메뉴 건너뛰기




Volumn 55, Issue 10, 2004, Pages 717-723

Molecular cloning and characterization of calreticulin from rainbow trout (Oncorhynchus mykiss)

Author keywords

Calcium; Calreticulin; Chaperone; Rainbow trout

Indexed keywords

AMINO ACID DERIVATIVE; CALRETICULIN; COMPLEMENTARY DNA; CYSTEINE DERIVATIVE; NITROGEN; PEPTIDE DERIVATIVE;

EID: 1242292363     PISSN: 00937711     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00251-003-0631-4     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 0033546416 scopus 로고    scopus 로고
    • Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules
    • Arosa FA, de Jesus O, Porto G, Carmo AM, de Sousa M (1999) Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. J Biol Chem 274:16917-16922
    • (1999) J Biol Chem , vol.274 , pp. 16917-16922
    • Arosa, F.A.1    De Jesus, O.2    Porto, G.3    Carmo, A.M.4    De Sousa, M.5
  • 7
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RA, Michalak M (1989) Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 264:21522-21528
    • (1989) J Biol Chem , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.4    Michalak, M.5
  • 8
    • 0032468408 scopus 로고    scopus 로고
    • Calreticulin, a component of the endoplasmic reticulum and of cytotoxic lymphocyte granules, regulates perforin-mediated lysis in the hemolytic model system
    • Fraser SA, Michalak M, Welch WH, Hudig D (1998) Calreticulin, a component of the endoplasmic reticulum and of cytotoxic lymphocyte granules, regulates perforin-mediated lysis in the hemolytic model system. Biochem Cell Biol 76:881-887
    • (1998) Biochem Cell Biol , vol.76 , pp. 881-887
    • Fraser, S.A.1    Michalak, M.2    Welch, W.H.3    Hudig, D.4
  • 9
    • 0034655278 scopus 로고    scopus 로고
    • Perform lytic activity is controlled by calreticulin
    • Fraser SA, Karimi R, Michalak M, Hudig D (2000) Perform lytic activity is controlled by calreticulin. J Immunol 164:4150-4155
    • (2000) J Immunol , vol.164 , pp. 4150-4155
    • Fraser, S.A.1    Karimi, R.2    Michalak, M.3    Hudig, D.4
  • 10
    • 0036449386 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA clones encoding CD9 from Atlantic salmon (Salmo salar) and rainbow trout (Oncorhynchus mykiss)
    • Fujiki K, Gauley J, Bols N, Dixon B (2002) Cloning and characterization of cDNA clones encoding CD9 from Atlantic salmon (Salmo salar) and rainbow trout (Oncorhynchus mykiss). Immunogenetics 54:604-609
    • (2002) Immunogenetics , vol.54 , pp. 604-609
    • Fujiki, K.1    Gauley, J.2    Bols, N.3    Dixon, B.4
  • 11
    • 0036089384 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of tumor necrosis factor alpha from a marine fish reveal its constitutive expression and ubiquitous nature
    • Garcia-Castillo JPP, Mulero V, Meseguer J (2002) Molecular cloning and expression analysis of tumor necrosis factor alpha from a marine fish reveal its constitutive expression and ubiquitous nature. Immunogenetics 54:200-207
    • (2002) Immunogenetics , vol.54 , pp. 200-207
    • Garcia-Castillo, J.P.P.1    Mulero, V.2    Meseguer, J.3
  • 12
    • 0030746953 scopus 로고    scopus 로고
    • Characterization of rainbow trout terminal deoxynucleotidyl transferase structure and expression. TdT and RAG1 co-expression define the trout primary lymphoid tissues
    • Hansen JD (1997) Characterization of rainbow trout terminal deoxynucleotidyl transferase structure and expression. TdT and RAG1 co-expression define the trout primary lymphoid tissues. Immunogenetics 46:367-375
    • (1997) Immunogenetics , vol.46 , pp. 367-375
    • Hansen, J.D.1
  • 13
    • 0034653507 scopus 로고    scopus 로고
    • Description of an ectothermic TCR coreceptor, CD8 a, in rainbow trout
    • Hansen JD, Strassburger P (2000) Description of an ectothermic TCR coreceptor, CD8 a, in rainbow trout. J Immunol 164: 3132-3139
    • (2000) J Immunol , vol.164 , pp. 3132-3139
    • Hansen, J.D.1    Strassburger, P.2
  • 14
    • 0034856389 scopus 로고    scopus 로고
    • Human placental calreticulin characterization of domain structure and post-translational modifications
    • Højrup P, Roepstorff P, Houen G (2001) Human placental calreticulin characterization of domain structure and post-translational modifications. Eur J Biochem 268:2558-2565
    • (2001) Eur J Biochem , vol.268 , pp. 2558-2565
    • Højrup, P.1    Roepstorff, P.2    Houen, G.3
  • 15
    • 0032053396 scopus 로고    scopus 로고
    • Calreticulin associates with stress proteins: Implications for chaperone function during heat stress
    • Jethmalani SM, Henle KJ (1998) Calreticulin associates with stress proteins: implications for chaperone function during heat stress. J Cell Biochem 69:30-43
    • (1998) J Cell Biochem , vol.69 , pp. 30-43
