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Volumn 203, Issue 1, 2009, Pages 167-174

The β104-109 sequence is essential for the secretion of correctly folded single-chain βα horse LH/CG and for its FSH activity

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CHORIONIC GONADOTROPIN; FOLLITROPIN; LUTEINIZING HORMONE; RECOMBINANT PROTEIN;

EID: 70349768778     PISSN: 00220795     EISSN: 14796805     Source Type: Journal    
DOI: 10.1677/JOE-09-0141     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0347916881 scopus 로고    scopus 로고
    • Comparative Genomic Analysis of the Eight-Membered Ring Cystine Knot-Containing Bone Morphogenetic Protein Antagonists
    • DOI 10.1210/me.2003-0227
    • Avsian-Kretchmer O & Hsueh AJ 2004 Comparative genomic analysis of the eight-membered ring cystine knot-containing bone morphogenetic protein antagonists. Molecular Endocrinology 18 1-12. (Pubitemid 38073149)
    • (2004) Molecular Endocrinology , vol.18 , Issue.1 , pp. 1-12
    • Avsian-Kretchmer, O.1    Hsueh, A.J.W.2
  • 2
    • 33244486752 scopus 로고    scopus 로고
    • Nitro-thiocyanobenzoic acid (NTCB) reactivity of cysteines β100 and β110 in porcine luteinizing hormone: Metastability and hypothetical isomerization of the two disulfide bridges of its β-subunit seatbelt
    • DOI 10.1016/j.mce.2006.01.001, PII S0303720706000050
    • Belghazi M, Klett D, Cahoreau C & Combarnous Y 2006 Nitrothiocyanobenzoic acid (NTCB) reactivity of cysteines β100 and β110 in porcine luteinizing hormone: metastability and hypothetical isomerization of the two disulfide bridges of its β-subunit seatbelt. Molecular and Cellular Endocrinology 247 175-182. (Pubitemid 43277721)
    • (2006) Molecular and Cellular Endocrinology , vol.247 , Issue.1-2 , pp. 175-182
    • Belghazi, M.1    Klett, D.2    Cahoreau, C.3    Combarnous, Y.4
  • 3
    • 0034746808 scopus 로고    scopus 로고
    • Identification of twelve O-glycosylation sites in equine chorionic gonadotropin beta and equine luteinizing hormone ss by solid-phase Edman degradation
    • Bousfield GR & Butnev VY 2001 Identification of twelve O-glycosylation sites in equine chorionic gonadotropin beta and equine luteinizing hormone ss by solid-phase Edman degradation. Biology of Reproduction 64 136-147.
    • (2001) Biology of Reproduction , vol.64 , pp. 136-147
    • Bousfield, G.R.1    Butnev, V.Y.2
  • 4
    • 0027312248 scopus 로고
    • Topography of equine chorionic gonadotropin epitopes relative to the luteinizing hormone and follicle-stimulating hormone receptor interaction sites
    • DOI 10.1016/0303-7207(93)90013-A
    • Chopineau M, Maurel MC, Combarnous Y & Durand P 1993 Topography of equine chorionic gonadotropin epitopes relative to the luteinizing hormone and follicle-stimulating hormone receptor interaction sites. Molecular and Cellular Endocrinology 92 229-239. (Pubitemid 23124988)
    • (1993) Molecular and Cellular Endocrinology , vol.92 , Issue.2 , pp. 229-239
    • Chopineau, M.1    Maurel, M.-C.2    Combarnous, Y.3    Durand, P.4
  • 5
    • 0029121505 scopus 로고
    • Cloning and analysis of the cDNA encoding the horse and donkey luteinizing hormone β-subunits
    • Chopineau M, Stewart F & Allen WR 1995 Cloning and analysis of the cDNA encoding the horse and donkey luteinizing hormone β-subunits. Gene 160 253-256.
