메뉴 건너뛰기




Volumn 195, Issue 4, 2015, Pages 1628-1636

Natural anti-infective pulmonary proteins: In vivo cooperative action of surfactant protein SP-A and the lung antimicrobial peptide SP-BN

Author keywords

[No Author keywords available]

Indexed keywords

SURFACTANT PROTEIN A; SURFACTANT PROTEIN B; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; CYTOKINE; PROTEIN BINDING; RECOMBINANT PROTEIN; SURFACTANT ASSOCIATED PROTEIN;

EID: 84938946420     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1500778     Document Type: Article
Times cited : (34)

References (30)
  • 1
    • 45949112254 scopus 로고    scopus 로고
    • Gram-negative antibiotic resistance: There is a price to pay
    • Slama, T. G. 2008. Gram-negative antibiotic resistance: there is a price to pay. Crit. Care 12(Suppl. 4): S4.
    • (2008) Crit. Care , vol.12 , pp. S4
    • Slama, T.G.1
  • 2
    • 77957740348 scopus 로고    scopus 로고
    • Hospital-acquired infections due to gram-negative bacteria
    • author reply 1483-1484
    • Argyres, M. I. 2010. Hospital-acquired infections due to gram-negative bacteria. N. Engl. J. Med. 363: 1483, author reply 1483-1484.
    • (2010) N. Engl. J. Med. , vol.363 , pp. 1483
    • Argyres, M.I.1
  • 3
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: Primeval molecules or future drugs?
    • Peters, B. M., M. E. Shirtliff, and M. A. Jabra-Rizk. 2010. Antimicrobial peptides: primeval molecules or future drugs? PLoS Pathog. 6: e1001067.
    • (2010) PLoS Pathog , vol.6 , pp. e1001067
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 4
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright, J. R. 2005. Immunoregulatory functions of surfactant proteins. Nat. Rev. Immunol. 5: 58-68.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 5
    • 76249088372 scopus 로고    scopus 로고
    • Surfactant protein B propeptide contains a saposin-like protein domain with antimicrobial activity at low pH
    • Yang, L., J. Johansson, R. Ridsdale, H. Willander, M. Fitzen, H. T. Akinbi, and T. E. Weaver. 2010. Surfactant protein B propeptide contains a saposin-like protein domain with antimicrobial activity at low pH. J. Immunol. 184: 975-983.
    • (2010) J. Immunol. , vol.184 , pp. 975-983
    • Yang, L.1    Johansson, J.2    Ridsdale, R.3    Willander, H.4    Fitzen, M.5    Akinbi, H.T.6    Weaver, T.E.7
  • 6
    • 21844449938 scopus 로고    scopus 로고
    • Surfactant protein A is a principal and oxidation-sensitive microbial permeabilizing factor in the alveolar lining fluid
    • Kuzmenko, A. I., H. Wu, S. Wan, and F. X. McCormack. 2005. Surfactant protein A is a principal and oxidation-sensitive microbial permeabilizing factor in the alveolar lining fluid. J. Biol. Chem. 280: 25913-25919.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25913-25919
    • Kuzmenko, A.I.1    Wu, H.2    Wan, S.3    McCormack, F.X.4
  • 7
    • 33748655463 scopus 로고    scopus 로고
    • Comparative signature-tagged mutagenesis identifies Pseudomonas factors conferring resistance to the pulmonary collectin SP-A
    • Zhang, S., Y. Chen, E. Potvin, F. Sanschagrin, R. C. Levesque, F. X. McCormack, and G. W. Lau. 2005. Comparative signature-tagged mutagenesis identifies Pseudomonas factors conferring resistance to the pulmonary collectin SP-A. PLoS Pathog. 1: 259-268.
    • (2005) PLoS Pathog. , vol.1 , pp. 259-268
    • Zhang, S.1    Chen, Y.2    Potvin, E.3    Sanschagrin, F.4    Levesque, R.C.5    McCormack, F.X.6    Lau, G.W.7
  • 8
    • 14844297019 scopus 로고    scopus 로고
    • Role of the degree of oligomerization in the structure and function of human surfactant protein A
    • Sánchez-Barbero, F., J. Strassner, R. Garc?a-Cañero, W. Steinhilber, and C. Casals. 2005. Role of the degree of oligomerization in the structure and function of human surfactant protein A. J. Biol. Chem. 280: 7659-7670.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7659-7670
