메뉴 건너뛰기




Volumn 119, Issue 5, 1996, Pages 953-960

Unique recognition of activin and inhibin by polyclonal antibodies to inhibin subunits

Author keywords

Activin; Follistatin; Inhibin; Polyclonal antibodies; Recognition

Indexed keywords

ACTIVIN; FOLLISTATIN; GLYCOSIDASE; INHIBIN; POLYCLONAL ANTIBODY; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

EID: 0029984011     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021335     Document Type: Article
Times cited : (8)

References (53)
  • 1
    • 0006000627 scopus 로고
    • Isolation and partial characterization of a Mw 32,000 protein with inhibin activity from porcine follicular fluid
    • Ling, N., Ying, S.-Y., Ueno, N., Esch, F., Denoray, L., and Guillemin, R. (1985) Isolation and partial characterization of a Mw 32,000 protein with inhibin activity from porcine follicular fluid. Proc. Natl. Acad. Sci. USA 82, 7217-7221
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7217-7221
    • Ling, N.1    Ying, S.-Y.2    Ueno, N.3    Esch, F.4    Denoray, L.5    Guillemin, R.6
  • 5
    • 0022470831 scopus 로고
    • Pituitary FSH is released by a heterodimer of the beta-subunits from the two forms of inhibin
    • Ling, N., Ying, S.-Y., Ueno, N., Shimasaki, S., Esch, F., Hotta, M., and Guillemin, R. (1986) Pituitary FSH is released by a heterodimer of the beta-subunits from the two forms of inhibin. Nature 321, 779-782
    • (1986) Nature , vol.321 , pp. 779-782
    • Ling, N.1    Ying, S.-Y.2    Ueno, N.3    Shimasaki, S.4    Esch, F.5    Hotta, M.6    Guillemin, R.7
  • 6
    • 0022907945 scopus 로고
    • Purification and characterization of an FSH-releasing protein from ovarian follicular fluid
    • Vale, W., Rivier, J., Vaughan, J., McClintock, R., Corrigan, A., Woo, W., Karr, D., and Spiess, J. (1986) Purification and characterization of an FSH-releasing protein from ovarian follicular fluid. Nature 321, 776-779
    • (1986) Nature , vol.321 , pp. 776-779
    • Vale, W.1    Rivier, J.2    Vaughan, J.3    McClintock, R.4    Corrigan, A.5    Woo, W.6    Karr, D.7    Spiess, J.8
  • 8
    • 0024004112 scopus 로고
    • Inhibins, activins, and follistatins: Gonadal proteins modulating the secretion of follicle-stimulating hormone
    • Ying, S.-Y. (1988) Inhibins, activins, and follistatins: Gonadal proteins modulating the secretion of follicle-stimulating hormone. Endocr. Rev. 9, 267-293
    • (1988) Endocr. Rev. , vol.9 , pp. 267-293
    • Ying, S.-Y.1
  • 10
    • 0029003329 scopus 로고
    • Molecular cloning and functional analysis of a new activin β subunit: A dorsal mesoderm-inducing activity in Xenopus
    • Oda, S., Nishimatsu, S., Murakami, K., and Ueno, N. (1995) Molecular cloning and functional analysis of a new activin β subunit: A dorsal mesoderm-inducing activity in Xenopus. Biochem. Biophys. Res. Commun. 210, 581-588
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 581-588
    • Oda, S.1    Nishimatsu, S.2    Murakami, K.3    Ueno, N.4
  • 11
  • 12
    • 0023106040 scopus 로고
    • Purification and characterization of erythroid differentiation factor (EDF) isolated from human leukemia cell line THP-1
    • Eto, Y., Tsuji, T., Takezawa, M., Takano, S., Yokogawa, Y., and Shibai, H. (1987) Purification and characterization of erythroid differentiation factor (EDF) isolated from human leukemia cell line THP-1. Biochem. Biophys. Res. Commun. 142, 1095-1103
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 1095-1103
    • Eto, Y.1    Tsuji, T.2    Takezawa, M.3    Takano, S.4    Yokogawa, Y.5    Shibai, H.6
  • 13
    • 0025324104 scopus 로고
    • Identification of a potent Xenopus mesoderm-inducing factor as an activin A homologue
    • Smith, J.C., Price, B.M., Van Nimmen, K.V., and Huylebroeck, D. (1990) Identification of a potent Xenopus mesoderm-inducing factor as an activin A homologue. Nature 345, 729-731
    • (1990) Nature , vol.345 , pp. 729-731
    • Smith, J.C.1    Price, B.M.2    Van Nimmen, K.V.3    Huylebroeck, D.4
  • 14
    • 0011964044 scopus 로고
    • Activin A (EDF) releases the "two-cell block" of mouse embryos in culture
    • Lu, R.-Z., Shiota, K., Toyoda, Y., and Takahashi, M. (1990) Activin A (EDF) releases the "two-cell block" of mouse embryos in culture. Jpn. J. Anim. Reprod. 36, 127-132
    • (1990) Jpn. J. Anim. Reprod. , vol.36 , pp. 127-132
    • Lu, R.-Z.1    Shiota, K.2    Toyoda, Y.3    Takahashi, M.4
  • 15
    • 0025895091 scopus 로고
    • Interactions between activin and FSH-suppressing protein, and their mechanisms of action on cultured rat granulosa cells
    • Xiao, S. and Findlay, J.K. (1991) Interactions between activin and FSH-suppressing protein, and their mechanisms of action on cultured rat granulosa cells. Mol. Cell. Endocrinol. 79, 99-107
    • (1991) Mol. Cell. Endocrinol. , vol.79 , pp. 99-107