    • (1995) Gene , vol.160 , pp. 253-256
    • Chopineau, M.1    Stewart, F.2    Allen, W.R.3
  • 7
    • 0035072738 scopus 로고    scopus 로고
    • β-Subunit 102-104 residues are crucial to confer FSH activity to equine LH/CG but are not sufficient to confer FSH activity to human CG
    • DOI 10.1677/joe.0.1690055
    • Chopineau M, Martinat N, Galet C, Guillou F & Combarnous Y 2001 β-Subunit 102-104 residues are crucial to confer FSH activity to equine LH/CG but are not sufficient to confer FSH activity to human CG. Journal of Endocrinology 169 55-63. (Pubitemid 32273214)
    • (2001) Journal of Endocrinology , vol.169 , Issue.1 , pp. 55-63
    • Chopineau, M.1    Martinat, N.2    Galet, C.3    Guillou, F.4    Combarnous, Y.5
  • 8
    • 0026440307 scopus 로고
    • Molecular basis of the specificity of binding of glycoprotein hormones to their receptors
    • DOI 10.1210/er.13.4.670
    • Combarnous Y 1992 Molecular basis of the specificity of binding of glycoprotein hormones to their receptor. Endocrine Reviews 13 670-691. (Pubitemid 23037210)
    • (1992) Endocrine Reviews , vol.13 , Issue.4 , pp. 670-691
    • Combarnous, Y.1
  • 9
    • 0027999473 scopus 로고
    • Receptor binding and functional properties of chimeric human follitropin prepared by an exchange between a small hydrophilic intercysteine loop of human follitropin and human lutropin
    • Dias JA, Zhang Y & Liu X 1994 Receptor binding and functional properties of chimeric human follitropin prepared by an exchange between a small hydrophilic intercysteine loop of human follitropin and human lutropin. Journal of Biological Chemistry 269 25289-25294. (Pubitemid 24336206)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.41 , pp. 25289-25294
    • Dias, J.A.1    Zhang, Y.2    Liu, X.3
  • 10
    • 0026551294 scopus 로고
    • Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin β subunit to the follitropin β subunit
    • Fares FA, Suganuma N, Nishimori K, LaPolt PS, Hsueh AJ & Boime I 1992 Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin β subunit to the follitropin β subunit. PNAS 89 4304-4308.
    • (1992) PNAS , vol.89 , pp. 4304-4308
    • Fares, F.A.1    Suganuma, N.2    Nishimori, K.3    LaPolt, P.S.4    Hsueh, A.J.5    Boime, I.6
  • 11
    • 0031788050 scopus 로고    scopus 로고
    • Conversion of thyrotropin heterodimer to a biologically active single- Chain
    • Fares FA, Yamabe S, Ben-Menahem D, Pixley M, Hsueh AJW & Boime I 1998 Conversion of thyrotropin heterodimer to a biologically active single-chain. Endocrinology 139 2459-2464. (Pubitemid 28513772)
    • (1998) Endocrinology , vol.139 , Issue.5 , pp. 2459-2464
    • Fares, F.A.1    Yamabe, S.2    Ben-Menahem, D.3    Pixley, M.4    Hsueh, A.J.W.5    Boime, I.6
  • 12
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • DOI 10.1210/me.15.3.378
    • Fox KM, Dias J & Van Roey P 2001 Three-dimensional structure of human follicle-stimulating hormone. Molecular Endocrinology 15 378-389. (Pubitemid 32221915)
    • (2001) Molecular Endocrinology , vol.15 , Issue.3 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 13
    • 0033782752 scopus 로고    scopus 로고
    • Expression of an in vitro biologically active equine LH/CG without C-terminal peptide (CTP) and/or β26-110 disulphide bridge
    • Galet C, Chopineau M, Martinat N, Combarnous Y & Guillou F 2000 Expression of an in vitro biologically active equine LH/CG without C-terminal peptide (CTP) and/or β26-110 disulphide bridge. Journal of Endocrinology 167 117-124. (Pubitemid 30781891)
    • (2000) Journal of Endocrinology , vol.167 , Issue.1 , pp. 117-124
    • Galet, C.1    Chopineau, M.2    Martinat, N.3    Combarnous, Y.4    Guillou, F.5
