Biol. Chem. 269 (1994) 17311-17319
    • (1994) J. Biol. Chem. , vol.269 , pp. 17311-17319
    • Crouch, E.1    Persson, A.2    Chang, D.3    Heuser, J.4
  • 5
    • 33745628379 scopus 로고    scopus 로고
    • Species differences in the carbohydrate binding preferences of surfactant protein D
    • Crouch E.C., Smith K., McDonald B., et al. Species differences in the carbohydrate binding preferences of surfactant protein D. Am. J. Respir. Cell. Mol. Biol. 35 (2006) 84-94
    • (2006) Am. J. Respir. Cell. Mol. Biol. , vol.35 , pp. 84-94
    • Crouch, E.C.1    Smith, K.2    McDonald, B.3
  • 6
    • 0033790682 scopus 로고    scopus 로고
    • Surfactant protein genetic marker alleles identify a subgroup of tuberculosis in a Mexican population
    • Floros J., Lin H.M., Garcia A., et al. Surfactant protein genetic marker alleles identify a subgroup of tuberculosis in a Mexican population. J. Infect. Dis. 182 (2000) 1473-1478
    • (2000) J. Infect. Dis. , vol.182 , pp. 1473-1478
    • Floros, J.1    Lin, H.M.2    Garcia, A.3
  • 7
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai S.J., Xiao Y.Q., Dickinson M., et al. By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115 (2003) 13-23
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3
  • 8
    • 56849117935 scopus 로고    scopus 로고
    • S-Nitrosylation of surfactant protein-d controls inflammatory function
    • Guo C.J., Atochina-Vasserman E.N., Abramova E., et al. S-Nitrosylation of surfactant protein-d controls inflammatory function. PLoS Biol. 6 (2008) e266
    • (2008) PLoS Biol. , vol.6
    • Guo, C.J.1    Atochina-Vasserman, E.N.2    Abramova, E.3
  • 9
    • 0029903353 scopus 로고    scopus 로고
    • Interactions of recombinant human pulmonary surfactant protein D and SP- D multimers with influenza A
    • Hartshorn K., Chang D., Rust K., et al. Interactions of recombinant human pulmonary surfactant protein D and SP- D multimers with influenza A. Am. J. Physiol. 271 (1996) L753-L762
    • (1996) Am. J. Physiol. , vol.271
    • Hartshorn, K.1    Chang, D.2    Rust, K.3
  • 10
    • 36148955605 scopus 로고    scopus 로고
    • Reduced influenza viral neutralizing activity of natural human trimers of surfactant protein D
    • Hartshorn K.L., White M.R., Tecle T., et al. Reduced influenza viral neutralizing activity of natural human trimers of surfactant protein D. Respir. Res. 5 (2007) 8-9
    • (2007) Respir. Res. , vol.5 , pp. 8-9
    • Hartshorn, K.L.1    White, M.R.2    Tecle, T.3
  • 11
    • 0031852357 scopus 로고    scopus 로고
    • Human lung surfactant protein A exists in several different oligomeric states: oligomer size distribution varies between patient groups
    • Hickling T.P., Malhotra R., and Sim R.B. Human lung surfactant protein A exists in several different oligomeric states: oligomer size distribution varies between patient groups. Mol. Med. 4 (1998) 266-275
    • (1998) Mol. Med. , vol.4 , pp. 266-275
    • Hickling, T.P.1    Malhotra, R.2    Sim, R.B.3
  • 12
    • 39849096350 scopus 로고    scopus 로고
    • Truncated recombinant human SP-D attenuates emphysema and type II cell changes in SP-D deficient mice
    • Knudsen L., Ochs M., Mackay R., et al. Truncated recombinant human SP-D attenuates emphysema and type II cell changes in SP-D deficient mice. Respir. Res. 8 (2007) 70
    • (2007) Respir. Res. , vol.8 , pp. 70
    • Knudsen, L.1    Ochs, M.2    Mackay, R.3
  • 13
    • 0036113682 scopus 로고    scopus 로고
    • Surfactant protein D gene polymorphism associated with severe respiratory syncytial virus infection
    • Lahti M., Lofgren J., Marttila R., et al. Surfactant protein D gene polymorphism associated with severe respiratory syncytial virus infection. Pediatr. Res. 51 (2002) 696-699
    • (2002) Pediatr. Res. , vol.51 , pp. 696-699
    • Lahti, M.1    Lofgren, J.2    Marttila, R.3
  • 14
    • 19944430458 scopus 로고    scopus 로고
    • A common polymorphism in the SFTPD gene influences assembly, function, and concentration of surfactant protein D
    • Leth-Larsen R., Garred P., Jensenius H., et al. A common polymorphism in the SFTPD gene influences assembly, function, and concentration of surfactant protein D. J. Immunol. 174 (2005) 1532-1538
    • (2005) J. Immunol. , vol.174 , pp. 1532-1538
    • Leth-Larsen, R.1    Garred, P.2    Jensenius, H.3
  • 15
    • 0033231023 scopus 로고    scopus 로고
    • Structural characterization of human and bovine lung surfactant protein D
    • Leth-Larsen R., Holmskov U., and Hojrup P. Structural characterization of human and bovine lung surfactant protein D. Biochem. J. 343 Pt 3 (1999) 645-652
    • (1999) Biochem. J. , vol.343 PART 3 , pp. 645-652
    • Leth-Larsen, R.1    Holmskov, U.2    Hojrup, P.3
  • 16
    • 0037675777 scopus 로고    scopus 로고
    • Surfactant protein D (SP-D) serum levels in patients with community-acquired pneumonia
