메뉴 건너뛰기




Volumn 35, Issue 9, 1998, Pages 503-512

Human complement factor I: Its expression by insect cells and its biochemical and structural characterisation

Author keywords

Baculovirus; Complement factor I; Expression; Spectroscopy; Structure

Indexed keywords

COMPLEMENT COMPONENT C3B; COMPLEMENT FACTOR H; COMPLEMENT FACTOR I; SERINE PROTEINASE; SIGNAL PEPTIDE;

EID: 0031784286     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(98)00052-2     Document Type: Article
Times cited : (14)

References (46)
  • 1
    • 0023105043 scopus 로고
    • Characterization of the primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones
    • Catterall, C.F., Lyons, A., Sim, R.B., Day, A.J., Harris, T.J.R., 1987. Characterization of the primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones. Biochem. J. 242, 849-856.
    • (1987) Biochem. J. , vol.242 , pp. 849-856
    • Catterall, C.F.1    Lyons, A.2    Sim, R.B.3    Day, A.J.4    Harris, T.J.R.5
  • 3
    • 0027380363 scopus 로고
    • Small-scale preparation of complement components C3 and C4
    • Dodds, A.W., 1993. Small-scale preparation of complement components C3 and C4. Meth. Enzymol. 223, 46-61.
    • (1993) Meth. Enzymol. , vol.223 , pp. 46-61
    • Dodds, A.W.1
  • 4
    • 0028094301 scopus 로고
    • Circular dichroism
    • Jones, C., Mulloy, B., Thomas, A.H. (Eds.), Humana Press Inc., New Jersey
    • Drake, A.F., 1994. Circular dichroism. In: Jones, C., Mulloy, B., Thomas, A.H. (Eds.), Physical Methods of Analysis. Methods Mol. Biol. 22, Humana Press Inc., New Jersey, pp. 219-244.
    • (1994) Physical Methods of Analysis. Methods Mol. Biol. , vol.22 , pp. 219-244
    • Drake, A.F.1
  • 5
    • 0030581168 scopus 로고    scopus 로고
    • Assessment of protein fold predictions from sequence information: The predicted α/β doubly wound fold of the von Willebrand Factor Type a domain is similar to its crystal structure
    • Edwards, Y.J.K., Perkins, S.J., 1996. Assessment of protein fold predictions from sequence information: the predicted α/β doubly wound fold of the von Willebrand Factor Type A domain is similar to its crystal structure. J Molec. Biol. 260, 277-285.
    • (1996) J Molec. Biol. , vol.260 , pp. 277-285
    • Edwards, Y.J.K.1    Perkins, S.J.2
  • 6
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
    • Fass, D., Blacklow, S., Kim, P.S., Berger, J.M., 1997. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature (London) 388, 691-693.
    • (1997) Nature (London) , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.S.3    Berger, J.M.4
  • 7
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide 1, 3, 4, 6-tetrachloro-3a, 6a-diphenylglycoluril
    • Fraker, P.J., Speck, J.C., 1978. Protein and cell membrane iodinations with a sparingly soluble chloroamide 1, 3, 4, 6-tetrachloro-3a, 6a-diphenylglycoluril. Biochem. Biophys. Res. Commun. 80, 849-857.
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speck, J.C.2
  • 8
    • 0021164865 scopus 로고
    • Biosynthesis and postsynthetic processing of human C3b/C4b inactivator (Factor I) in three hepatoma cell lines
    • Goldberger, G., Arnaout, M.A., Aden, D., Kay, R., Rits, M., Colten, H.R., 1984. Biosynthesis and postsynthetic processing of human C3b/C4b inactivator (Factor I) in three hepatoma cell lines. J. Biol. Chem. 259, 6492-6497.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6492-6497
    • Goldberger, G.1    Arnaout, M.A.2    Aden, D.3    Kay, R.4    Rits, M.5    Colten, H.R.6
  • 9
    • 0023250642 scopus 로고
    • Human complement factor I: Analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4
    • Goldberger, G., Bruns, G.A.P., Rits, M., Edge, M.D., Kwiatkowski, D.J., 1987. Human complement factor I: analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4. J. Biol. Chem. 262, 10065-10071.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10065-10071
    • Goldberger, G.1    Bruns, G.A.P.2    Rits, M.3    Edge, M.D.4    Kwiatkowski, D.J.5
  • 10
    • 0028062558 scopus 로고
    • Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy
    • Humana Press Inc., New Jersey
    • Haris, P.I., Chapman, D., 1994. Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. Methods Mol. Biol. 22, 183-202. Humana Press Inc., New Jersey.
    • (1994) Methods Mol. Biol. , vol.22 , pp. 183-202
    • Haris, P.I.1    Chapman, D.2
  • 11
    • 0023047824 scopus 로고
