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Volumn 125, Issue 1-2, 1996, Pages 3-19

Structural features of mammalian gonadotropins

Author keywords

Equine; Gonadotropins; Hybrid hormone; Oligosaccharide; Receptor

Indexed keywords

ASPARAGINE; ASPARAGINE LINKED OLIGOSACCHARIDE; ASPARTIC ACID; CHORIONIC GONADOTROPIN BETA SUBUNIT; FOLLITROPIN; FOLLITROPIN RECEPTOR; GONADOTROPIN; LUTEINIZING HORMONE; LUTEINIZING HORMONE RECEPTOR;

EID: 0030596155     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(96)03945-7     Document Type: Conference Paper
Times cited : (97)

References (44)
  • 1
    • 0000676471 scopus 로고
    • Gonadotropins: Chemistry and biosynthesis
    • (Knobil, E., Neill, J.D. eds.), Raven Press, New York
    • [1] Bousfield, G.R., Perry, W.M. and Ward, D.N. (1994) Gonadotropins: chemistry and biosynthesis. In: The Physiology of Reproduction (Knobil, E., Neill, J.D. eds.), pp. 1749-1792, Raven Press, New York.
    • (1994) The Physiology of Reproduction , pp. 1749-1792
    • Bousfield, G.R.1    Perry, W.M.2    Ward, D.N.3
  • 2
    • 0003332222 scopus 로고    scopus 로고
    • Gonadotropins
    • (Adashi, E.Y., Rock, J.A., Rosenwaks, Z. eds.), Lippincott Raven, Hagerstown
    • [2] Moyle, W.R. and Campbell, R.K. (1996) Gonadotropins. In: Reproductive Endocrinology, Surgery, and Technology (Adashi, E.Y., Rock, J.A., Rosenwaks, Z. eds.), pp. 683-724, Lippincott Raven, Hagerstown.
    • (1996) Reproductive Endocrinology, Surgery, and Technology , pp. 683-724
    • Moyle, W.R.1    Campbell, R.K.2
  • 3
    • 0020714623 scopus 로고
    • Difference in sizes of human compared to murine α-subunits of the glycoprotein hormones arises by a four-codon gene deletion or insertion
    • [3] Chin, W.W., Maizel, J.V. Jr. and Habener, J.F. (1983) Difference in sizes of human compared to murine α-subunits of the glycoprotein hormones arises by a four-codon gene deletion or insertion. Endocrinology 112, 482-485.
    • (1983) Endocrinology , vol.112 , pp. 482-485
    • Chin, W.W.1    Maizel J.V., Jr.2    Habener, J.F.3
  • 4
    • 0023664547 scopus 로고
    • Structural studies on equine glycoprotein hormones: Amino acid sequence of equine lutropin β-subunit
    • [4] Bousfield, G.R., Liu, W.-K., Sugino, H. and Ward, D.N. (1987) Structural studies on equine glycoprotein hormones: amino acid sequence of equine lutropin β-subunit. J. Biol. Chem. 262, 8610-8620.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8610-8620
    • Bousfield, G.R.1    Liu, W.-K.2    Sugino, H.3    Ward, D.N.4
  • 6
    • 0020888557 scopus 로고
    • The human genome contains seven genes for the β-subunit of chorionic gonadotropin but only one gene for the β-subunit of luteinizing hormone
    • [6] Talmadge, K. Boorstein, W.R. and Fiddes, J.C. (1983) The human genome contains seven genes for the β-subunit of chorionic gonadotropin but only one gene for the β-subunit of luteinizing hormone. DNA Cell Biol. 2, 281-289.
    • (1983) DNA Cell Biol. , vol.2 , pp. 281-289
    • Talmadge, K.1    Boorstein, W.R.2    Fiddes, J.C.3
  • 7
    • 0023930204 scopus 로고
    • Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin II. Distributions of sulphated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones
    • [7] Green, E.D. and Baenziger, J.U. (1988) Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin II. distributions of sulphated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones. J. Biol. Chem. 263, 36-44.
