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Volumn 55, Issue 4, 1998, Pages 455-464

Heterogeneous forms of adenotin-1 of different subcellular localization

Author keywords

Adenosine binding protein; Adenotin; NECA; prp94 homologue; Radioligand binding; Rat liver

Indexed keywords

2 CHLOROADENOSINE; ADENOSINE 5' (N ETHYLCARBOXAMIDE); ADENOSINE DERIVATIVE; ADENOTIN; FAT; RADIOLIGAND;

EID: 0032519873     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00483-8     Document Type: Article
Times cited : (3)

References (52)
  • 1
    • 0020956911 scopus 로고
    • Binding characteristics of an adenosine receptor in human placenta
    • Fox IH and Kurpis L, Binding characteristics of an adenosine receptor in human placenta. J Biol Chem 258: 6952-6955, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 6952-6955
    • Fox, I.H.1    Kurpis, L.2
  • 3
    • 0024336081 scopus 로고
    • 3H]-adenosine binding sites of mouse mastocytoma P815 cell membranes: Characterization and solubilization
    • 3H]-adenosine binding sites of mouse mastocytoma P815 cell membranes: characterization and solubilization. J Biochem 105: 888-893, 1989.
    • (1989) J Biochem , vol.105 , pp. 888-893
    • Nakata, H.1    Fujisawa, H.2
  • 4
    • 0023550773 scopus 로고
    • 3H]adenosine binding to pig aorta smooth muscle membranes
    • 3H]adenosine binding to pig aorta smooth muscle membranes. Biochem Pharmacol 36: 3621-3627, 1987.
    • (1987) Biochem Pharmacol , vol.36 , pp. 3621-3627
    • Diocee, D.K.1    Souness, J.E.2
  • 5
    • 0023799020 scopus 로고
    • 3H]adenosine binds to two different adenosine receptors in membranes from the cerebral cortex of the rat
    • 3H]adenosine binds to two different adenosine receptors in membranes from the cerebral cortex of the rat. Neuropharmacology 27: 85-94, 1988.
    • (1988) Neuropharmacology , vol.27 , pp. 85-94
    • Florio, C.1    Traversa, U.2    Vertua, R.3    Puppini, P.4
  • 8
    • 0026740909 scopus 로고
    • Identification of a novel high affinity adenosine binding protein from bovine striatum
    • Lorenzen A, Grün S, Vogt H and Schwabe U, Identification of a novel high affinity adenosine binding protein from bovine striatum. Naunyn-Schmiedebergs Arch Pharmacol 346: 63-68, 1992.
    • (1992) Naunyn-Schmiedebergs Arch Pharmacol , vol.346 , pp. 63-68
    • Lorenzen, A.1    Grün, S.2    Vogt, H.3    Schwabe, U.4
  • 9
    • 0030575917 scopus 로고    scopus 로고
    • Characterization of a novel adenosine binding protein sensitive to cyclic AMP in rat brain cytosolic and particulate fractions
    • Lorenzen A, Groæekatthöfer B, Kerst B, Vogt H, Fein T and Schwabe U, Characterization of a novel adenosine binding protein sensitive to cyclic AMP in rat brain cytosolic and particulate fractions. Biochem Pharmacol 52: 1375-1385, 1996.
    • (1996) Biochem Pharmacol , vol.52 , pp. 1375-1385
    • Lorenzen, A.1    Groæekatthöfer, B.2    Kerst, B.3    Vogt, H.4    Fein, T.5    Schwabe, U.6
  • 10
    • 0024978686 scopus 로고
    • 2-like binding site from human placental membranes
    • 2-like binding site from human placental membranes. J Biol Chem 264: 19898-19903, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 19898-19903
    • Hutchison, K.A.1    Fox, I.H.2
  • 11
    • 0025354022 scopus 로고
    • Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): Properties and homology with mammalian and avian stress proteins
    • Hutchison KA, Nevins B, Perini F and Fox IH, Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): Properties and homology with mammalian and avian stress proteins. Biochemistry 29: 5138-5144, 1990.
    • (1990) Biochemistry , vol.29 , pp. 5138-5144
    • Hutchison, K.A.1    Nevins, B.2    Perini, F.3    Fox, I.H.4
  • 12
    • 0028288905 scopus 로고
    • Purification and characterization of an adenotin-like adenosine binding protein from human platelets
    • Fein T, Schulze E, Bär J and Schwabe U, Purification and characterization of an adenotin-like adenosine binding protein from human platelets. Naunyn-Schmiedebergs Arch Pharmacol 349: 374-380, 1994.
    • (1994) Naunyn-Schmiedebergs Arch Pharmacol , vol.349 , pp. 374-380