    • Sánchez-Barbero, F.1    Strassner, J.2    Garća-Cañero, R.3    Steinhilber, W.4    Casals, C.5
  • 9
    • 77957844255 scopus 로고    scopus 로고
    • Fluidizing effects of C-reactive protein on lung surfactant membranes: Protective role of surfactant protein A
    • Sáenz, A., A. López-Sánchez, J. Mojica-Lázaro, L. Mart?nez-Caro, N. Nin, L. A. Bagatolli, and C. Casals. 2010. Fluidizing effects of C-reactive protein on lung surfactant membranes: protective role of surfactant protein A. FASEB J. 24: 3662-3673.
    • (2010) FASEB J. , vol.24 , pp. 3662-3673
    • Sáenz, A.1    López-Sánchez, A.2    Mojica-Lázaro, J.3    Martnez-Caro, L.4    Nin, N.5    Bagatolli, L.A.6    Casals, C.7
  • 10
    • 34548802927 scopus 로고    scopus 로고
    • Structural and functional differences among human surfactant proteins SP-A1, SP-A2 and co-expressed SP-A1/SP-A2: Role of supratrimeric oligomerization
    • Sánchez-Barbero, F., G. Rivas, W. Steinhilber, and C. Casals. 2007. Structural and functional differences among human surfactant proteins SP-A1, SP-A2 and co-expressed SP-A1/SP-A2: role of supratrimeric oligomerization. Biochem. J. 406: 479-489.
    • (2007) Biochem. J. , vol.406 , pp. 479-489
    • Sánchez-Barbero, F.1    Rivas, G.2    Steinhilber, W.3    Casals, C.4
  • 11
    • 58949097012 scopus 로고    scopus 로고
    • Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
    • Llobet, E., J. M. Tomás, and J. A. Bengoechea. 2008. Capsule polysaccharide is a bacterial decoy for antimicrobial peptides. Microbiology 154: 3877-3886.
    • (2008) Microbiology , vol.154 , pp. 3877-3886
    • Llobet, E.1    Tomás, J.M.2    Bengoechea, J.A.3
  • 13
    • 0027765632 scopus 로고
    • Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles
    • Casals, C., E. Miguel, and J. Perez-Gil. 1993. Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles. Biochem. J. 296: 585-593.
    • (1993) Biochem. J. , vol.296 , pp. 585-593
    • Casals, C.1    Miguel, E.2    Perez-Gil, J.3
  • 14
    • 0034669924 scopus 로고    scopus 로고
    • Bacterial killing is enhanced by expression of lysozyme in the lungs of transgenic mice
    • Akinbi, H. T., R. Epaud, H. Bhatt, and T. E. Weaver. 2000. Bacterial killing is enhanced by expression of lysozyme in the lungs of transgenic mice. J. Immunol. 165: 5760-5766.
    • (2000) J. Immunol. , vol.165 , pp. 5760-5766
    • Akinbi, H.T.1    Epaud, R.2    Bhatt, H.3    Weaver, T.E.4
  • 15
    • 0033516641 scopus 로고    scopus 로고
    • Surfactant protein B (SP-B)-/-mice are rescued by restoration of SP-B expression in alveolar type II cells but not Clara cells
    • Lin, S., C. L. Na, H. T. Akinbi, K. S. Apsley, J. A. Whitsett, and T. E. Weaver. 1999. Surfactant protein B (SP-B)-/-mice are rescued by restoration of SP-B expression in alveolar type II cells but not Clara cells. J. Biol. Chem. 274: 19168-19174.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19168-19174
    • Lin, S.1    Na, C.L.2    Akinbi, H.T.3    Apsley, K.S.4    Whitsett, J.A.5    Weaver, T.E.6
  • 16
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan, H., and R. E. Hancock. 2001. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother. 45: 1558-1560.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.2
  • 17
    • 0033725250 scopus 로고    scopus 로고
    • Synergistic and additive killing by antimicrobial factors found in human airway surface liquid
    • Singh, P. K., B. F. Tack, P. B. McCray, Jr., and M. J. Welsh. 2000. Synergistic and additive killing by antimicrobial factors found in human airway surface liquid. Am. J. Physiol. Lung Cell. Mol. Physiol. 279: L799-L805.
    • (2000) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.279 , pp. L799-L805
    • Singh, P.K.1    Tack, B.F.2    McCray, P.B.3    Welsh, M.J.4
  • 18
    • 84871300505 scopus 로고    scopus 로고
    • The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins
