메뉴 건너뛰기




Volumn 40, Issue 13, 2004, Pages 943-948

Stabilization of peptide guinea pig myelin basic protein 72-85 by N-terminal acetylation - Implications for immunological studies

Author keywords

Acetylation; Experimental autoimmune encephalomyelitis, EAE; Major histocompatibility complex, MHC; Myelin basic protein, MBP; Peptide; Pyroglutamic acid

Indexed keywords

AMINO ACID; GLUTAMINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MYELIN BASIC PROTEIN; PEPTIDE DERIVATIVE; PYROGLUTAMIC ACID;

EID: 0347915528     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2003.10.015     Document Type: Article
Times cited : (11)

References (36)
  • 1
    • 0002509419 scopus 로고
    • Sequencing of proteins and peptides
    • Work T.S., Burdon R.H. (Eds.). Elsevier, Amsterdam
    • Allen, G., 1981. Sequencing of proteins and peptides. In: Work T.S., Burdon R.H. (Eds.), Laboratory techniques in biochemistry and molecular biology. Elsevier, Amsterdam, pp. 245-250.
    • (1981) Laboratory Techniques in Biochemistry and Molecular Biology , pp. 245-250
    • Allen, G.1
  • 2
    • 0037100296 scopus 로고    scopus 로고
    • The majority of immunogenic epitopes generate CD4(+) T cells that are dependent on MHC class II-bound peptide-flanking residues
    • Arnold P.Y., La Gruta N.L., Miller T., Vignali K.M., Adams P.S., Woodland D.L., Vignali D.A.A. The majority of immunogenic epitopes generate CD4(+) T cells that are dependent on MHC class II-bound peptide-flanking residues. J. Immunol. 169:2002;739-749.
    • (2002) J. Immunol. , vol.169 , pp. 739-749
    • Arnold, P.Y.1    La Gruta, N.L.2    Miller, T.3    Vignali, K.M.4    Adams, P.S.5    Woodland, D.L.6    Vignali, D.A.A.7
  • 5
    • 0019465142 scopus 로고
    • The rapid isolation of clonable antigen-specific T lymphocyte lines capable of mediating autoimmune encephalomyelitis
    • Ben-Nun A., Wekerle H., Cohen I.R. The rapid isolation of clonable antigen-specific T lymphocyte lines capable of mediating autoimmune encephalomyelitis. Eur. J. Immunol. 11:1981;195-199.
    • (1981) Eur. J. Immunol. , vol.11 , pp. 195-199
    • Ben-Nun, A.1    Wekerle, H.2    Cohen, I.R.3
  • 7
    • 0023664609 scopus 로고
    • An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl- peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes
    • Busby W.H. Jr., Quackenbush G.E., Humm J., Youngblood W.W., Kizer J.S. An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. J. Biol. Chem. 262:1987;8532-8536.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8532-8536
    • Busby, W.H.Jr.1    Quackenbush, G.E.2    Humm, J.3    Youngblood, W.W.4    Kizer, J.S.5
  • 8
    • 0026742152 scopus 로고
    • Degradation of myelin basic protein by a membrane-associated metalloprotease: Neural distribution of the enzyme
    • Chantry A., Gregson N., Glynn P. Degradation of myelin basic protein by a membrane-associated metalloprotease: neural distribution of the enzyme. Neurochem. Res. 17:1992;861-867.
    • (1992) Neurochem. Res. , vol.17 , pp. 861-867
    • Chantry, A.1    Gregson, N.2    Glynn, P.3
  • 9
    • 0026733449 scopus 로고
    • Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size
    • Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A.A., Strominger J.L. Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size. Nature. 358:1992;764-768.
    • (1992) Nature , vol.358 , pp. 764-768
    • Chicz, R.M.1    Urban, R.G.2    Lane, W.S.3    Gorga, J.C.4    Stern, L.J.5    Vignali, D.A.A.6    Strominger, J.L.7
  • 10
    • 0017362295 scopus 로고
    • The major site of guinea-pig myelin basic protein encephalitogenic in Lewis rats
    • Chou C.H.J., Chou F.C.H., Kowalski T.J., Shapira R., Kibler R.F. The major site of guinea-pig myelin basic protein encephalitogenic in Lewis rats. J. Neurochem. 28:1977;115-119.
    • (1977) J. Neurochem. , vol.28 , pp. 115-119
    • Chou, C.H.J.1    Chou, F.C.H.2    Kowalski, T.J.3    Shapira, R.4    Kibler, R.F.5
  • 11
    • 0018725601 scopus 로고