  • 15
    • 0030969880 scopus 로고    scopus 로고
    • Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) β-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH
    • DOI 10.1074/jbc.272.24.15532
    • Grossmann M, Szkudlinski MW, Wong R, Dias JA, Ji TH & Weintraub BD 1997 Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) β-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH. Journal of Biological Chemistry 272 15532-15540. (Pubitemid 27255583)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.24 , pp. 15532-15540
    • Grossmann, M.1    Szkudlinski, M.W.2    Wong, R.3    Dias, J.A.4    Ji, T.H.5    Weintraub, B.D.6
  • 16
    • 0020696389 scopus 로고
    • Purification of equine gonadotropins and comparative study of their acid-dissociation and receptor-binding specificity
    • Guillou F & Combarnous Y 1983 Purification of equine gonadotropins and comparative study of their acid-dissociation and receptor binding specificity. Biochimica et Biophysica Acta 755 229-236. (Pubitemid 13153879)
    • (1983) Biochimica et Biophysica Acta , vol.755 , Issue.2 , pp. 229-236
    • Guillou, F.1    Combarnous, Y.2
  • 17
    • 0030606149 scopus 로고    scopus 로고
    • HCGβ Residues 94-96 alter LH activity without appearing to make key receptor contacts
    • DOI 10.1016/S0303-7207(96)03936-6, PII S0303720796039366
    • Han Y, Bernard MP & Moyle WR 1996 hCGβ residues 94-96 alter LH activity without appearing to make key receptor contacts. Molecular and Cellular Endocrinology 124 151-161. (Pubitemid 27042074)
    • (1996) Molecular and Cellular Endocrinology , vol.124 , Issue.1-2 , pp. 151-161
    • Han, Y.1    Bernard, M.P.2    Moyle, W.R.3
  • 19
    • 0027102058 scopus 로고
    • Enzyme immunoassay (EIA) for equine chorionic gonadotropin/pregnant mare serum gonadotropin (eCG/PMSG)
    • Lecompte F & Combarnous Y 1992 Enzyme immunoassay (EIA) for equine chorionic gonadotropin/pregnant mare serum gonadotropin (eCG/PMSG). Journal of Immunoassay 13 483-493. (Pubitemid 23035248)
    • (1992) Journal of Immunoassay , vol.13 , Issue.4 , pp. 483-493
    • Lecompte, F.1    Combarnous, Y.2
  • 20
    • 0024454312 scopus 로고
    • Mutagenesis and chimeric genes define determinants in the β subunits of human chorionic gonadotropin and lutropin for secretion and assembly
    • Matzuk MM, Splanger MM, Camel M, Suganuma N & Boime I 1989 Mutagenesis and chimeric genes define determinants in the β subunits of human chorionic gonadotropin and lutropin for secretion and assembly. Journal of Cell Biology 109 1429-1438. (Pubitemid 19251201)
    • (1989) Journal of Cell Biology , vol.109 , Issue.4 I , pp. 1429-1438
    • Matzuk, M.M.1    Spangler, M.M.2    Camel, M.3    Suganuma, N.4    Boime, I.5
  • 21
    • 0025020754 scopus 로고
    • The biological role of the carboxyl-terminal extension of human chorionic gonadotroin β-subunit
    • Matzuk MM, Hsueh AJW, Lapolt P, Tsafriri A, Keene JL & Boime I 1990 The biological role of the carboxyl-terminal extension of human chorionic gonadotropin β-subunit. Endocrinology 126 376-383. (Pubitemid 20037166)
    • (1990) Endocrinology , vol.126 , Issue.1 , pp. 376-383
    • Matzuk, M.M.1    Hsueh, A.J.W.2    Lapolt, P.3    Tsafriri, A.4    Keene, J.L.5    Boime, I.6
  • 23
    • 0032230253 scopus 로고    scopus 로고
    • The carboxyl-terminal region is a determinant for the intracellular behavior of the chorionic gonadotropin β subunit: Effects on the processing of the Asn-linked oligosaccharides
    • Muyan M & Boime I 1998 The carboxyl-terminal region is a determinant for the intracellular behavior of the chorionic gonadotropin β subunit: effects on the processing of the Asn-linked oligosaccharides. Molecular Endocrinology 12 766-772. (Pubitemid 30659077)