    • Tripathi, S., T. Tecle, A. Verma, E. Crouch, M. White, and K. L. Hartshorn. 2013. The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins. J. Gen. Virol. 94: 40-49.
    • (2013) J. Gen. Virol. , vol.94 , pp. 40-49
    • Tripathi, S.1    Tecle, T.2    Verma, A.3    Crouch, E.4    White, M.5    Hartshorn, K.L.6
  • 20
    • 55949101551 scopus 로고    scopus 로고
    • SP-A permeabilizes lipopolysaccharide membranes by forming protein aggregates that extract lipids from the membrane
    • Cañadas, O., I. Garc?a-Verdugo, K. M. Keough, and C. Casals. 2008. SP-A permeabilizes lipopolysaccharide membranes by forming protein aggregates that extract lipids from the membrane. Biophys. J. 95: 3287-3294.
    • (2008) Biophys. J. , vol.95 , pp. 3287-3294
    • Cañadas, O.1    Garća-Verdugo, I.2    Keough, K.M.3    Casals, C.4
  • 21
    • 67649274356 scopus 로고    scopus 로고
    • Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L
    • Mahalka, A. K., and P. K. Kinnunen. 2009. Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L. Biochim. Biophys. Acta 1788: 1600-1609.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1600-1609
    • Mahalka, A.K.1    Kinnunen, P.K.2
  • 22
    • 79959651424 scopus 로고    scopus 로고
    • Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link
    • Jang, H., F. T. Arce, M. Mustata, S. Ramachandran, R. Capone, R. Nussinov, and R. Lal. 2011. Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link. Biophys. J. 100: 1775-1783.
    • (2011) Biophys. J. , vol.100 , pp. 1775-1783
    • Jang, H.1    Arce, F.T.2    Mustata, M.3    Ramachandran, S.4    Capone, R.5    Nussinov, R.6    Lal, R.7
  • 26
    • 84871147196 scopus 로고    scopus 로고
    • Intrapulmonary G-CSF rescues neutrophil recruitment to the lung and neutrophil release to blood in Gram-negative bacterial infection in MCP-1-/-mice
    • Balamayooran, G., S. Batra, B. Theivanthiran, S. Cai, P. Pacher, and S. Jeyaseelan. 2012. Intrapulmonary G-CSF rescues neutrophil recruitment to the lung and neutrophil release to blood in Gram-negative bacterial infection in MCP-1-/-mice. J. Immunol. 189: 5849-5859.
    • (2012) J. Immunol. , vol.189 , pp. 5849-5859
    • Balamayooran, G.1    Batra, S.2    Theivanthiran, B.3    Cai, S.4    Pacher, P.5    Jeyaseelan, S.6
  • 27
    • 84875442814 scopus 로고    scopus 로고
    • Neutrophil recruitment and function in health and inflammation
    • Kolaczkowska, E., and P. Kubes. 2013. Neutrophil recruitment and function in health and inflammation. Nat. Rev. Immunol. 13: 159-175.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 159-175
    • Kolaczkowska, E.1    Kubes, P.2
  • 28
    • 58349090235 scopus 로고    scopus 로고
    • The human antimicrobial peptide dermcidin activates normal human keratinocytes
    • Niyonsaba, F., A. Suzuki, H. Ushio, I. Nagaoka, H. Ogawa, and K. Okumura. 2009. The human antimicrobial peptide dermcidin activates normal human keratinocytes. Br. J. Dermatol. 160: 243-249.
    • (2009) Br. J. Dermatol. , vol.160 , pp. 243-249
    • Niyonsaba, F.1    Suzuki, A.2    Ushio, H.3    Nagaoka, I.4    Ogawa, H.5    Okumura, K.6
  • 29
    • 84922565465 scopus 로고    scopus 로고
    • Host defense peptides: Front-line immunomodulators
    • Mansour, S. C., O. M. Pena, and R. E. Hancock. 2014. Host defense peptides: front-line immunomodulators. Trends Immunol. 35: 443-450.
    • (2014) Trends Immunol. , vol.35 , pp. 443-450
    • Mansour, S.C.1    Pena, O.M.2    Hancock, R.E.3
  • 30
    • 0141791335 scopus 로고    scopus 로고
    • Surfactant protein A enhances apoptotic cell uptake and TGF-beta1 release by inflammatory alveolar macrophages
    • Reidy, M. F., and J. R. Wright. 2003. Surfactant protein A enhances apoptotic cell uptake and TGF-beta1 release by inflammatory alveolar macrophages. Am. J. Physiol. Lung Cell. Mol. Physiol. 285: L854-L861.
    • (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.285 , pp. L854-L861
    • Reidy, M.F.1    Wright, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.