    • (1988) J. Biol. Chem. , vol.263 , pp. 36-44
    • Green, E.D.1    Baenziger, J.U.2
  • 8
    • 0021690978 scopus 로고
    • Comparison of in vitro follicle-stimulating hormone (FSH) activity of equine gonadotropins (luteinizing hormone, FSH and chorionic gonadotropin) in male and female rats
    • [8] Combarnous, Y., Guillou, F. and Martinat, N. (1984) Comparison of in vitro follicle-stimulating hormone (FSH) activity of equine gonadotropins (luteinizing hormone, FSH and chorionic gonadotropin) in male and female rats. Endocrinology 115, 1821-1827.
    • (1984) Endocrinology , vol.115 , pp. 1821-1827
    • Combarnous, Y.1    Guillou, F.2    Martinat, N.3
  • 9
    • 0024362258 scopus 로고
    • Comparative binding of FSH to chicken and rat testis
    • [9] Gordon, W.L., Bousfield, G.R. and Ward, D.N. (1989) Comparative binding of FSH to chicken and rat testis. J. Endocrinol. Invest. 12, 383-392.
    • (1989) J. Endocrinol. Invest. , vol.12 , pp. 383-392
    • Gordon, W.L.1    Bousfield, G.R.2    Ward, D.N.3
  • 10
    • 0029931343 scopus 로고    scopus 로고
    • Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin on its luteinizing hormone and follicle-stimulating hormone receptor-binding activities
    • [10] Butnev, V.Y., Gotschall, R.R., Baker, V.L., Moore, W.T. and Bousfield, G.R. (1996) Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin on its luteinizing hormone and follicle-stimulating hormone receptor-binding activities. Endocrinology 137, 2530-2542.
    • (1996) Endocrinology , vol.137 , pp. 2530-2542
    • Butnev, V.Y.1    Gotschall, R.R.2    Baker, V.L.3    Moore, W.T.4    Bousfield, G.R.5
  • 12
    • 0025355741 scopus 로고
    • Structure determination of the major N- and O-linked carbohydrate chains of the β-subunit from equine chorionic gonadotropin
    • [12] Damm, J.B.L., Hard, K., Kammerling, J.P., van Dedem, G.W.K. and Vliegenthart, F.G. (1990) Structure determination of the major N- and O-linked carbohydrate chains of the β-subunit from equine chorionic gonadotropin. Eur. J. Biochem. 189, 175-183.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 175-183
    • Damm, J.B.L.1    Hard, K.2    Kammerling, J.P.3    Van Dedem, G.W.K.4    Vliegenthart, F.G.5
  • 13
    • 0027939019 scopus 로고
    • Structural analysis of N-linked oligosaccharides from equine chorionic gonadotropin and lutropin β-subunits
    • [13] Matsui, T., Mizouchi, T., Titani, K., Okinaga, T., Hoshi, M., Bousfield, G.R., Sugino, H. and Ward, D.N. (1994) Structural analysis of N-linked oligosaccharides from equine chorionic gonadotropin and lutropin β-subunits. Biochemistry 33, 14039-14048.
    • (1994) Biochemistry , vol.33 , pp. 14039-14048
    • Matsui, T.1    Mizouchi, T.2    Titani, K.3    Okinaga, T.4    Hoshi, M.5    Bousfield, G.R.6    Sugino, H.7    Ward, D.N.8
  • 15
    • 0028262323 scopus 로고
    • Structure determination of the disalylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin
    • [15] Hokke, C.H., Roosenboom, M.J.H., Thomas-Oates, J.E., Kamerling, J.P. and Vliegenthart, J.F.G. (1994) Structure determination of the disalylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin. Glycoconjugate J. 11, 35-41.
