메뉴 건너뛰기




Volumn 148, Issue 12, 2007, Pages 5831-5841

Nonassembled human chorionic gonadotropin subunits and αα- homodimers use fast-track processing in the secretory pathway in contrast to αβ-heterodimers

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CHORIONIC GONADOTROPIN BETA SUBUNIT; HETERODIMER;

EID: 36348986740     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2007-0789     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce JG, Parsons TF 1981 Glycoprotein hormones: structure and function. Annu Rev Biochem 50:465-495
    • (1981) Annu Rev Biochem , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 3
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA 1994 Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. Structure 2:545-558
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 4
    • 0032834630 scopus 로고    scopus 로고
    • Structure, pathology and function of the N-linked sugar chains of human chorionic gonadotropin
    • Kobata A, Takeuchi M 1999 Structure, pathology and function of the N-linked sugar chains of human chorionic gonadotropin. Biochim Biophys Acta 1455:315-326
    • (1999) Biochim Biophys Acta , vol.1455 , pp. 315-326
    • Kobata, A.1    Takeuchi, M.2
  • 5
    • 0029801625 scopus 로고    scopus 로고
    • Expression of the human chorionic gonadotropin-β gene cluster in human pituitaries and alternate use of exon 1
    • Dirnhofer S, Hermann M, Hittmair A, Hoermann R, Kapelari K, Berger P 1996 Expression of the human chorionic gonadotropin-β gene cluster in human pituitaries and alternate use of exon 1. J Clin Endocrinol Metab 81:4212-4217
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 4212-4217
    • Dirnhofer, S.1    Hermann, M.2    Hittmair, A.3    Hoermann, R.4    Kapelari, K.5    Berger, P.6
  • 6
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk MM, Keene JL, Boime I 1989 Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J Biol Chem 264:2409-2414
    • (1989) J Biol Chem , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1    Keene, J.L.2    Boime, I.3
  • 7
    • 0035010433 scopus 로고    scopus 로고
    • Evolution and classification of cystine knot-containing hormones and related extracellular signaling molecules
    • Vitt UA, Hsu SY, Hsueh AJ 2001 Evolution and classification of cystine knot-containing hormones and related extracellular signaling molecules. Mol Endocrinol 15:681-694
    • (2001) Mol Endocrinol , vol.15 , pp. 681-694
    • Vitt, U.A.1    Hsu, S.Y.2    Hsueh, A.J.3
  • 8
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg PJ 2003 Disulfide bonds as switches for protein function. Trends Biochem Sci 28:210-214
    • (2003) Trends Biochem Sci , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 9
    • 0042763566 scopus 로고    scopus 로고
    • Not every disulfide lasts forever: Disulfide bond formation as a redox switch
    • Linke K, Jakob U 2003 Not every disulfide lasts forever: disulfide bond formation as a redox switch. Antioxid Redox Signal 5:425-434
    • (2003) Antioxid Redox Signal , vol.5 , pp. 425-434
    • Linke, K.1    Jakob, U.2
  • 10
    • 4143090403 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive beta-subunit disulfide switch
    • Xing Y, Myers R V, Cao D, Lin W, Jiang M, Bernard MP, Moyle WR 2004 Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive beta-subunit disulfide switch. J Biol Chem 279:35437-35448
    • (2004) J Biol Chem , vol.279 , pp. 35437-35448
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7
  • 11
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond C, Helenius A 1995 Quality control in the secretory pathway. Curr Opin Cell Biol 7:523-529
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 13
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags
    • Hebert DN, Garman SC, Molinari M 2005 The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol 15:364-370
    • (2005) Trends Cell Biol , vol.15 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 14
    • 0014450750 scopus 로고
    • Reoxidation of the disulfide bridges of human chorionic gonadotropin (HCG)]
    • German
    • Schlumberger HD, Blobel R 1969 [Reoxidation of the disulfide bridges of human chorionic gonadotropin (HCG)]. Z Naturforsch B 24:54-57 (German)
    • (1969) Z Naturforsch , vol.B 24 , pp. 54-57
