메뉴 건너뛰기




Volumn 90, Issue 1, 1997, Pages 372-381

Calreticulin biosynthesis and processing in human myeloid cells: Demonstration of signal peptide cleavage and N-glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

CALRETICULIN;

EID: 0030910249     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.1.372.372_372_381     Document Type: Article
Times cited : (36)

References (49)
  • 2
    • 0026567608 scopus 로고
    • Purification of an inositol 1,4,5-trisphosphate-binding calreticulin-containing intracellular compartment of HL-60 cells
    • Van Delden C, Favre C, Spät A, Cerny E, Krause K-H, Lew DP: Purification of an inositol 1,4,5-trisphosphate-binding calreticulin-containing intracellular compartment of HL-60 cells. Biochem J 281:651, 1992
    • (1992) Biochem J , vol.281 , pp. 651
    • Van Delden, C.1    Favre, C.2    Spät, A.3    Cerny, E.4    Krause, K.-H.5    Lew, D.P.6
  • 4
    • 0027982729 scopus 로고
    • Calreticulin: Not just another calcium-binding protein
    • Nash PD, Opas M, Michalak M: Calreticulin: Not just another calcium-binding protein. Mol Cell Biochem 135:71, 1994
    • (1994) Mol Cell Biochem , vol.135 , pp. 71
    • Nash, P.D.1    Opas, M.2    Michalak, M.3
  • 5
    • 0022606290 scopus 로고
    • Development of a radioimmunoassay for quantitation of calregulin in bovine tissues
    • Khanna NC, Waisman DM: Development of a radioimmunoassay for quantitation of calregulin in bovine tissues. Biochemistry 25:1078, 1986
    • (1986) Biochemistry , vol.25 , pp. 1078
    • Khanna, N.C.1    Waisman, D.M.2
  • 6
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) or skeletal muscle sarcoplasmic reliculum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M: Molecular cloning of the high affinity calcium-binding protein (calreticulin) or skeletal muscle sarcoplasmic reliculum. J Biol Chem 264:21522, 1989
    • (1989) J Biol Chem , vol.264 , pp. 21522
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Michalak, M.5
  • 7
    • 0025345647 scopus 로고
    • A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia "memory molecule"
    • McCauliffe DP, Zappi E, Lieu T-S, Michalak M, Sontheimer RD, Capra JD: A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia "memory molecule". J Clin Invest 86:332, 1990
    • (1990) J Clin Invest , vol.86 , pp. 332
    • McCauliffe, D.P.1    Zappi, E.2    Lieu, T.-S.3    Michalak, M.4    Sontheimer, R.D.5    Capra, J.D.6
  • 9
    • 0028240392 scopus 로고
    • Novel functions for calreticulin: Interaction with integrins and modulation of gene expression
    • Dedhar S: Novel functions for calreticulin: Interaction with integrins and modulation of gene expression. Trends Biochem Sci 19:269, 1994
    • (1994) Trends Biochem Sci , vol.19 , pp. 269
    • Dedhar, S.1
  • 10
  • 11
    • 0029737757 scopus 로고    scopus 로고
    • Calreticulin: How many functions in how many cellular compartments
    • Meldolesi J, Krause KH, Michalak M: Calreticulin: How many functions in how many cellular compartments. Cell Calcium 20:83, 1996
    • (1996) Cell Calcium , vol.20 , pp. 83
    • Meldolesi, J.1    Krause, K.H.2    Michalak, M.3
  • 12
    • 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 a subunits
    • Rojiani MV, Finlay BB, Gray V, Dedhar S: 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 a subunits. Biochemistry 30:9859, 1991
    • (1991) Biochemistry , vol.30 , pp. 9859
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 13
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin α-subunit-binding protein
    • Leung-Hagesteijn CY, Milankov K, Michalak M, Wilkins J, Dedhar S: Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin α-subunit-binding protein. J Cell Sci 107:589, 1994
    • (1994) J Cell Sci , vol.107 , pp. 589
    • Leung-Hagesteijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 16
    • 0027507325 scopus 로고
    • The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes
    • Dupuis M, Schaerer E, Krause K-H, Tschopp J: The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. J Exp Med 177:1, 1993
    • (1993) J Exp Med , vol.177 , pp. 1
    • Dupuis, M.1    Schaerer, E.2    Krause, K.-H.3    Tschopp, J.4
  • 20
    • 0029889209 scopus 로고    scopus 로고
    • Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen
    • Cheng ST, Nguyen TQ, Yang YS, Capra JD, Sontheimer RD: Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen. J Immunol 156:4484, 1996
    • (1996) J Immunol , vol.156 , pp. 4484
    • Cheng, S.T.1    Nguyen, T.Q.2    Yang, Y.S.3    Capra, J.D.4    Sontheimer, R.D.5
  • 21
    • 0028606112 scopus 로고
    • Identification of calreticulin as a rubella virus RNA binding protein
