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Volumn 1768, Issue 5, 2007, Pages 1059-1069

Identification of a segment in the precursor of pulmonary surfactant protein SP-B, potentially involved in pH-dependent membrane assembly of the protein

Author keywords

Interfacial hydrophobicity; Lipid protein interactions; Lung surfactant; Secretory pathway; SP B; Synthetic peptides

Indexed keywords

BPH PEPTIDE; BPH W PEPTIDE; LUNG SURFACTANT; PROTEIN PRECURSOR; SURFACTANT PROTEIN B; SYNTHETIC PEPTIDE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 34047245418     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.01.010     Document Type: Article
Times cited : (11)

References (52)
  • 1
    • 3042526283 scopus 로고    scopus 로고
    • Surfactant protein B: structure and function
    • Hawgood S. Surfactant protein B: structure and function. Biol. Neonate 85 (2004) 285-289
    • (2004) Biol. Neonate , vol.85 , pp. 285-289
    • Hawgood, S.1
  • 3
    • 0034781002 scopus 로고    scopus 로고
    • Lipid-protein interactions of hydrophobic proteins SP-B and SP-C in lung surfactant assembly and dynamics
    • Perez-Gil J. Lipid-protein interactions of hydrophobic proteins SP-B and SP-C in lung surfactant assembly and dynamics. Pediatr. Pathol. Mol. Med. 20 (2001) 445-469
    • (2001) Pediatr. Pathol. Mol. Med. , vol.20 , pp. 445-469
    • Perez-Gil, J.1
  • 4
    • 33646555466 scopus 로고    scopus 로고
    • Protein-lipid interactions and surface activity in the pulmonary surfactant system
    • Serrano A.G., and Perez-Gil J. Protein-lipid interactions and surface activity in the pulmonary surfactant system. Chem. Phys. Lipids 141 (2006) 105-118
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 105-118
    • Serrano, A.G.1    Perez-Gil, J.2
  • 5
    • 0037180829 scopus 로고    scopus 로고
    • Hydrophobic surfactant proteins in lung function and disease
    • Whitsett J.A., and Weaver T.E. Hydrophobic surfactant proteins in lung function and disease. N. Engl. J. Med. 347 (2002) 2141-2148
    • (2002) N. Engl. J. Med. , vol.347 , pp. 2141-2148
    • Whitsett, J.A.1    Weaver, T.E.2
  • 6
    • 0028875787 scopus 로고
    • Human surfactant protein B: structure, function, regulation, and genetic disease
    • Whitsett J.A., Nogee L.M., Weaver T.E., and Horowitz A.D. Human surfactant protein B: structure, function, regulation, and genetic disease. Physiol. Rev. 75 (1995) 749-757
    • (1995) Physiol. Rev. , vol.75 , pp. 749-757
    • Whitsett, J.A.1    Nogee, L.M.2    Weaver, T.E.3    Horowitz, A.D.4
  • 8
    • 0034708780 scopus 로고    scopus 로고
    • Intracellular localization of processing events in human surfactant protein B biosynthesis
    • Korimilli A., Gonzales L.W., and Guttentag S.H. Intracellular localization of processing events in human surfactant protein B biosynthesis. J. Biol. Chem. 275 (2000) 8672-8679
    • (2000) J. Biol. Chem. , vol.275 , pp. 8672-8679
    • Korimilli, A.1    Gonzales, L.W.2    Guttentag, S.H.3
  • 9
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford R.S., Sheppard P.O., and O'Hara P.J. Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J. Lipid Res. 36 (1995) 1653-1663
    • (1995) J. Lipid Res. , vol.36 , pp. 1653-1663
    • Munford, R.S.1    Sheppard, P.O.2    O'Hara, P.J.3
  • 12
    • 13844299352 scopus 로고    scopus 로고
    • Solution structure of human saposin C in a detergent environment
    • Hawkins C.A., Alba E., and Tjandra N. Solution structure of human saposin C in a detergent environment. J. Mol. Biol. 346 (2005) 1381-1392