    • Schlumberger, H.D.1    Blobel, R.2
  • 15
    • 0026786741 scopus 로고
    • Domain-dependent protein folding is indicated by the intracellular kinetics of disulfide bond formation of human chorionic gonadotropin β subunit
    • Huth JR, Mountjoy K, Perini F, Bedows E, Ruddon RW 1992 Domain-dependent protein folding is indicated by the intracellular kinetics of disulfide bond formation of human chorionic gonadotropin β subunit. J Biol Chem 267:21396-21403
    • (1992) J Biol Chem , vol.267 , pp. 21396-21403
    • Huth, J.R.1    Mountjoy, K.2    Perini, F.3    Bedows, E.4    Ruddon, R.W.5
  • 16
    • 0031030579 scopus 로고    scopus 로고
    • Assisted protein folding
    • Ruddon RW, Bedows E 1997 Assisted protein folding. J Biol Chem 272:3125-3128
    • (1997) J Biol Chem , vol.272 , pp. 3125-3128
    • Ruddon, R.W.1    Bedows, E.2
  • 17
    • 0034697117 scopus 로고    scopus 로고
    • Disulfide bond formation is not required for human chorionic gonadotropin subunit association. Studies with dithiothreitol in JEG-3 cells
    • Singh V, Merz WE 2000 Disulfide bond formation is not required for human chorionic gonadotropin subunit association. Studies with dithiothreitol in JEG-3 cells. J Biol Chem 275:11765-11770
    • (2000) J Biol Chem , vol.275 , pp. 11765-11770
    • Singh, V.1    Merz, W.E.2
  • 19
    • 0035107847 scopus 로고    scopus 로고
    • Threading of a glycosylated protein loop through a protein hole: Implications for combination of human chorionic gonadotropin subunits
    • Xing Y, Williams C, Campbell RK, Cook S, Knoppers M, Addona T, Altarocca V, Moyle WR 2001 Threading of a glycosylated protein loop through a protein hole: implications for combination of human chorionic gonadotropin subunits. Protein Sci 10:226-235
    • (2001) Protein Sci , vol.10 , pp. 226-235
    • Xing, Y.1    Williams, C.2    Campbell, R.K.3    Cook, S.4    Knoppers, M.5    Addona, T.6    Altarocca, V.7    Moyle, W.R.8
  • 20
    • 0025176736 scopus 로고
    • Role of disulfide bond formation in the folding of human chorionic gonadotropin β subunit into an α β dimer assembly-competent form
    • Beebe JS, Mountjoy K, Krzesicki RF, Perini F, Ruddon RW 1990 Role of disulfide bond formation in the folding of human chorionic gonadotropin β subunit into an α β dimer assembly-competent form. J Biol Chem 265:312-317
    • (1990) J Biol Chem , vol.265 , pp. 312-317
    • Beebe, J.S.1    Mountjoy, K.2    Krzesicki, R.F.3    Perini, F.4    Ruddon, R.W.5
  • 21
    • 0027156984 scopus 로고
    • Disulfide bond mutations affect the folding of the human chorionic gonadotropin-β subunit in transfected Chinese hamster ovary cells
    • Bedows E, Huth JR, Suganuma N, Bartels CF, Boime I, Ruddon RW 1993 Disulfide bond mutations affect the folding of the human chorionic gonadotropin-β subunit in transfected Chinese hamster ovary cells. J Biol Chem 268:11655-11662
    • (1993) J Biol Chem , vol.268 , pp. 11655-11662
    • Bedows, E.1    Huth, J.R.2    Suganuma, N.3    Bartels, C.F.4    Boime, I.5    Ruddon, R.W.6
  • 22
    • 0027182764 scopus 로고
    • Protein folding and assembly in vitro parallel intracellular folding and assembly. Catalysis of folding and assembly of the human chorionic gonadotropin α β dimer by protein disulfide isomerase
    • Huth JR, Perini F, Lockridge O, Bedows E, Ruddon RW 1993 Protein folding and assembly in vitro parallel intracellular folding and assembly. Catalysis of folding and assembly of the human chorionic gonadotropin α β dimer by protein disulfide isomerase. J Biol Chem 268:16472-16482
    • (1993) J Biol Chem , vol.268 , pp. 16472-16482
    • Huth, J.R.1    Perini, F.2    Lockridge, O.3    Bedows, E.4    Ruddon, R.W.5
  • 23
    • 0025644869 scopus 로고
    • Permeabilizing cells: Some methods and applications for the study of intracellular processes
    • Schulz I 1990 Permeabilizing cells: some methods and applications for the study of intracellular processes. Methods Enzymol 192:280-300
    • (1990) Methods Enzymol , vol.192 , pp. 280-300
    • Schulz, I.1
  • 24
    • 0023653298 scopus 로고
    • Semi-intact cells permeable to macromolecules: Use in reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex
    • Beckers CJ, Keller DS, Balch WE 1987 Semi-intact cells permeable to macromolecules: use in reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex. Cell 50:523-534