    • Fein, T.1    Schulze, E.2    Bär, J.3    Schwabe, U.4
  • 13
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S and Pelham HRB, A C-terminal signal prevents secretion of luminal ER proteins. Cell 48: 899-907, 1987.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 14
    • 0022833371 scopus 로고
    • Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin
    • Koch G, Smith M, Macer D, Webster P and Mortara R, Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. J Cell Sci 86: 217-232, 1986.
    • (1986) J Cell Sci , vol.86 , pp. 217-232
    • Koch, G.1    Smith, M.2    Macer, D.3    Webster, P.4    Mortara, R.5
  • 15
    • 0021910786 scopus 로고
    • Structure and assembly of the endoplasmic reticulum. the synthesis of three major endoplasmic reticulum proteins during lipopoly-saccharide-induced differentiation of murine lymphocytes
    • Lewis MJ, Mazzarella RA and Green M, Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopoly-saccharide-induced differentiation of murine lymphocytes. J Biol Chem 260: 3050-3057, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3050-3057
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 16
    • 0023664518 scopus 로고
    • ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)
    • Mazzarella RA and Green M, ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J Biol Chem. 262: 8875-8883, 1987.
    • (1987) J Biol Chem. , vol.262 , pp. 8875-8883
    • Mazzarella, R.A.1    Green, M.2
  • 18
    • 0025354155 scopus 로고
    • Human homologue of murine tumor rejection antigen gp96: 5′-Regulatory and coding regions and relationship to stress-induced proteins
    • Maki RG, Old LJ and Srivastava PK, Human homologue of murine tumor rejection antigen gp96: 5′-Regulatory and coding regions and relationship to stress-induced proteins. Proc Natl Acad Sci USA 87: 5658-5662, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5658-5662
    • Maki, R.G.1    Old, L.J.2    Srivastava, P.K.3
  • 19
    • 0024326031 scopus 로고
    • Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium
    • Nguyen Van P, Peter F and Soling H-D, Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. J Biol Chem 264: 17494-17501, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 17494-17501
    • Van Nguyen, P.1    Peter, F.2    Soling, H.-D.3
  • 20
    • 0024450145 scopus 로고
    • Isolation and partial characterization of an 80,000-Dalton protein kinase from the microvessels of the porcine brain
    • Dechert U, Weber M, Weber-Schaeuffelen M and Wollny E, Isolation and partial characterization of an 80,000-Dalton protein kinase from the microvessels of the porcine brain. J Neurochem 53: 1268-1275, 1989.
    • (1989) J Neurochem , vol.53 , pp. 1268-1275
    • Dechert, U.1    Weber, M.2    Weber-Schaeuffelen, M.3    Wollny, E.4
  • 22
    • 0023133224 scopus 로고
    • Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells
    • Lee AS, Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem Sci 12: 20-23, 1987.
    • (1987) Trends Biochem Sci , vol.12 , pp. 20-23
    • Lee, A.S.1
  • 23
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething M-J and Sambrook J, The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464, 1988.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 24
    • 0023240964 scopus 로고
    • Extracellular adenosine, inosine, hypoxanthine, and xanthine in relation to tissue nucleotides and purines in rat striatum during transient ischemia
    • Hagberg H, Andersson P, Lacarewicz J, Jacobson I, Butcher S and Sandberg M, Extracellular adenosine, inosine, hypoxanthine, and xanthine in relation to tissue nucleotides and purines in rat striatum during transient ischemia. J Neurochem 49: 227-231, 1987.
    • (1987) J Neurochem , vol.49 , pp. 227-231
    • Hagberg, H.1    Andersson, P.2    Lacarewicz, J.3    Jacobson, I.4    Butcher, S.5    Sandberg, M.6
  • 25
    • 0028061921 scopus 로고
    • Ethanol-responsive genes in neural cells include the 78-kilodalton glucose-regulated protein (grp78) and the 94-kilodalton glucose-regulated protein (grp94) molecular chaperones