    • (1994) Glycoconjugate J. , vol.11 , pp. 35-41
    • Hokke, C.H.1    Roosenboom, M.J.H.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Vliegenthart, J.F.G.5
  • 16
    • 0017723084 scopus 로고
    • Isolation and amino acid sequence of COOH-terminal fragments from the β-subunit of human choriogonadotropin
    • [16] Birken, S. and Canfield, R.E. (1977) Isolation and amino acid sequence of COOH-terminal fragments from the β-subunit of human choriogonadotropin. J. Biol. Chem. 252, 5386-5392.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5386-5392
    • Birken, S.1    Canfield, R.E.2
  • 17
    • 0017654112 scopus 로고
    • Human chorionic gonadotropin: Amino acid sequence of the hormone-specific COOH-terminal region
    • [17] Keutmann, H.T. and Williams, R.M. (1977) Human chorionic gonadotropin: amino acid sequence of the hormone-specific COOH-terminal region. J. Biol. Chem. 252, 5393-5397.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5393-5397
    • Keutmann, H.T.1    Williams, R.M.2
  • 18
    • 0018675127 scopus 로고
    • Structure and location of the O-glycosidic carbohydrate units of human chorionic gonadotropin
    • [18] Kessler, M.J., Mise, T., Ghai, R.D. and Bahl, O.P. (1979) Structure and location of the O-glycosidic carbohydrate units of human chorionic gonadotropin. J. Biol. Chem. 254, 7909-7914.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7909-7914
    • Kessler, M.J.1    Mise, T.2    Ghai, R.D.3    Bahl, O.P.4
  • 19
    • 0026051641 scopus 로고
    • Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: The detection of Xaa-Pro-Xaa-Xaa as a motif for Thr O-glycosylation
    • [19] Gooley, A.A., Classon, B.J., Marschalek, R. and Williams, K.L. (1991) Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: the detection of Xaa-Pro-Xaa-Xaa as a motif for Thr O-glycosylation. Biochem. Biophys. Res. Commun. 178, 1194-1201.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1194-1201
    • Gooley, A.A.1    Classon, B.J.2    Marschalek, R.3    Williams, K.L.4
  • 20
    • 0023664623 scopus 로고
    • Structural studies on equine gonadotropins: Amino acid sequence of equine chorionic gonadotropin β-subunit
    • [20] Sugino, H., Bousfield, G.R., Moore, W.T. Jr. and Ward, D.N. (1987) Structural studies on equine gonadotropins: amino acid sequence of equine chorionic gonadotropin β-subunit. J. Biol. Chem. 262, 8603-8609.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8603-8609
    • Sugino, H.1    Bousfield, G.R.2    Moore W.T., Jr.3    Ward, D.N.4
  • 21
    • 0024498370 scopus 로고
    • Effects of removal of carboxy-terminal extension from equine luteinizing hormone (LH) β-subunit on LH and follicle-stimulating hormone receptor binding activities and LH steroidogenic activity in rat testicular leydig cells
    • [21] Bousfield, G.R., Liu, W.-K. and Ward, D.N. (1989) Effects of removal of carboxy-terminal extension from equine luteinizing hormone (LH) β-subunit on LH and follicle-stimulating hormone receptor binding activities and LH steroidogenic activity in rat testicular leydig cells. Endocrinology 124, 379-387.
    • (1989) Endocrinology , vol.124 , pp. 379-387
    • Bousfield, G.R.1    Liu, W.-K.2    Ward, D.N.3
  • 22
    • 0024438106 scopus 로고
    • Site-directed mutagenesis of the human chorionic gonadotropin β-subunit: Bioactivity of a heterologous hormone, bovine α-human des-(122-145)β
    • [22] El-Deiry, S., Kaetzel, D., Kennedy, G., Nilson J. and Puett, D. (1989) Site-directed mutagenesis of the human chorionic gonadotropin β-subunit: bioactivity of a heterologous hormone, bovine α-human des-(122-145)β. Mol. Endocrinol. 3, 1523-1528.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1523-1528
    • El-Deiry, S.1    Kaetzel, D.2    Kennedy, G.3    Nilson, J.4    Puett, D.5
  • 23
    • 0025020754 scopus 로고
    • The biological role of the carboxyl-terminal extension of human chorionic gonadotropin β-subunit
    • [23] Matzuk, M.M., Hsueh, A.J.W., Lapolt, P., Tsafriri, A., Keene, J.L. and Boime, I. (1990) The biological role of the carboxyl-terminal extension of human chorionic gonadotropin β-subunit. Endocrinology 126, 376-383.