    • (1987) Cell , vol.50 , pp. 523-534
    • Beckers, C.J.1    Keller, D.S.2    Balch, W.E.3
  • 25
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J 1992 Protein folding in the cell. Nature 355:33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 26
    • 0023656167 scopus 로고
    • Detection of a glycosylated, incompletely folded form of chorionic gonadotropin β subunit that is a precursor of hormone assembly in trophoblastic cells
    • Ruddon RW, Krzesicki RF, Norton SE, Beebe JS, Peters BP, Perini F 1987 Detection of a glycosylated, incompletely folded form of chorionic gonadotropin β subunit that is a precursor of hormone assembly in trophoblastic cells. J Biol Chem 262:12533-12540
    • (1987) J Biol Chem , vol.262 , pp. 12533-12540
    • Ruddon, R.W.1    Krzesicki, R.F.2    Norton, S.E.3    Beebe, J.S.4    Peters, B.P.5    Perini, F.6
  • 29
    • 0029944851 scopus 로고    scopus 로고
    • Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains
    • Reddy P, Sparvoli A, Fagioli C, Fassina G, Sitia R 1996 Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains. EMBO J 15:2077-2085
    • (1996) EMBO J , vol.15 , pp. 2077-2085
    • Reddy, P.1    Sparvoli, A.2    Fagioli, C.3    Fassina, G.4    Sitia, R.5
  • 30
    • 0029780765 scopus 로고    scopus 로고
    • Novel covalent chaperone complexes associated with human chorionic gonadotropin β subunit folding intermediates
    • Feng W, Bedows E, Norton SE, Ruddon RW 1996 Novel covalent chaperone complexes associated with human chorionic gonadotropin β subunit folding intermediates. J Biol Chem 271:18543-18548
    • (1996) J Biol Chem , vol.271 , pp. 18543-18548
    • Feng, W.1    Bedows, E.2    Norton, S.E.3    Ruddon, R.W.4
  • 31
    • 0033545187 scopus 로고    scopus 로고
    • The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
    • Hellman R, Vanhove M, Lejeune A, Stevens FJ, Hendershot LM 1999 The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J Cell Biol 144:21-30
    • (1999) J Cell Biol , vol.144 , pp. 21-30
    • Hellman, R.1    Vanhove, M.2    Lejeune, A.3    Stevens, F.J.4    Hendershot, L.M.5
  • 32
    • 33751211226 scopus 로고    scopus 로고
    • Time-dependant folding of immunological epitopes of the human chorionic gonadotropin β-subunit
    • Roig J, Krause JM, Berger P, Merz WE 2007 Time-dependant folding of immunological epitopes of the human chorionic gonadotropin β-subunit. Mol Cell Endocrinol 260- 262:12-22
    • (2007) Mol Cell Endocrinol
    • Roig, J.1    Krause, J.M.2    Berger, P.3    Merz, W.E.4
  • 33
    • 0015501028 scopus 로고
    • Regulation of hemoglobin synthesis. Equal rates of translation and termination of α- and β-globin chains
    • Lodish HF, Jacobsen M 1972 Regulation of hemoglobin synthesis. Equal rates of translation and termination of α- and β-globin chains. J Biol Chem 247:3622-3629
    • (1972) J Biol Chem , vol.247 , pp. 3622-3629
    • Lodish, H.F.1    Jacobsen, M.2
  • 34
  • 35
    • 0018613233 scopus 로고
    • A kinetic model of protein synthesis. Application to hemoglobin synthesis and translational control
    • Bergmann JE, Lodish HF 1979 A kinetic model of protein synthesis. Application to hemoglobin synthesis and translational control. J Biol Chem 254:11927-11937
    • (1979) J Biol Chem , vol.254 , pp. 11927-11937
    • Bergmann, J.E.1    Lodish, H.F.2
  • 36
    • 0036462601 scopus 로고    scopus 로고
    • Protein N-glycosylation along the secretory pathway: Relationship to organelle topography and function, protein quality control, and cell interactions
    • Roth J 2002 Protein N-glycosylation along the secretory pathway: relationship to organelle topography and function, protein quality control, and cell interactions. Chem Rev 102:285-303
    • (2002) Chem Rev , vol.102 , pp. 285-303
    • Roth, J.1
  • 37
    • 0022065627 scopus 로고
    • How Golgi-associated glycosylation works
    • Berger EG 1985 How Golgi-associated glycosylation works. Cell Biol Int Rep 9:407-417
    • (1985) Cell Biol Int Rep , vol.9 , pp. 407-417
    • Berger, E.G.1
  • 38
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille C, Hui N, Hunte F, Kieckbusch R, Berger EG, Warren G, Nilsson T 1995 Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J Cell Sci 108:1617-1627
    • (1995) J Cell Sci , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6    Nilsson, T.7