    • Singh NK, Atreya CD, Nakhasi HL: Identification of calreticulin as a rubella virus RNA binding protein. Proc Natl Acad Sci USA 91:12770, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12770
    • Singh, N.K.1    Atreya, C.D.2    Nakhasi, H.L.3
  • 22
    • 0029066118 scopus 로고
    • The rubella virus RNA binding activity of human calreticulin is localized to the N-terminal domain
    • Atreya CD, Singh NK, Nakhasi HL: The rubella virus RNA binding activity of human calreticulin is localized to the N-terminal domain. J Virol 69:3848, 1995
    • (1995) J Virol , vol.69 , pp. 3848
    • Atreya, C.D.1    Singh, N.K.2    Nakhasi, H.L.3
  • 23
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White TK, Zhu Q, Tanzer ML: Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J Biol Chem 270:15926, 1995
    • (1995) J Biol Chem , vol.270 , pp. 15926
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 25
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef WM, McCormick SJ, Clark RA: Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem 270:4741, 1995
    • (1995) J Biol Chem , vol.270 , pp. 4741
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 26
    • 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: Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol Cell 6:1173, 1995
    • (1995) Mol Biol Cell , vol.6 , pp. 1173
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 27
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein
    • Smith MJ, Koch GLE: Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J 8:3581, 1989
    • (1989) EMBO J , vol.8 , pp. 3581
    • Smith, M.J.1    Koch, G.L.E.2
  • 29
    • 0342266916 scopus 로고
    • Cloning of the cDNA and functional expression of the 47 kilodalton cytosolic component of the human neutrophil respiratory burst oxidase
    • Volpp BD, Nauseef WM, Donelson JE, Moser DR, Clark RA: Cloning of the cDNA and functional expression of the 47 kilodalton cytosolic component of the human neutrophil respiratory burst oxidase. Proc Natl Acad Sci USA 86:7195, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7195
    • Volpp, B.D.1    Nauseef, W.M.2    Donelson, J.E.3    Moser, D.R.4    Clark, R.A.5
  • 31
    • 0025834610 scopus 로고
    • Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum
    • Milner RE, Baksh S, Shemanko C, Carpenter MR, Smillie L, Vance JE, Opas M, Michalak M: Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum. J Biol Chem 266:7155, 1991
    • (1991) J Biol Chem , vol.266 , pp. 7155
    • Milner, R.E.1    Baksh, S.2    Shemanko, C.3    Carpenter, M.R.4    Smillie, L.5    Vance, J.E.6    Opas, M.7    Michalak, M.8
  • 33
    • 0020643575 scopus 로고
    • Staining of the Ca2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "stains-all"
    • Campbell KP, MacLennan DH, Jorgensen AO: Staining of the Ca2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "stains-all". J Biol Chem 258:11267, 1983
    • (1983) J Biol Chem , vol.258 , pp. 11267
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 34
    • 0020540731 scopus 로고
    • Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase. Translocation during activation
    • Borregaard N, Heiple JM, Simons ER, Clark RA: Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase. Translocation during activation. J Cell Biol 97:52, 1983
    • (1983) J Cell Biol , vol.97 , pp. 52
    • Borregaard, N.1    Heiple, J.M.2    Simons, E.R.3    Clark, R.A.4
  • 35
    • 0017782474 scopus 로고
    • Continuous growth and differentiation of human myeloid leukaemic cells in suspension culture
    • Collins SJ, Gallo RC, Gallagher RE: Continuous growth and differentiation of human myeloid leukaemic cells in suspension culture. Nature 270:347, 1977
    • (1977) Nature , vol.270 , pp. 347
    • Collins, S.J.1    Gallo, R.C.2    Gallagher, R.E.3
  • 36
    • 0023264655 scopus 로고
    • Characterization of a new human diploid myeloid leukemia cell line (PLB-985) with granulocytic and monocytic differentiating capacity
    • Tucker KA, Lilly MB, Heck L Jr, Rado TA: Characterization of a new human diploid myeloid leukemia cell line (PLB-985) with granulocytic and monocytic differentiating capacity. Blood 70:372, 1987
    • (1987) Blood , vol.70 , pp. 372
    • Tucker, K.A.1    Lilly, M.B.2    Heck Jr., L.3    Rado, T.A.4
  • 37
    • 0022640063 scopus 로고
    • Myeloperoxidase biosynthesis by a human promyelocytic leukemia cell line: Insight into myeloperoxidase deficiency
    • Nauseef WM: Myeloperoxidase biosynthesis by a human promyelocytic leukemia cell line: Insight into myeloperoxidase deficiency. Blood 67:865, 1986