    • Leth-Larsen R., Nordenbaek C., Tornoe I., et al. Surfactant protein D (SP-D) serum levels in patients with community-acquired pneumonia. Clin. Immunol. 108 (2003) 29-37
    • (2003) Clin. Immunol. , vol.108 , pp. 29-37
    • Leth-Larsen, R.1    Nordenbaek, C.2    Tornoe, I.3
  • 17
    • 0031789747 scopus 로고    scopus 로고
    • A 50-kDa variant form of human surfactant protein D
    • Mason R.J., Nielsen L.D., Kuroki Y., et al. A 50-kDa variant form of human surfactant protein D. Eur. Respir. J. 12 (1998) 1147-1155
    • (1998) Eur. Respir. J. , vol.12 , pp. 1147-1155
    • Mason, R.J.1    Nielsen, L.D.2    Kuroki, Y.3
  • 18
    • 68749102352 scopus 로고    scopus 로고
    • Modification of surfactant protein D by reactive oxygen-nitrogen intermediates is accompanied by loss of aggregating activity, in vitro and in vivo
    • Matalon S., Shrestha K., Kirk M., et al. Modification of surfactant protein D by reactive oxygen-nitrogen intermediates is accompanied by loss of aggregating activity, in vitro and in vivo. FASEB J. 23 (2009) 1415-1430
    • (2009) FASEB J. , vol.23 , pp. 1415-1430
    • Matalon, S.1    Shrestha, K.2    Kirk, M.3
  • 19
    • 33750685946 scopus 로고    scopus 로고
    • Surfactant protein D of the innate immune defence is inversely associated with human obesity and SP-D deficiency infers increased body weight in mice
    • Sorensen G.L., Hjelmborg J.V., Leth-Larsen R., et al. Surfactant protein D of the innate immune defence is inversely associated with human obesity and SP-D deficiency infers increased body weight in mice. Scand. J. Immunol. 64 (2006) 633-638
    • (2006) Scand. J. Immunol. , vol.64 , pp. 633-638
    • Sorensen, G.L.1    Hjelmborg, J.V.2    Leth-Larsen, R.3
  • 20
    • 34249671245 scopus 로고    scopus 로고
    • Surfactant protein A and surfactant protein D variation in pulmonary disease
    • Sorensen G.L., Husby S., and Holmskov U. Surfactant protein A and surfactant protein D variation in pulmonary disease. Immunobiology 212 (2007) 381-416
    • (2007) Immunobiology , vol.212 , pp. 381-416
    • Sorensen, G.L.1    Husby, S.2    Holmskov, U.3
  • 22
    • 0031732489 scopus 로고    scopus 로고
    • A novel method of purifying lung surfactant proteins A and D from the lung lavage of alveolar proteinosis patients and from pooled amniotic fluid
    • Strong P., Kishore U., Morgan C., et al. A novel method of purifying lung surfactant proteins A and D from the lung lavage of alveolar proteinosis patients and from pooled amniotic fluid. J. Immunol. Methods 220 (1998) 139-149
    • (1998) J. Immunol. Methods , vol.220 , pp. 139-149
    • Strong, P.1    Kishore, U.2    Morgan, C.3
  • 23
    • 0141924849 scopus 로고    scopus 로고
    • Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin
    • Waki H., Yamauchi T., Kamon J., et al. Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin. J. Biol. Chem. 278 (2003) 40352-40363
    • (2003) J. Biol. Chem. , vol.278 , pp. 40352-40363
    • Waki, H.1    Yamauchi, T.2    Kamon, J.3
  • 24
    • 0032736419 scopus 로고    scopus 로고
    • Molecular defects in variant forms of mannose-binding protein associated with immunodeficiency
    • Wallis R., and Cheng J.Y. Molecular defects in variant forms of mannose-binding protein associated with immunodeficiency. J. Immunol. 163 (1999) 4953-4959
    • (1999) J. Immunol. , vol.163 , pp. 4953-4959
    • Wallis, R.1    Cheng, J.Y.2
  • 25
    • 0034705208 scopus 로고    scopus 로고
    • Increased metalloproteinase activity, oxidant production, and emphysema in surfactant protein D gene-inactivated mice
    • Wert S.E., Yoshida M., LeVine A.M., et al. Increased metalloproteinase activity, oxidant production, and emphysema in surfactant protein D gene-inactivated mice. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 5972-5977
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5972-5977
    • Wert, S.E.1    Yoshida, M.2    LeVine, A.M.3
  • 26
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright J.R. Immunoregulatory functions of surfactant proteins. Nat. Rev. Immunol. 5 (2005) 58-68
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 27
    • 0033828950 scopus 로고    scopus 로고
    • Reduction of von Willebrand factor by endothelial cells
    • Xie L., Chesterman C.N., and Hogg P.J. Reduction of von Willebrand factor by endothelial cells. Thromb. Haemost. 84 (2000) 506-513
    • (2000) Thromb. Haemost. , vol.84 , pp. 506-513
    • Xie, L.1    Chesterman, C.N.2    Hogg, P.J.3
  • 28
    • 0035374390 scopus 로고    scopus 로고
    • Activity of pulmonary surfactant protein-D (SP-D) in vivo is dependent on oligomeric structure
    • Zhang L., Ikegami M., Crouch E.C., et al. Activity of pulmonary surfactant protein-D (SP-D) in vivo is dependent on oligomeric structure. J. Biol. Chem. 276 (2001) 19214-19219
    • (2001) J. Biol. Chem. , vol.276 , pp. 19214-19219
    • Zhang, L.1    Ikegami, M.2    Crouch, E.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.