    • (2005) J. Mol. Biol. , vol.346 , pp. 1381-1392
    • Hawkins, C.A.1    Alba, E.2    Tjandra, N.3
  • 15
    • 0029807305 scopus 로고    scopus 로고
    • Structural requirements for targeting of surfactant protein B (SP-B) to secretory granules in vitro and in vivo
    • Lin S., Akinbi H.T., Breslin J.S., and Weaver T.E. Structural requirements for targeting of surfactant protein B (SP-B) to secretory granules in vitro and in vivo. J. Biol. Chem. 271 (1996) 19689-19695
    • (1996) J. Biol. Chem. , vol.271 , pp. 19689-19695
    • Lin, S.1    Akinbi, H.T.2    Breslin, J.S.3    Weaver, T.E.4
  • 16
    • 0030600233 scopus 로고    scopus 로고
    • Structural requirements for intracellular transport of pulmonary surfactant protein B (SP-B)
    • Lin S., Phillips K.S., Wilder M.R., and Weaver T.E. Structural requirements for intracellular transport of pulmonary surfactant protein B (SP-B). Biochim. Biophys. Acta 1312 (1996) 177-185
    • (1996) Biochim. Biophys. Acta , vol.1312 , pp. 177-185
    • Lin, S.1    Phillips, K.S.2    Wilder, M.R.3    Weaver, T.E.4
  • 18
    • 33749049579 scopus 로고    scopus 로고
    • Production in Escherichia coli of a recombinant C-terminal truncated precursor of surfactant protein B (rproSP-B Delta C). Structure and interaction with lipid interfaces
    • Serrano A.G., Cabre E.J., Oviedo J.M., Cruz A., Gonzalez B., Palacios A., Estrada P., and Perez-Gil J. Production in Escherichia coli of a recombinant C-terminal truncated precursor of surfactant protein B (rproSP-B Delta C). Structure and interaction with lipid interfaces. Biochim. Biophys. Acta 1758 (2006) 1621-1632
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1621-1632
    • Serrano, A.G.1    Cabre, E.J.2    Oviedo, J.M.3    Cruz, A.4    Gonzalez, B.5    Palacios, A.6    Estrada, P.7    Perez-Gil, J.8
  • 19
    • 0031740744 scopus 로고    scopus 로고
    • Structure, processing and properties of surfactant protein A
    • McCormack F.X. Structure, processing and properties of surfactant protein A. Biochim. Biophys. Acta 1408 (1998) 109-131
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 109-131
    • McCormack, F.X.1
  • 20
    • 0031772193 scopus 로고    scopus 로고
    • Synthesis, processing and secretion of surfactant proteins B and C
    • Weaver T.E. Synthesis, processing and secretion of surfactant proteins B and C. Biochim. Biophys. Acta 1408 (1998) 173-179
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 173-179
    • Weaver, T.E.1
  • 22
    • 17544375900 scopus 로고    scopus 로고
    • Inhibition of cellular processing of surfactant protein C by drugs affecting intracellular pH gradients
    • Beers M.F. Inhibition of cellular processing of surfactant protein C by drugs affecting intracellular pH gradients. J. Biol. Chem. 271 (1996) 14361-14370
    • (1996) J. Biol. Chem. , vol.271 , pp. 14361-14370
    • Beers, M.F.1
  • 24
    • 33646147571 scopus 로고    scopus 로고
    • Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein SP-B
    • Serrano A.G., Ryan M., Weaver T.E., and Perez-Gil J. Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein SP-B. Biophys. J. 90 (2006) 238-249
    • (2006) Biophys. J. , vol.90 , pp. 238-249
    • Serrano, A.G.1    Ryan, M.2    Weaver, T.E.3    Perez-Gil, J.4
  • 25
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 26
    • 0347994116 scopus 로고    scopus 로고
    • On the analysis of membrane protein circular dichroism spectra
    • Sreerama N., and Woody R.W. On the analysis of membrane protein circular dichroism spectra. Protein Sci. 13 (2004) 100-112