    • (1986) Blood , vol.67 , pp. 865
    • Nauseef, W.M.1
  • 38
    • 0343893080 scopus 로고
    • Molecular biology of MPO
    • Everse J, Everse KE, Grisham MB (eds), Boca Raton, FL, CRC
    • Johnson KR, Nauseef WM: Molecular biology of MPO, in Everse J, Everse KE, Grisham MB (eds): Peroxidases in Chemistry and Biology, Boca Raton, FL, CRC, 1991, p 63
    • (1991) Peroxidases in Chemistry and Biology , pp. 63
    • Johnson, K.R.1    Nauseef, W.M.2
  • 39
    • 0018863514 scopus 로고
    • Induction of differentiation of human and murine myeloid leukemia cells in culture by tunicamycin
    • Nakayasu M, Terada M, Tamura G, Sugimura T: Induction of differentiation of human and murine myeloid leukemia cells in culture by tunicamycin. Proc Natl Acad Sci USA 77:409, 1980
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 409
    • Nakayasu, M.1    Terada, M.2    Tamura, G.3    Sugimura, T.4
  • 40
    • 0023638218 scopus 로고
    • Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase
    • Nauseef WM: Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase. Blood 70:1143, 1987
    • (1987) Blood , vol.70 , pp. 1143
    • Nauseef, W.M.1
  • 41
    • 0026737234 scopus 로고
    • Different sorting of Lys-AspGlu-Leu proteins in rat liver
    • Peter F, Van PN, Söling H-D: Different sorting of Lys-AspGlu-Leu proteins in rat liver. J Biol Chem 267:10631, 1992
    • (1992) J Biol Chem , vol.267 , pp. 10631
    • Peter, F.1    Van, P.N.2    Söling, H.-D.3
  • 42
    • 0023124195 scopus 로고
    • Comparison of calregulins from vertebrate livers
    • Khanna NC, Tokuda M, Waisman DM: Comparison of calregulins from vertebrate livers. Biochem J 242:245, 1987
    • (1987) Biochem J , vol.242 , pp. 245
    • Khanna, N.C.1    Tokuda, M.2    Waisman, D.M.3
  • 43
    • 0019332267 scopus 로고
    • Assembly of the sarcoplasmic reticulum: Biosynthesis of the high affinity calcium binding protein in rat skeletal muscle cell cultures
    • Michalak M, MacLennan DH: Assembly of the sarcoplasmic reticulum: Biosynthesis of the high affinity calcium binding protein in rat skeletal muscle cell cultures. J Biol Chem 255:1327, 1980
    • (1980) J Biol Chem , vol.255 , pp. 1327
    • Michalak, M.1    MacLennan, D.H.2
  • 44
    • 0019332294 scopus 로고
    • Localization of the high affinity calcium binding protein and an intrinsic glycoprotein in sarcoplasmic reticulum membranes
    • Michalak M, Campbell KP, MacLennan DH: Localization of the high affinity calcium binding protein and an intrinsic glycoprotein in sarcoplasmic reticulum membranes. J Biol Chem 255:1317, 1980
    • (1980) J Biol Chem , vol.255 , pp. 1317
    • Michalak, M.1    Campbell, K.P.2    MacLennan, D.H.3
  • 45
    • 0021821853 scopus 로고
    • Structure and assembly of the endoplasmic reticulum. Biosynthetic sorting of endoplasmic reticulum proteins
    • Lewis MJ, Turco SJ, Green M: Structure and assembly of the endoplasmic reticulum. Biosynthetic sorting of endoplasmic reticulum proteins. J Biol Chem 260:6926, 1985
    • (1985) J Biol Chem , vol.260 , pp. 6926
    • Lewis, M.J.1    Turco, S.J.2    Green, M.3
  • 46
    • 0021910786 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes
    • Lewis MJ, Mazzarella RA, Green M: Structure and assembly of the endoplasmic reticulum: The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes. J Biol Chem 260:3050, 1985
    • (1985) J Biol Chem , vol.260 , pp. 3050
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 47
    • 0022547428 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum
    • Lewis MJ, Mazzarella RA, Green M: Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum. Arch Biochem Biophys 245:389, 1986
    • (1986) Arch Biochem Biophys , vol.245 , pp. 389
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 48
    • 0024326031 scopus 로고
    • Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium: No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles
    • Van PN, Peter F, Soling H-D: Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium: No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles. J Biol Chem 264:17494, 1989
    • (1989) J Biol Chem , vol.264 , pp. 17494
    • Van, P.N.1    Peter, F.2    Soling, H.-D.3
  • 49
    • 0028128694 scopus 로고
    • Heat shock-induced prompt glycosylation. Identification of P-SG67 as calreticulin
    • Jethmalani SM, Henle KJ, Kaushal GP: Heat shock-induced prompt glycosylation. Identification of P-SG67 as calreticulin. J Biol Chem 269:23603, 1994
    • (1994) J Biol Chem , vol.269 , pp. 23603
    • Jethmalani, S.M.1    Henle, K.J.2    Kaushal, G.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.