    • (1990) Endocrinology , vol.126 , 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
  • 24
    • 0022258720 scopus 로고
    • A role for glycosylation of the α-subunit in transduction of biological signal in glycoprotein hormones
    • [24] Sairam, M.R. and Bhargavi, G.N. (1985) A role for glycosylation of the α-subunit in transduction of biological signal in glycoprotein hormones. Science 229, 65-67.
    • (1985) Science , vol.229 , pp. 65-67
    • Sairam, M.R.1    Bhargavi, G.N.2
  • 25
    • 0024340857 scopus 로고
    • Role of carbohydrates in glycoprotein hormone signal transduction
    • [25] Sairam, M.R. (1989) Role of carbohydrates in glycoprotein hormone signal transduction. FASEB J. 3, 1915-1926.
    • (1989) FASEB J. , vol.3 , pp. 1915-1926
    • Sairam, M.R.1
  • 27
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • [27] Wu, H., Lustbader, J.W., Liu, Y., Canfield, R.E. and Hendrickson, W.A. (1994) Structure of human chorionic gonadotropin at 2.6 Å 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
  • 28
    • 0025689177 scopus 로고
    • N-linked oligosaccharides on free α interfere with its ability to combine with human chorionic gonadotropin-β-subunit
    • [28] Blithe, D.L. (1990) N-linked oligosaccharides on free α interfere with its ability to combine with human chorionic gonadotropin-β-subunit. J. Biol. Chem. 265, 21951-21956.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21951-21956
    • Blithe, D.L.1
  • 29
    • 0028855750 scopus 로고
    • The role of glycosylation in regulating the glycoprotein hormone free α-subunit and free β-subunit combination in the extraembryonic coelomic fluid of early pregnancy
    • [29] Blithe, D.L. and Iles, R.K. (1995) The role of glycosylation in regulating the glycoprotein hormone free α-subunit and free β-subunit combination in the extraembryonic coelomic fluid of early pregnancy. Endocrinology 136, 903-910.
    • (1995) Endocrinology , vol.136 , pp. 903-910
    • Blithe, D.L.1    Iles, R.K.2
  • 30
    • 0023808074 scopus 로고
    • Differential susceptibility to N-Glycanase at the individual glycosylation sites of mouse thyrotropin and free α-subunits
    • [30] Miura, Y., Perkel, V.S. and Magner, J.A. (1988) Differential susceptibility to N-Glycanase at the individual glycosylation sites of mouse thyrotropin and free α-subunits. Endocrinology 123, 2207-2213.
    • (1988) Endocrinology , vol.123 , pp. 2207-2213
    • Miura, Y.1    Perkel, V.S.2    Magner, J.A.3
  • 31
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • [31] Matzuk, M.M., Keene, J.L. and 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
  • 33
    • 0028861254 scopus 로고
    • Asparagine-linked oligosaccharides facilitate human chorionic gonadotropin β-subunit folding but not assembly of prefolded β with α
    • [33] Feng, W., Huth, J.R., Norton, S.E. and Ruddon, R.W. (1995) Asparagine-linked oligosaccharides facilitate human chorionic gonadotropin β-subunit folding but not assembly of prefolded β with α. Endocrinology 136, 52-61.
    • (1995) Endocrinology , vol.136 , pp. 52-61
    • Feng, W.1    Huth, J.R.2    Norton, S.E.3    Ruddon, R.W.4
  • 34
    • 0024851291 scopus 로고
    • Separation of oligosaccharides using high-performance anion-exchange chromatography with pulsed amperometric detection
    • [34] Townsend, R.R., Hardy, M. and Lee, Y.C. (1989) Separation of oligosaccharides using high-performance anion-exchange chromatography with pulsed amperometric detection. Methods Enzymol. 179, 65-82.