    • Miles MF, Wilke N, Elliot M, Tanner W and Shah S, Ethanol-responsive genes in neural cells include the 78-kilodalton glucose-regulated protein (grp78) and the 94-kilodalton glucose-regulated protein (grp94) molecular chaperones. Mol Pharmacol 46: 873-879, 1994.
    • (1994) Mol Pharmacol , vol.46 , pp. 873-879
    • Miles, M.F.1    Wilke, N.2    Elliot, M.3    Tanner, W.4    Shah, S.5
  • 26
    • 0030040433 scopus 로고    scopus 로고
    • Regulation of the stress-like protein adenotin in PC-12 cells by ethanol exposure
    • Rabin RA, Regulation of the stress-like protein adenotin in PC-12 cells by ethanol exposure. Biochem Pharmacol 51: 183-186, 1996.
    • (1996) Biochem Pharmacol , vol.51 , pp. 183-186
    • Rabin, R.A.1
  • 27
    • 0025784485 scopus 로고
    • A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum
    • Navarro D, Qadri I and Pereira L, A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum. Virology 184: 253-264, 1991.
    • (1991) Virology , vol.184 , pp. 253-264
    • Navarro, D.1    Qadri, I.2    Pereira, L.3
  • 28
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff WT, Hruska KA Jr, McCourt DW, Green M and Schwartz BD, HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J Exp Med 176: 657-666, 1992.
    • (1992) J Exp Med , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska Jr., K.A.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 29
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick J, Aviel S and Argon Y, The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem 267: 21303-21306, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 31
    • 0027208741 scopus 로고
    • Tumor rejection antigen gp96/grp94 is an ATPase: Implications for protein folding and antigen presentation
    • Li Z and Srivastava PK, Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J 12: 3143-3151, 1993.
    • (1993) EMBO J , vol.12 , pp. 3143-3151
    • Li, Z.1    Srivastava, P.K.2
  • 33
    • 0016361823 scopus 로고
    • Long-term preservation of liver for subcellular fractionation
    • Fleischer S and Kervina M, Long-term preservation of liver for subcellular fractionation. Methods Enzymol 31: 3-6, 1974.
    • (1974) Methods Enzymol , vol.31 , pp. 3-6
    • Fleischer, S.1    Kervina, M.2
  • 34
    • 0016378181 scopus 로고
    • Subcellular fractionation of rat liver
    • Fleischer S and Kervina M, Subcellular fractionation of rat liver. Methods Enzymol 31: 6-41, 1974.
    • (1974) Methods Enzymol , vol.31 , pp. 6-41
    • Fleischer, S.1    Kervina, M.2
  • 35
    • 0018801562 scopus 로고
    • Purification and characterization of a rat liver Golgi alpha-mannosidase capable of processing asparagine-linked oligosaccharides
    • Tabas I and Kornfeld S, Purification and characterization of a rat liver Golgi alpha-mannosidase capable of processing asparagine-linked oligosaccharides. J Biol Chem 254: 1655-11663, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 1655-11663
    • Tabas, I.1    Kornfeld, S.2
  • 36
    • 0015504823 scopus 로고
    • Studies on 5′-nucleotidases of rat liver
    • Pletsch QA and Coffey JW, Studies on 5′-nucleotidases of rat liver. Biochim Biophys Acta 276: 192-205, 1972.
    • (1972) Biochim Biophys Acta , vol.276 , pp. 192-205
    • Pletsch, Q.A.1    Coffey, J.W.2
  • 37
    • 84911255601 scopus 로고
    • 5′-Nucleotidase, UV-method
    • Ed. Bergmeyer HU, Verlag Chemie, Weinheim, Deerfield Beach, Basel
    • Heinz F and Haeckel R, 5′-Nucleotidase, UV-method. In: Methods of Enzymatic Analysis, Vol. IV (Ed. Bergmeyer HU), pp. 113-120. Verlag Chemie, Weinheim, Deerfield Beach, Basel, 1984.
    • (1984) Methods of Enzymatic Analysis , vol.4 , pp. 113-120
    • Heinz, F.1    Haeckel, R.2
  • 38
    • 0000191753 scopus 로고
    • Lactate dehydrogenase, UV-method with pyruvate and NADH
    • Ed. Bergmeyer HU, Verlag Chemie, Weinheim, Deerfield Beach, Basel
    • Vassault A, Lactate dehydrogenase, UV-method with pyruvate and NADH. In: Methods of Enzymatic Analysis, Vol. III (Ed. Bergmeyer HU), pp. 118-126. Verlag Chemie, Weinheim, Deerfield Beach, Basel, 1984.
    • (1984) Methods of Enzymatic Analysis , vol.3 , pp. 118-126