    • The immune response of Lewis rats to peptide 68-88 of guinea pig myelin basic protein. I. T cell determinants
    • Chou C.H.J., Fritz R.B., Chou F.C.H., Kibler R.F. The immune response of Lewis rats to peptide 68-88 of guinea pig myelin basic protein. I. T cell determinants. J. Immunol. 123:1979;1540-1543.
    • (1979) J. Immunol. , vol.123 , pp. 1540-1543
    • Chou, C.H.J.1    Fritz, R.B.2    Chou, F.C.H.3    Kibler, R.F.4
  • 12
    • 0024599368 scopus 로고
    • Selection of encephalitogenic rat T-lymphocyte clones recognizing an immunodominant epitope on myelin basic protein
    • Chou Y.K., Vandenbark A.A., Jones R.E., Hashim G., Offner H. Selection of encephalitogenic rat T-lymphocyte clones recognizing an immunodominant epitope on myelin basic protein. J. Neurosci. Res. 22:1989;181-187.
    • (1989) J. Neurosci. Res. , vol.22 , pp. 181-187
    • Chou, Y.K.1    Vandenbark, A.A.2    Jones, R.E.3    Hashim, G.4    Offner, H.5
  • 14
    • 0033961824 scopus 로고    scopus 로고
    • Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells
    • Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A., Salter R.D. Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells. J. Immunol. 164:2000;129-135.
    • (2000) J. Immunol. , vol.164 , pp. 129-135
    • Dong, X.1    An, B.2    Salvucci Kierstead, L.3    Storkus, W.J.4    Amoscato, A.A.5    Salter, R.D.6
  • 16
    • 0023785427 scopus 로고
    • A new epitope on human myelin basic protein arising from cleavage by a metalloendoprotease associated with brain myelin membranes
    • Groome N., Chantry A., Earl C., Newcombe J., Keen J., Findlay J., Glynn P. A new epitope on human myelin basic protein arising from cleavage by a metalloendoprotease associated with brain myelin membranes. J. Neuroimmunol. 19:1988;77-88.
    • (1988) J. Neuroimmunol. , vol.19 , pp. 77-88
    • Groome, N.1    Chantry, A.2    Earl, C.3    Newcombe, J.4    Keen, J.5    Findlay, J.6    Glynn, P.7
  • 17
    • 0036337673 scopus 로고    scopus 로고
    • Structural snapshot of aberrant antigen presentation linked to autoimmunity: The immunodominant epitope of MBP complexed with I-Au
    • He X.L., Radu C., Sidney J., Sette A., Ward E.S., Garcia K.C. Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au. Immunity. 17:2002;83-94.
    • (2002) Immunity , vol.17 , pp. 83-94
    • He, X.L.1    Radu, C.2    Sidney, J.3    Sette, A.4    Ward, E.S.5    Garcia, K.C.6
  • 19
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
    • Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L., Wiley D.C. Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. U.S.A. 93:1996;734-738.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 22
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden D.R. The three-dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 13:1995;587-622.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 23
    • 0041167210 scopus 로고    scopus 로고
    • The specificity of antibodies raised against a T cell peptide is influenced by peptide amidation
    • Maillère B., Hervé M. The specificity of antibodies raised against a T cell peptide is influenced by peptide amidation. Mol. Immunol. 34:1997;1003-1009.
    • (1997) Mol. Immunol. , vol.34 , pp. 1003-1009
    • Maillère, B.1    Hervé, M.2
  • 24
    • 0029586024 scopus 로고
    • Fine chemical modifications at N- and C-termini enhance peptide presentation to T cells by increasing the lifespan of both free and MHC-complexed peptides
    • Maillère B., Mourier G., Hervé M., Ménez A. Fine chemical modifications at N- and C-termini enhance peptide presentation to T cells by increasing the lifespan of both free and MHC-complexed peptides. Mol. Immunol. 32:1995;1377-1385.
    • (1995) Mol. Immunol. , vol.32 , pp. 1377-1385
    • Maillère, B.1    Mourier, G.2    Hervé, M.3    Ménez, A.4
  • 25
    • 0017616282 scopus 로고
    • Experimental allergic encephalomyelitis in the Lewis rat: Farther delineation of active sites in guinea pig and bovine myelin basic proteins