    • (1989) Methods Enzymol. , vol.179 , pp. 65-82
    • Townsend, R.R.1    Hardy, M.2    Lee, Y.C.3
  • 35
    • 0029015130 scopus 로고
    • Separation of asparagine-linked oligosaccharides by high-pH anion-exchange chromatography with pulsed amperometric detection: Empirical relationships between oligosaccharide structure on chromatographic retention
    • [35] Rohrer, J.S. (1995) Separation of asparagine-linked oligosaccharides by high-pH anion-exchange chromatography with pulsed amperometric detection: empirical relationships between oligosaccharide structure on chromatographic retention. Glycobiology 5, 359-360.
    • (1995) Glycobiology , vol.5 , pp. 359-360
    • Rohrer, J.S.1
  • 36
    • 0024991081 scopus 로고
    • Site-specific N-glycosylation of ovine lutropin: Structural analysis by one- and two-dimensional 1H-NMR spectroscopy
    • [36] Weisshaar, G. Hiyama, J. and Renwick, A.G.C. (1990) Site-specific N-glycosylation of ovine lutropin: structural analysis by one- and two-dimensional 1H-NMR spectroscopy. Eur. J. Biochem. 192, 741-751.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 741-751
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 37
    • 0025992391 scopus 로고
    • Site-specific N-glycosylation of human chorionic gonadotropin-structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy
    • [37] Weisshaar, G., Hiyama, J. and Renwick, A.G.C. (1991) Site-specific N-glycosylation of human chorionic gonadotropin-structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy. Glycobiology 1, 393-404.
    • (1991) Glycobiology , vol.1 , pp. 393-404
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 38
    • 0017727845 scopus 로고
    • Isolation and recombination of ovine lutropin subunits with complete recovery of biological activity
    • [38] Ascoli, M., Liu, W.-K. and Ward, D.N. (1977) Isolation and recombination of ovine lutropin subunits with complete recovery of biological activity. J. Biol. Chem. 252, 5280-5286.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5280-5286
    • Ascoli, M.1    Liu, W.-K.2    Ward, D.N.3
  • 39
    • 0021928573 scopus 로고
    • Hybrids from equine LH: Alpha enhances, beta diminishes activity
    • [39] Bousfield, G.R., Liu, W.-K. and Ward, D.N. (1985) Hybrids from equine LH: alpha enhances, beta diminishes activity. Mol. Cell. Endocrinol. 40, 69-77.
    • (1985) Mol. Cell. Endocrinol. , vol.40 , pp. 69-77
    • Bousfield, G.R.1    Liu, W.-K.2    Ward, D.N.3
  • 41
    • 0001915062 scopus 로고
    • Chemistry of the peptide components of glycoprotein hormones
    • (Keel, B.A., Grotjan, H.E. Jr., ed.), CRC Press, Boca Raton
    • [41] Ward, D.N., Bousfield, G.R., Gordon, W.L. and Sugino, H. (1989) Chemistry of the peptide components of glycoprotein hormones. In: Microheterogeneity of Glycoprotein Hormones (Keel, B.A., Grotjan, H.E. Jr., ed.), pp. 1-21, CRC Press, Boca Raton.
    • (1989) Microheterogeneity of Glycoprotein Hormones , pp. 1-21
    • Ward, D.N.1    Bousfield, G.R.2    Gordon, W.L.3    Sugino, H.4
  • 42
    • 0027998433 scopus 로고
    • Evidence for two folding domains in glycoprotein hormone α-subunits
    • [42] Bousfield, G.R. and Ward, D.N. (1994) Evidence for two folding domains in glycoprotein hormone α-subunits. Endocrinology 135, 624-635.
    • (1994) Endocrinology , vol.135 , pp. 624-635
    • Bousfield, G.R.1    Ward, D.N.2


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