    • Vassault, A.1
  • 39
    • 0000076302 scopus 로고
    • Ed. Bergmeyer HU, Verlag Chemie, Weinheim, Deerfield Beach, Basel
    • Stitt M, Fumarase. In: Methods of Enzymatic Analysis, Vol. IV, (Ed. Bergmeyer HU), pp. 359-362. Verlag Chemie, Weinheim, Deerfield Beach, Basel, 1984.
    • (1984) Methods of Enzymatic Analysis , vol.4 , pp. 359-362
    • Fumarase, S.M.1
  • 40
    • 77957006891 scopus 로고
    • Olucose-6-phosphatase from liver
    • Swanson MA, Olucose-6-phosphatase from liver. Methods Enzymol 3: 541-543, 1955.
    • (1955) Methods Enzymol , vol.3 , pp. 541-543
    • Swanson, M.A.1
  • 41
    • 0342953642 scopus 로고
    • Galactosyltransferase
    • Ed. Bergmeyer HU, Verlag Chemie, Weinheim, Deerfield Beach, Basel
    • Verdon B and Berger EG, Galactosyltransferase. In: Methods of Enzymatic Analysis, Vol. III (Ed. Bergmeyer HU), pp. 374-381. Verlag Chemie, Weinheim, Deerfield Beach, Basel, 1984.
    • (1984) Methods of Enzymatic Analysis , vol.3 , pp. 374-381
    • Verdon, B.1    Berger, E.G.2
  • 42
    • 0018850985 scopus 로고
    • A simple, rapid, and sensitive DNA assay procedure
    • Labarca C and Paigen K, A simple, rapid, and sensitive DNA assay procedure. Anal Biochem 102: 344-352, 1980.
    • (1980) Anal Biochem , vol.102 , pp. 344-352
    • Labarca, C.1    Paigen, K.2
  • 43
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson GL, A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83: 346-356, 1977.
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0020084268 scopus 로고
    • Validation and statistical analysis of radioligand binding data for mixtures of pharmacological receptor subtypes
    • De Lean A, Hancock AA and Lefkowitz RJ, Validation and statistical analysis of radioligand binding data for mixtures of pharmacological receptor subtypes. Mol Pharmocol 21: 5-16, 1982.
    • (1982) Mol Pharmocol , vol.21 , pp. 5-16
    • De Lean, A.1    Hancock, A.A.2    Lefkowitz, R.J.3
  • 47
    • 0023019562 scopus 로고
    • Hsp108, a novel heat shock inducible protein of chicken
    • Sargan DR, Tsai M-J and O'Malley BW, Hsp108, a novel heat shock inducible protein of chicken. Biochemistry 25: 6252-6258, 1986.
    • (1986) Biochemistry , vol.25 , pp. 6252-6258
    • Sargan, D.R.1    Tsai, M.-J.2    O'Malley, B.W.3
  • 48
    • 0027931855 scopus 로고
    • GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II
    • Cala SE and Jones LR, GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II. J Biol Chem 269: 5926-5931, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 5926-5931
    • Cala, S.E.1    Jones, L.R.2
  • 49
    • 0026689538 scopus 로고
    • Heavy chain binding protein (BiP/ GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase
    • Takemoto H, Yoshimori T, Yamamoto A, Miyata Y, Yahara I, Inoue K and Tashiro Y, Heavy chain binding protein (BiP/ GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase. Arch Biochem Biophys 296: 129-136, 1992.
    • (1992) Arch Biochem Biophys , vol.296 , pp. 129-136
    • Takemoto, H.1    Yoshimori, T.2    Yamamoto, A.3    Miyata, Y.4    Yahara, I.5    Inoue, K.6    Tashiro, Y.7
  • 50
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C and Koch GLE, Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59: 729-737, 1989.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 51
    • 0022534393 scopus 로고
    • Tumor rejection antigens of chemically induced sarcomas of inbred mice
    • Srivastava PK, DeLeo AB and Old LJ, Tumor rejection antigens of chemically induced sarcomas of inbred mice. Proc Natl Acad Sci USA 83: 3407-3411, 1986.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3407-3411
    • Srivastava, P.K.1    Deleo, A.B.2    Old, L.J.3
  • 52
    • 0028811321 scopus 로고
    • Molecular heterogeneity of tumor rejection antigen/heat shock protein gp96
    • Feldweg AM and Srivastava PK, Molecular heterogeneity of tumor rejection antigen/heat shock protein gp96. Int J Cancer 63: 310-314, 1995.
    • (1995) Int J Cancer , vol.63 , pp. 310-314
    • Feldweg, A.M.1    Srivastava, P.K.2


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