    • A Fourier transform infrared investigation of the structural differences between ribonuclease a and ribonuclease S
    • Haris, P.I., Lee, D.C., Chapman, D., 1986. A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S. Biochim. Biophys. Acta. 874, 255-265.
    • (1986) Biochim. Biophys. Acta. , vol.874 , pp. 255-265
    • Haris, P.I.1    Lee, D.C.2    Chapman, D.3
  • 12
    • 0030995856 scopus 로고    scopus 로고
    • Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40
    • Hohenester, E., Maurer, P., Timpl, R., 1997. Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J. 16, 3778-3786.
    • (1997) EMBO J. , vol.16 , pp. 3778-3786
    • Hohenester, E.1    Maurer, P.2    Timpl, R.3
  • 13
    • 0019950783 scopus 로고
    • Purification of human C3b inactivator by monoclonal antibody affinity chromatography
    • Hsiung, L.-M., Barclay, A.N., Brandon, M.R., Sim, E., Porter, R.R. 1982. Purification of human C3b inactivator by monoclonal antibody affinity chromatography. Biochem. J. 203, 293-298.
    • (1982) Biochem. J. , vol.203 , pp. 293-298
    • Hsiung, L.-M.1    Barclay, A.N.2    Brandon, M.R.3    Sim, E.4    Porter, R.R.5
  • 14
    • 0028789632 scopus 로고
    • Biochemical analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells
    • Jarvis, D.J., Finn, E.E., 1995. Biochemical analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells. Virology 212, 500-511.
    • (1995) Virology , vol.212 , pp. 500-511
    • Jarvis, D.J.1    Finn, E.E.2
  • 15
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., Sander, C., 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 16
    • 0003910124 scopus 로고
    • Baculovirus expression systems: A laboratory guide
    • King, L.A., Possee, R.D., 1992. Baculovirus expression systems: a laboratory guide. Chapman and Hall, 1992.
    • (1992) Chapman and Hall , vol.1992
    • King, L.A.1    Possee, R.D.2
  • 17
    • 0027989820 scopus 로고
    • Tamm-Horsfall glycoprotein: Role in inhibition and promotion of renal calcium oxalate stone formation studied with Fourier transform infrared spectroscopy
    • Knörle, R., Schnierle, P., Koch, A., Buchholz, N.-P., Hering, F., Seiler, H., Ackermann, T., Rutishauser, G., 1994. Tamm-Horsfall glycoprotein: Role in inhibition and promotion of renal calcium oxalate stone formation studied with Fourier transform infrared spectroscopy. Clin. Chem. 40, 1739-1743.
    • (1994) Clin. Chem. , vol.40 , pp. 1739-1743
    • Knörle, R.1    Schnierle, P.2    Koch, A.3    Buchholz, N.-P.4    Hering, F.5    Seiler, H.6    Ackermann, T.7    Rutishauser, G.8
  • 18
    • 0027422822 scopus 로고
    • Characterization of Xenopus laevis complement factor I structure - Conservation of modular structure except for an unusual insert not present in human factor I
    • Kunnath-Muglia, L.M., Chang, G.H., Sim, R.B., Day, A.J., Ezekowitz, R.A., 1993. Characterization of Xenopus laevis complement factor I structure - conservation of modular structure except for an unusual insert not present in human factor I. Molec. Immun. 30,1249-1256.
    • (1993) Molec. Immun. , vol.30 , pp. 1249-1256
    • Kunnath-Muglia, L.M.1    Chang, G.H.2    Sim, R.B.3    Day, A.J.4    Ezekowitz, R.A.5
  • 19
    • 0030004710 scopus 로고    scopus 로고
    • Dissection of CR1, factor H, membrane cofactor protein and factor B binding and functional sites in the third complement component
    • Lambris, J.D., Lao, Z., Oglesby, T.J., Atkinson, J.P., Hack, C.E., Becherer, J.D., 1996. Dissection of CR1, factor H, membrane cofactor protein and factor B binding and functional sites in the third complement component. J. Immun. 156, 4821-4832.
    • (1996) J. Immun. , vol.156 , pp. 4821-4832
    • Lambris, J.D.1    Lao, Z.2    Oglesby, T.J.3    Atkinson, J.P.4    Hack, C.E.5    Becherer, J.D.6
  • 20
    • 0028117588 scopus 로고
    • Overexpression, purification and characterization of third component of complement
    • Lao, Z., Wang Y., Mavroidis, M., Kostavasili, I., Lambris, J.D., 1994. Overexpression, purification and characterization of third component of complement. J. Immun. Meth. 176,127-139.
    • (1994) J. Immun. Meth. , vol.176 , pp. 127-139
    • Lao, Z.1    Wang, Y.2    Mavroidis, M.3    Kostavasili, I.4    Lambris, J.D.5
  • 22
    • 0024999461 scopus 로고
    • Determination of protein secondary-structure using factor analysis of infrared spectra