    • (2004) Protein Sci. , vol.13 , pp. 100-112
    • Sreerama, N.1    Woody, R.W.2
  • 27
    • 11844286267 scopus 로고    scopus 로고
    • Intrinsic structural and functional determinants within the amino acid sequence of mature pulmonary surfactant protein SP-B
    • Serrano A.G., Cruz A., Rodriguez-Capote K., Possmayer F., and Perez-Gil J. Intrinsic structural and functional determinants within the amino acid sequence of mature pulmonary surfactant protein SP-B. Biochemistry 44 (2005) 417-430
    • (2005) Biochemistry , vol.44 , pp. 417-430
    • Serrano, A.G.1    Cruz, A.2    Rodriguez-Capote, K.3    Possmayer, F.4    Perez-Gil, J.5
  • 29
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 30
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3 (1996) 842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 31
    • 0028912411 scopus 로고
    • Conformational flexibility of pulmonary surfactant proteins SP-B and SP-C, studied in aqueous organic solvents
    • Cruz A., Casals C., and Perez-Gil J. Conformational flexibility of pulmonary surfactant proteins SP-B and SP-C, studied in aqueous organic solvents. Biochim. Biophys. Acta 1255 (1995) 68-76
    • (1995) Biochim. Biophys. Acta , vol.1255 , pp. 68-76
    • Cruz, A.1    Casals, C.2    Perez-Gil, J.3
  • 33
    • 0032581011 scopus 로고    scopus 로고
    • Depth profiles of pulmonary surfactant protein B in phosphatidylcholine bilayers, studied by fluorescence and electron spin resonance spectroscopy
    • Cruz A., Casals C., Plasencia I., Marsh D., and Perez-Gil J. Depth profiles of pulmonary surfactant protein B in phosphatidylcholine bilayers, studied by fluorescence and electron spin resonance spectroscopy. Biochemistry 37 (1998) 9488-9496
    • (1998) Biochemistry , vol.37 , pp. 9488-9496
    • Cruz, A.1    Casals, C.2    Plasencia, I.3    Marsh, D.4    Perez-Gil, J.5
  • 34
    • 33646560648 scopus 로고    scopus 로고
    • Anchoring mechanisms of membrane-associated M13 major coat protein
    • Stopar D., Spruijt R.B., and Hemminga M.A. Anchoring mechanisms of membrane-associated M13 major coat protein. Chem. Phys. Lipids 141 (2006) 83-93
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 83-93
    • Stopar, D.1    Spruijt, R.B.2    Hemminga, M.A.3
  • 35
    • 1942533534 scopus 로고    scopus 로고
    • Processing of pulmonary surfactant protein B by napsin and cathepsin H
    • Ueno T., Linder S., Na C.L., Rice W.R., Johansson J., and Weaver T.E. Processing of pulmonary surfactant protein B by napsin and cathepsin H. J. Biol. Chem. 279 (2004) 16178-16184
    • (2004) J. Biol. Chem. , vol.279 , pp. 16178-16184
    • Ueno, T.1    Linder, S.2    Na, C.L.3    Rice, W.R.4    Johansson, J.5    Weaver, T.E.6
  • 39
    • 0035839568 scopus 로고    scopus 로고
    • Response of an integral granule membrane protein to changes in pH
    • Bell-Parikh L.C., Eipper B.A., and Mains R.E. Response of an integral granule membrane protein to changes in pH. J. Biol. Chem. 276 (2001) 29854-29863
    • (2001) J. Biol. Chem. , vol.276 , pp. 29854-29863
    • Bell-Parikh, L.C.1    Eipper, B.A.2    Mains, R.E.3
  • 40
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E., and Huttner W.B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 115 (1991) 1505-1519
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 41
    • 0030043593 scopus 로고    scopus 로고
    • Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH
    • Colomer V., Kicska G.A., and Rindler M.J. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Chem. 271 (1996) 48-55