    • Martenson R.E., Nomura K., Levine S., Sowinski R. Experimental allergic encephalomyelitis in the Lewis rat: farther delineation of active sites in guinea pig and bovine myelin basic proteins. J. Immunol. 118:1977;1280-1285.
    • (1977) J. Immunol. , vol.118 , pp. 1280-1285
    • Martenson, R.E.1    Nomura, K.2    Levine, S.3    Sowinski, R.4
  • 26
    • 0026756712 scopus 로고
    • The N terminus of human myelin basic protein consists of C2, C4, C6, and C8 alkyl carboxylic acids
    • Moscarello M.A., Pang H., Pace-Asciak C.R., Wood D.D. The N terminus of human myelin basic protein consists of C2, C4, C6, and C8 alkyl carboxylic acids. J. Biol. Chem. 267:1992;9779-9782.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9779-9782
    • Moscarello, M.A.1    Pang, H.2    Pace-Asciak, C.R.3    Wood, D.D.4
  • 27
    • 0027475731 scopus 로고
    • Identification of two distinct properties of class II major histocompatibility complex-associated peptides
    • Nelson C.A., Petzold S.J., Unanue E.R. Identification of two distinct properties of class II major histocompatibility complex-associated peptides. Proc. Natl. Acad. Sci. U.S.A. 90:1993;1227-1231.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1227-1231
    • Nelson, C.A.1    Petzold, S.J.2    Unanue, E.R.3
  • 28
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • Riese R.J., Chapman H.A. Cathepsins and compartmentalization in antigen presentation. Curr. Opin. Immunol. 12:2000;107-113.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 29
    • 0037120160 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides
    • Rijkers D.T.S., Höppener J.W.M., Posthuma G., Lips C.J.M., Liskamp R.M.J. Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides. Chem.-Eur. J. 8:2002;4285-4291.
    • (2002) Chem.-Eur. J. , vol.8 , pp. 4285-4291
    • Rijkers, D.T.S.1    Höppener, J.W.M.2    Posthuma, G.3    Lips, C.J.M.4    Liskamp, R.M.J.5
  • 31
    • 0029736997 scopus 로고    scopus 로고
    • Encephalitogenic T cells are present in Lewis rats protected from autoimmune encephalomyelitis by coimmunization with MBP73-84 and its analog
    • Stepaniak J.A., Gould K.E., Swanborg R.H. Encephalitogenic T cells are present in Lewis rats protected from autoimmune encephalomyelitis by coimmunization with MBP73-84 and its analog. J. Neurosci. Res. 45:1996;447-454.
    • (1996) J. Neurosci. Res. , vol.45 , pp. 447-454
    • Stepaniak, J.A.1    Gould, K.E.2    Swanborg, R.H.3
  • 32
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Watts C. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15:1997;821-850.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 821-850
    • Watts, C.1
  • 33
    • 0035145332 scopus 로고    scopus 로고
    • Antigen processing in the endocytic compartment
    • Watts C. Antigen processing in the endocytic compartment. Curr. Opin. Immunol. 13:2001;26-31.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 26-31
    • Watts, C.1
  • 34
    • 0031058161 scopus 로고    scopus 로고
    • Definition of an extended MHC class II-peptide binding motif for the autoimmune disease-associated Lewis rat RT1.BL molecule
    • Wauben M.H.M., van der Kraan M., Grosfeld-Stulemeyer M.C., Joosten I. Definition of an extended MHC class II-peptide binding motif for the autoimmune disease-associated Lewis rat RT1.BL molecule. Int. Immunol. 9:1997;281-290.
    • (1997) Int. Immunol. , vol.9 , pp. 281-290
    • Wauben, M.H.M.1    Van Der Kraan, M.2    Grosfeld-Stulemeyer, M.C.3    Joosten, I.4
  • 36
    • 0022974996 scopus 로고
    • T-cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis
    • Zamvil S.S., Mitchell D.J., Moore A.C., Kitamura K., Steinman L., Rothbard J.B. T-cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis. Nature. 324:1986;258-260.
    • (1986) Nature , vol.324 , pp. 258-260
    • Zamvil, S.S.1    Mitchell, D.J.2    Moore, A.C.3    Kitamura, K.4    Steinman, L.5    Rothbard, J.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.