    • Jethmalani, S.M.1    Henle, K.J.2
  • 16
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • Munro HN (ed) Academic Press, New York
    • Jukes TH, Cantor CR (1969) Evolution of protein molecules. In: Munro HN (ed) Mammalian protein metabolism. Academic Press, New York, pp 21-132
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 17
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M (2001) MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17:1244-1245
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 18
    • 0033966713 scopus 로고    scopus 로고
    • Molecular cloning and characterization of calreticulin, a calcium-binding protein involved in the regeneration of rice-cultured suspension cells
    • Li Z, Komatsu S (2000) Molecular cloning and characterization of calreticulin, a calcium-binding protein involved in the regeneration of rice-cultured suspension cells. Eur J Biochem 267:737-745
    • (2000) Eur J Biochem , vol.267 , pp. 737-745
    • Li, Z.1    Komatsu, S.2
  • 19
    • 0026801469 scopus 로고
    • The 5′ flanking region of human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters
    • McCauliffe DP, Yang Y, Wilson J, Sontheimer RD, Capra D (1992) The 5′ flanking region of human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. J Biol Chem 267:2557-2562
    • (1992) J Biol Chem , vol.267 , pp. 2557-2562
    • McCauliffe, D.P.1    Yang, Y.2    Wilson, J.3    Sontheimer, R.D.4    Capra, D.5
  • 21
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S, Pelham HR (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 22
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 23
    • 0015955240 scopus 로고
    • Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum
    • Ostwald TJ, McLennan DH (1974) Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J Biol Chem 249:974-979
    • (1974) J Biol Chem , vol.249 , pp. 974-979
    • Ostwald, T.J.1    McLennan, D.H.2
  • 24
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson JR, Ora A, Van PN, Helenius A (1995) Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol Cell 6:1173-1184
    • (1995) Mol Biol Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 25
    • 13044294042 scopus 로고    scopus 로고
    • Expression and temperature-dependent regulation of the beta2-microglobulin (Cyca-B2m) gene in a cold-blooded vertebrate, the common carp (Cyprinus carpio L.)
    • Rodrigues PN, Dixon B, Roelofs J, Rombout JH, Egberts E, Pohajdak B, Stet RJ (1998) Expression and temperature-dependent regulation of the beta2-microglobulin (Cyca-B2m) gene in a cold-blooded vertebrate, the common carp (Cyprinus carpio L.). Dev Immunol 5:263-275
    • (1998) Dev Immunol , vol.5 , pp. 263-275
    • Rodrigues, P.N.1    Dixon, B.2    Roelofs, J.3    Rombout, J.H.4    Egberts, E.5    Pohajdak, B.6    Stet, R.J.7
  • 26
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits
    • Rojiani MV, Finlay BB, Gray V, Dedhar S (1991) In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits. Biochemistry 30:9859-9866
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 28
    • 0034048613 scopus 로고    scopus 로고
    • Genes dependent on zebrafish cyclops function identified by AFLP differential gene expression screen
    • Rubinstein AL, Lee D, Luo R, Henion PD, Halpern ME (2000) Genes dependent on zebrafish cyclops function identified by AFLP differential gene expression screen. Genesis 26:86-97
    • (2000) Genesis , vol.26 , pp. 86-97
    • Rubinstein, A.L.1    Lee, D.2    Luo, R.3    Henion, P.D.4    Halpern, M.E.5
  • 29
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan B, Lehner PJ, Ortmann B, Spies T, Cresswell P (1996) Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5:103-114
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 30
    • 0023375195 scopus 로고
    • The neighbour-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbour-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 32
    • 0019453144 scopus 로고
    • Single-copy DNA relationships between diploid and tetraploid teleostean fish species
    • Schmidtke J, Kandt I (1981) Single-copy DNA relationships between diploid and tetraploid teleostean fish species. Chromosoma 83:191-197
    • (1981) Chromosoma , vol.83 , pp. 191-197
    • Schmidtke, J.1    Kandt, I.2
  • 34
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium-binding ER/SR protein
    • Smith MJ, Koch GL (1989) Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium-binding ER/SR protein. EMBO J 8:3581-3586
    • (1989) EMBO J , vol.8 , pp. 3581-3586
    • Smith, M.J.1    Koch, G.L.2
  • 35
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1974) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1974) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.