    • Lee, D.C., Haris, P.I., Chapman, D., Mitchell, R.C., 1990. Determination of protein secondary-structure using factor analysis of infrared spectra. Biochemistry 29, 9185-9193.
    • (1990) Biochemistry , vol.29 , pp. 9185-9193
    • Lee, D.C.1    Haris, P.I.2    Chapman, D.3    Mitchell, R.C.4
  • 23
    • 0029924246 scopus 로고    scopus 로고
    • DNa cloning, sequencing and chromosomal assignment of the gene for mouse complement factor I (C3b/C4b inactivator): Identification of a species specific divergent segment in factor I
    • Minta, J.O., Wong, M.J., Kozak, C.A., Kunnath-Muglia, L.M., Goldberger, G., 1996. cDNA cloning, sequencing and chromosomal assignment of the gene for mouse complement factor I (C3b/C4b inactivator): identification of a species specific divergent segment in factor I. Molec. Immunol. 33, 101-112.
    • (1996) Molec. Immunol. , vol.33 , pp. 101-112
    • Minta, J.O.1    Wong, M.J.2    Kozak, C.A.3    Kunnath-Muglia, L.M.4    Goldberger, G.5
  • 24
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: The calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S.J., 1986. Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Fur. J. Biochem. 157, 169-180.
    • (1986) Fur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 25
    • 0027371944 scopus 로고
    • Identity of the putative serine-proteinase fold in proteins of the complement system with nine relevant crystal structures
    • Perkins, S.J., Smith, K.F., 1993. Identity of the putative serine-proteinase fold in proteins of the complement system with nine relevant crystal structures. Biochem. J. 295, 109-114.
    • (1993) Biochem. J. , vol.295 , pp. 109-114
    • Perkins, S.J.1    Smith, K.F.2
  • 26
    • 0027381489 scopus 로고
    • Molecular modelling of the domain structure of factor I of human complement by X-ray and neutron solution scattering
    • Perkins, S.J., Smith, K.F., Sim, R.B., 1993. Molecular modelling of the domain structure of factor I of human complement by X-ray and neutron solution scattering. Biochem. J. 295, 101-108.
    • (1993) Biochem. J. , vol.295 , pp. 101-108
    • Perkins, S.J.1    Smith, K.F.2    Sim, R.B.3
  • 27
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral-equations. CONTIN - A general-purpose constrained regularization program for inverting noisy linear algebraic and integral-equations
    • Provencher, S.W., 1982. A constrained regularization method for inverting data represented by linear algebraic or integral-equations. CONTIN - a general-purpose constrained regularization program for inverting noisy linear algebraic and integral-equations. Comput. Phys. Commun. 27, 213-227 and 229-242.
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 28
    • 0028158348 scopus 로고
    • The SRCR superfamily: A family reminiscent of the Ig superfamily
    • Resnick, D., Pearson, A., Krieger, M., 1994. The SRCR superfamily: a family reminiscent of the Ig superfamily. TIBS 19, 5-8.
    • (1994) TIBS , vol.19 , pp. 5-8
    • Resnick, D.1    Pearson, A.2    Krieger, M.3
  • 30
    • 0029902780 scopus 로고    scopus 로고
    • Bridging the protein sequence-structure gap by structure predictions
    • Rost, B., Sander, C., 1996. Bridging the protein sequence-structure gap by structure predictions. Annu. Rev. Biophys. Biomol. Struct. 25, 113-136.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 113-136
    • Rost, B.1    Sander, C.2
  • 31
    • 0028284219 scopus 로고
    • Biologically active recombinant human complement factor H: Synthesis and secretion by the baculovirus system
    • Sharma, A.K., Pangburn, M.K., 1994. Biologically active recombinant human complement factor H: synthesis and secretion by the baculovirus system. Gene. 143, 301-302.
    • (1994) Gene. , vol.143 , pp. 301-302
    • Sharma, A.K.1    Pangburn, M.K.2
  • 32
    • 0029763437 scopus 로고    scopus 로고
    • Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis
    • Sharma, A.K., Pangburn, M.K., 1996. Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis. Proc. natl. Acad. Sci. U.S.A. 93, 10996-11001.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10996-11001
    • Sharma, A.K.1    Pangburn, M.K.2
  • 33
    • 0031035409 scopus 로고    scopus 로고
    • Localization by site-directed mutagenesis of the site in human complement factor H that binds to Streptococcus pyogenes M protein