    • (1996) J. Biol. Chem. , vol.271 , pp. 48-55
    • Colomer, V.1    Kicska, G.A.2    Rindler, M.J.3
  • 42
    • 0023610730 scopus 로고
    • Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles
    • Orci L., Ravazzola M., Storch M.J., Anderson R.G., Vassalli J.D., and Perrelet A. Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. Cell 49 (1987) 865-868
    • (1987) Cell , vol.49 , pp. 865-868
    • Orci, L.1    Ravazzola, M.2    Storch, M.J.3    Anderson, R.G.4    Vassalli, J.D.5    Perrelet, A.6
  • 43
    • 0027200952 scopus 로고
    • The family of pro-hormone and pro-protein convertases
    • Seidah N.G., Day R., and Chretien M. The family of pro-hormone and pro-protein convertases. Biochem. Soc. Trans. 21 Pt. 3 (1993) 685-691
    • (1993) Biochem. Soc. Trans. , vol.21 , Issue.PART 3 , pp. 685-691
    • Seidah, N.G.1    Day, R.2    Chretien, M.3
  • 44
    • 0028238359 scopus 로고
    • Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2
    • Shennan K.I., Taylor N.A., and Docherty K. Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2. J. Biol. Chem. 269 (1994) 18646-18650
    • (1994) J. Biol. Chem. , vol.269 , pp. 18646-18650
    • Shennan, K.I.1    Taylor, N.A.2    Docherty, K.3
  • 45
    • 0038731763 scopus 로고    scopus 로고
    • Acidification and protein traffic
    • Weisz O.A. Acidification and protein traffic. Int. Rev. Cytol. 226 (2003) 259-319
    • (2003) Int. Rev. Cytol. , vol.226 , pp. 259-319
    • Weisz, O.A.1
  • 49
    • 0032512712 scopus 로고    scopus 로고
    • Secondary structure and limited proteolysis give experimental evidence that the precursor of pulmonary surfactant protein B contains three saposin-like domains
    • Zaltash S., and Johansson J. Secondary structure and limited proteolysis give experimental evidence that the precursor of pulmonary surfactant protein B contains three saposin-like domains. FEBS Lett. 423 (1998) 1-4
    • (1998) FEBS Lett. , vol.423 , pp. 1-4
    • Zaltash, S.1    Johansson, J.2
  • 50
    • 0034697239 scopus 로고    scopus 로고
    • Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids
    • Salvioli R., Tatti M., Ciaffoni F., and Vaccaro A.M. Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids. FEBS Lett. 472 (2000) 17-21
    • (2000) FEBS Lett. , vol.472 , pp. 17-21
    • Salvioli, R.1    Tatti, M.2    Ciaffoni, F.3    Vaccaro, A.M.4
  • 51
    • 0029417339 scopus 로고
    • pH-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • Vaccaro A.M., Ciaffoni F., Tatti M., Salvioli R., Barca A., Tognozzi D., and Scerch C. pH-dependent conformational properties of saposins and their interactions with phospholipid membranes. J. Biol. Chem. 270 (1995) 30576-30580
    • (1995) J. Biol. Chem. , vol.270 , pp. 30576-30580
    • Vaccaro, A.M.1    Ciaffoni, F.2    Tatti, M.3    Salvioli, R.4    Barca, A.5    Tognozzi, D.6    Scerch, C.7
  • 52
    • 2642714907 scopus 로고    scopus 로고
    • Effect of acidic pH on the structure and lipid binding properties of porcine surfactant protein A. Potential role of acidification along its exocytic pathway
    • Ruano M.L., Perez-Gil J., and Casals C. Effect of acidic pH on the structure and lipid binding properties of porcine surfactant protein A. Potential role of acidification along its exocytic pathway. J. Biol. Chem. 273 (1998) 15183-15191
    • (1998) J. Biol. Chem. , vol.273 , pp. 15183-15191
    • Ruano, M.L.1    Perez-Gil, J.2    Casals, C.3


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