  • 39
    • 14044256547 scopus 로고    scopus 로고
    • Multiple signals are required for alpha2,6-sialyltransferase (ST6Gal I) oligomerization and Golgi localization
    • Fenteany FH, Colley KJ 2005 Multiple signals are required for alpha2,6-sialyltransferase (ST6Gal I) oligomerization and Golgi localization. J Biol Chem 280:5423-5429
    • (2005) J Biol Chem , vol.280 , pp. 5423-5429
    • Fenteany, F.H.1    Colley, K.J.2
  • 40
    • 0031761360 scopus 로고    scopus 로고
    • Protein maturation in the endoplasmic reticulum
    • Leitzgen K, Haas IG 1998 Protein maturation in the endoplasmic reticulum. Chemtracts-Biochem Mol Biol 11:423-445
    • (1998) Chemtracts-Biochem Mol Biol , vol.11 , pp. 423-445
    • Leitzgen, K.1    Haas, I.G.2
  • 42
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M 2004 Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73:1019-1049
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 43
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M, Helenius A 1999 Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402:90-93
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 45
    • 0036186554 scopus 로고    scopus 로고
    • The importance of trimming reactions on asparagine-linked oligosaccharides for protein quality control
    • Roth J, Zuber C, Guhl B, Fan JY, Ziak M 2002 The importance of trimming reactions on asparagine-linked oligosaccharides for protein quality control. Histochem Cell Biol 117:159-169
    • (2002) Histochem Cell Biol , vol.117 , pp. 159-169
    • Roth, J.1    Zuber, C.2    Guhl, B.3    Fan, J.Y.4    Ziak, M.5
  • 46
    • 0024562263 scopus 로고
    • Chorionic gonadotropin synthesis by human tumor cell lines: Examination of subunit accumulation, steady-state levels of mRNA, and gene structure
    • Cosgrove DE, Campain JA, Cox GS 1989 Chorionic gonadotropin synthesis by human tumor cell lines: examination of subunit accumulation, steady-state levels of mRNA, and gene structure. Biochem Biophys Acta 1007:44-54
    • (1989) Biochem Biophys Acta , vol.1007 , pp. 44-54
    • Cosgrove, D.E.1    Campain, J.A.2    Cox, G.S.3
  • 47
    • 34948877981 scopus 로고    scopus 로고
    • Rapid maturation of glycoprotein hormone free α-subunit (GPHα) and GPHαα homodimers
    • Krause J-M, Berger P, Roig J, Singh V, Merz WE 2007 Rapid maturation of glycoprotein hormone free α-subunit (GPHα) and GPHαα homodimers. Mol Endocrinol 21:2551-2564
    • (2007) Mol Endocrinol , vol.21 , pp. 2551-2564
    • Krause, J.-M.1    Berger, P.2    Roig, J.3    Singh, V.4    Merz, W.E.5
  • 48
    • 0034664730 scopus 로고    scopus 로고
    • The debate about transport in the Golgi-two sides of the same coin?
    • Pelham HR, Rothman JE 2000 The debate about transport in the Golgi-two sides of the same coin? Cell 102:713-719
    • (2000) Cell , vol.102 , pp. 713-719
    • Pelham, H.R.1    Rothman, J.E.2
  • 49
    • 0032838622 scopus 로고    scopus 로고
    • BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
    • Lee YK, Brewer JW, Hellman R, Hendershot LM 1999 BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol Biol Cell 10:2209-2219
    • (1999) Mol Biol Cell , vol.10 , pp. 2209-2219
    • Lee, Y.K.1    Brewer, J.W.2    Hellman, R.3    Hendershot, L.M.4
  • 50
    • 0036124932 scopus 로고    scopus 로고
    • The ISOBM TD-7 Workshop on hCG and related molecules. Towards user-oriented standardization of pregnancy and tumor diagnosis: Assignment of epitopes to the three-dimensional structure of diagnostically and commercially relevant monoclonal antibodies directed against human chorionic gonadotropin and derivatives
    • Berger P, Sturgeon C, Bidart JM, Paus E, Gerth R, Niang M, Bristow A, Birken S, Stenman UH 2002 The ISOBM TD-7 Workshop on hCG and related molecules. Towards user-oriented standardization of pregnancy and tumor diagnosis: assignment of epitopes to the three-dimensional structure of diagnostically and commercially relevant monoclonal antibodies directed against human chorionic gonadotropin and derivatives. Tumour Biol 23:1-38
    • (2002) Tumour Biol , vol.23 , pp. 1-38
    • Berger, P.1    Sturgeon, C.2    Bidart, J.M.3    Paus, E.4    Gerth, R.5    Niang, M.6    Bristow, A.7    Birken, S.8    Stenman, U.H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.