    • Sharma, A.K., Pangburn, M.K., 1997. Localization by site-directed mutagenesis of the site in human complement factor H that binds to Streptococcus pyogenes M protein. Infect. Immun. 65, 484-487.
    • (1997) Infect. Immun. , vol.65 , pp. 484-487
    • Sharma, A.K.1    Pangburn, M.K.2
  • 34
    • 0020967243 scopus 로고
    • Enzymic assay of C3b receptor on intact cells and solubilized cells
    • Sim, E., Sim, R.B., 1983. Enzymic assay of C3b receptor on intact cells and solubilized cells. Biochem. J. 210, 567-576.
    • (1983) Biochem. J. , vol.210 , pp. 567-576
    • Sim, E.1    Sim, R.B.2
  • 35
    • 0027377724 scopus 로고
    • Complement factor I and cofactors in control of complement system convertase enzymes
    • Sim, R.B., Day, A.J., Moffatt, B.E., Fontaine, M., 1993. Complement factor I and cofactors in control of complement system convertase enzymes. Meth. Enzymol. 223, 13-35.
    • (1993) Meth. Enzymol. , vol.223 , pp. 13-35
    • Sim, R.B.1    Day, A.J.2    Moffatt, B.E.3    Fontaine, M.4
  • 36
    • 0030773223 scopus 로고    scopus 로고
    • Interactions between human complement components factor H, factor I and C3b
    • Soames, C.J., Sim, R.B., 1997. Interactions between human complement components factor H, factor I and C3b. Biochem. J. 326, 553-561.
    • (1997) Biochem. J. , vol.326 , pp. 553-561
    • Soames, C.J.1    Sim, R.B.2
  • 38
    • 0027945541 scopus 로고
    • Altered glycosylation and selected mutation in recombinant human complement component C9: Effects on haemolytic activity
    • Taylor, K.M., Morgan, B.P., Campbell, A.K., 1994. Altered glycosylation and selected mutation in recombinant human complement component C9: effects on haemolytic activity. Immunology 83, 501-506.
    • (1994) Immunology , vol.83 , pp. 501-506
    • Taylor, K.M.1    Morgan, B.P.2    Campbell, A.K.3
  • 39
    • 84889234408 scopus 로고
    • PhD Thesis. University of London
    • Ullman, C.G., 1994. PhD Thesis. University of London.
    • (1994)
    • Ullman, C.G.1
  • 40
    • 0030770324 scopus 로고    scopus 로고
    • The factor I and follistatin domain families: The return of a prodigal son
    • Ullman, C.G., Perkins, S.J., 1997. The factor I and follistatin domain families: the return of a prodigal son. Biochem. J. 326, 939-941.
    • (1997) Biochem. J. , vol.326 , pp. 939-941
    • Ullman, C.G.1    Perkins, S.J.2
  • 41
    • 0028979029 scopus 로고
    • β-sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy
    • Ullman, C.G., Haris, P.I., Smith, K.F., Sim, R.B., Emery, V.C., Perkins, S.J., 1995. β-sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy. FEBS Lett. 371, 199-203.
    • (1995) FEBS Lett. , vol.371 , pp. 199-203
    • Ullman, C.G.1    Haris, P.I.2    Smith, K.F.3    Sim, R.B.4    Emery, V.C.5    Perkins, S.J.6
  • 42
    • 84889182220 scopus 로고    scopus 로고
    • β-sheet structures in the five domains of human complement factor I
    • Abstract
    • Ullman, C.G., Sim, R.B., Perkins, S.J., 1996. β-sheet structures in the five domains of human complement factor I. Molec. Immun. 33, 80-80 (Abstract).
    • (1996) Molec. Immun. , vol.33 , pp. 80-80
    • Ullman, C.G.1    Sim, R.B.2    Perkins, S.J.3
  • 43
    • 84889206288 scopus 로고    scopus 로고
    • Expression, secretion and characterisation of active human factor I by insect cells
    • Abstract
    • Ullman, C.G., Chamberlain, D., Sim, R.B., Perkins, S.J., 1997. Expression, secretion and characterisation of active human factor I by insect cells. Exp. Clin. Immunogenet. 14, 38-38 (Abstract).
    • (1997) Exp. Clin. Immunogenet. , vol.14 , pp. 38-38
    • Ullman, C.G.1    Chamberlain, D.2    Sim, R.B.3    Perkins, S.J.4
  • 44
    • 0027318961 scopus 로고
    • Biological role of oligosaccharides: All of the theories are correct
    • Varki, A., 1993. Biological role of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 46
    • 0028904950 scopus 로고
    • Processing of human factor I in COS-1 cells co-transfected with factor I and paired basic amino acid cleaving enzyme (PACE) cDNA
    • Wong, M.J., Goldberger, G., Isenman, D.E., Minta, J.O., 1995. Processing of human factor I in COS-1 cells co-transfected with factor I and paired basic amino acid cleaving enzyme (PACE) cDNA. Molec. Immun. 32, 379-387.
    • (1995) Molec. Immun. , vol.32 , pp. 379-387
    • Wong, M.J.1    Goldberger, G.2    Isenman, D.E.3    Minta, J.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.