    • (1998) Molecular Endocrinology , vol.12 , Issue.5 , pp. 766-772
    • Muyan, M.1    Boime, I.2
  • 24
    • 0029859757 scopus 로고    scopus 로고
    • The carboxy-terminal region of the β-subunits of luteinizing hormone and chorionic gonadotropin differentially influence secretion and assembly of the heterodimers
    • DOI 10.1210/me.10.12.1678
    • Muyan M, Furuhashi M, Sugahara T & Boime I 1996 The carboxy-terminal region of the β-subunits of luteinizing hormone and chorionic gonadotropin differentially influence secretion and assembly of the heterodimer. Molecular Endocrinology 10 1678-1687. (Pubitemid 26408755)
    • (1996) Molecular Endocrinology , vol.10 , Issue.12 , pp. 1678-1687
    • Muyan, M.1    Furuhashi, M.2    Sugahara, T.3    Boime, I.4
  • 27
    • 0019985826 scopus 로고
    • Establishment of gonadotropin-responsive murine leydig tumor cell line
    • Rebois RV 1982 Establishment of gonadotropin-responsive murine leydig tumor cell line. Journal of Cell Biology 94 70-76.
    • (1982) Journal of Cell Biology , vol.94 , pp. 70-76
    • Rebois, R.V.1
  • 28
    • 0000932676 scopus 로고
    • Changes in milk and plasma concentrations of progesterone in cows after treatrment to induce superovulation and their relationships with number of ovulations and of embryos collected
    • Saumande J, Tamboura D & Chupin D 1985 Changes in milk and plasma concentrations of progesterone in cows after treatrment to induce superovulation and their relationships with number of ovulations and of embryos collected. Theriogenology 23 719-731.
    • (1985) Theriogenology , vol.23 , pp. 719-731
    • Saumande, J.1    Tamboura, D.2    Chupin, D.3
  • 30
    • 0017622511 scopus 로고
    • Influence of fetal genotype on the follicle stimulating hormone: Luteinizing hormone ratio of pregnant mare serum gonadotrophin
    • Stewart F, Allen WR & Moor RM 1977 Influence of fetal genotype on the follicle-stimulating hormone: luteinizing hormone ratio of pregnant mare serum gonadotropin. Journal of Endocrinology 73 419-425. (Pubitemid 8118842)
    • (1977) Journal of Endocrinology , vol.73 , Issue.3 , pp. 419-425
    • Stewart, F.1    Allen, W.R.2    Moor, R.M.3
  • 31
    • 0030596069 scopus 로고    scopus 로고
    • Expression of biologically active fusion genes encoding the common or subunit and either the CGβ or FSHβ subunits: Role of a linker sequence
    • DOI 10.1016/S0303-7207(96)03944-5, PII S0303720796039445
    • Sugahara T, Grootenhuis PD, Sato A, Kudo M, Ben-Menahem D, Pixley MR, Hsueh AJ & Boime I 1996 Expression of biologically active fusion genes encoding the common α subunit and either the CGβ or FSHβ subunits: rôle of a linker sequence. Molecular and Cellular Endocrinology 125 71-77. (Pubitemid 27037786)
    • (1996) Molecular and Cellular Endocrinology , vol.125 , Issue.1-2 , pp. 71-77
    • Sugahara, T.1    Grootenhuis, P.D.J.2    Sato, A.3    Kudo, M.4    Ben-Menahem, D.5    Pixley, M.R.6    Hsueh, A.J.W.7    Boime, I.8
  • 32
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotrophin at 2.6A resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE & HendricksonWA 1994 Structure of human chorionic gonadotrophin at 2.6A 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
  • 33
    • 4143090403 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive β-subunit disulfide switch
    • DOI 10.1074/jbc.M403053200
    • Xing Y, Myers RV, 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 β-subunit disulfide switch. Journal of Biological Chemistry 279 35437-35448. (Pubitemid 39100543)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.