    • Xiao, S.1    Findlay, J.K.2
  • 16
    • 0024286302 scopus 로고
    • A novel action of activin A: Stimulation of insulin secretion in rat pancreatic islets
    • Totsuka, Y., Tabuchi, M., Kojima, I., Shibai, H., and Ogata, E. (1988) A novel action of activin A: Stimulation of insulin secretion in rat pancreatic islets. Biochem. Biophys. Res. Commun. 156, 335-339
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 335-339
    • Totsuka, Y.1    Tabuchi, M.2    Kojima, I.3    Shibai, H.4    Ogata, E.5
  • 17
    • 0025341426 scopus 로고
    • Activin A modulates growth hormone secretion from cultures of rat anterior pituitary cells
    • Bilezikjian, L.M., Corrigan, A.Z., and Vale, W. (1990) Activin A modulates growth hormone secretion from cultures of rat anterior pituitary cells. Endocrinology 128, 2369-2376
    • (1990) Endocrinology , vol.128 , pp. 2369-2376
    • Bilezikjian, L.M.1    Corrigan, A.Z.2    Vale, W.3
  • 18
    • 0025946915 scopus 로고
    • Transforming growth factor-β and activin inhibit basal secretion of prolactin in a pituitary monolayer culture system
    • Murata, T. and Ying, S.-Y. (1991) Transforming growth factor-β and activin inhibit basal secretion of prolactin in a pituitary monolayer culture system. Proc. Soc. Exp. Biol. Med. 198, 599-605
    • (1991) Proc. Soc. Exp. Biol. Med. , vol.198 , pp. 599-605
    • Murata, T.1    Ying, S.-Y.2
  • 21
    • 0023196580 scopus 로고
    • Heterodimers and homodimers of inhibin subunits have different paracrine actions in the modulation of luteinizing hormone-stimulated androgen biosynthesis
    • Hsueh, A.J.W., Dahl, K.D., Vaughan, J., Tucker, E., Rivier, J., Bardin, C.W., and Vale, W. (1987) Heterodimers and homodimers of inhibin subunits have different paracrine actions in the modulation of luteinizing hormone-stimulated androgen biosynthesis. Proc. Natl. Acad. Sci. USA 84, 5082-5086
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5082-5086
    • Hsueh, A.J.W.1    Dahl, K.D.2    Vaughan, J.3    Tucker, E.4    Rivier, J.5    Bardin, C.W.6    Vale, W.7
  • 22
    • 0024426772 scopus 로고
    • Activin-A, inhibin and transforming growth factor-β modulate growth of two gonadal cell lines
    • Gonzalez-Manchón, C. and Vale, W. (1989) Activin-A, inhibin and transforming growth factor-β modulate growth of two gonadal cell lines. Endocrinology 125, 1666-1672
    • (1989) Endocrinology , vol.125 , pp. 1666-1672
    • Gonzalez-Manchón, C.1    Vale, W.2
  • 23
    • 0027294895 scopus 로고
    • Chondrogenesis in chick limb bud mesodermal cells: Reciprocal modulation by activin and inhibin
    • Chen, P., Yu, Y.M., and Reddi, A.H. (1993) Chondrogenesis in chick limb bud mesodermal cells: Reciprocal modulation by activin and inhibin. Exp. Cell Res. 206, 119-127
    • (1993) Exp. Cell Res. , vol.206 , pp. 119-127
    • Chen, P.1    Yu, Y.M.2    Reddi, A.H.3
  • 24
    • 0025167701 scopus 로고
    • Identification of anovel member (GDF-1) of the transforming growth factor-β superfamily
    • Lee, S.-J. (1990) Identification of anovel member (GDF-1) of the transforming growth factor-β superfamily. Mol. Endocrinol. 4, 1034-1040
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1034-1040
    • Lee, S.-J.1
  • 26
    • 0025741546 scopus 로고
    • Follistatin binds to both activin and inhibin through the common beta-subunit
    • Shimonaka, M., Inouye, S., Shimasaki, S., and Ling, N. (1991) Follistatin binds to both activin and inhibin through the common beta-subunit. Endocrinology 128, 3313-3315
    • (1991) Endocrinology , vol.128 , pp. 3313-3315
    • Shimonaka, M.1    Inouye, S.2    Shimasaki, S.3    Ling, N.4
  • 27
    • 0027991604 scopus 로고
    • Characterization of unique binding kinetics of follistatin and activin or inhibin in serum
    • Schneyer, A.L., Rzucidlo, D.A., Sluss, P.M., and Crowley, W.F., Jr. (1994) Characterization of unique binding kinetics of follistatin and activin or inhibin in serum. Endocrinology 135, 667-674
    • (1994) Endocrinology , vol.135 , pp. 667-674
    • Schneyer, A.L.1    Rzucidlo, D.A.2    Sluss, P.M.3    Crowley Jr., W.F.4
  • 28
    • 0023848482 scopus 로고
    • Expression of erythroid differentiation factor (EDF) in Chinese hamster ovary cells
    • Murata, M., Onomichi, K., Eto, Y., Shibai, H., and Muramatsu, M. (1988) Expression of erythroid differentiation factor (EDF) in Chinese hamster ovary cells. Biochem, Biophys. Res. Commun. 151, 230-235
    • (1988) Biochem, Biophys. Res. Commun. , vol.151 , pp. 230-235
    • Murata, M.1    Onomichi, K.2    Eto, Y.3    Shibai, H.4    Muramatsu, M.5
  • 31
    • 0028566660 scopus 로고
    • B,-inhibin/activin genes: Identification of transcription factor AP-2-binding sites in the 5′-flanking regions by DNase I foot-printing
    • B,-inhibin/activin genes: Identification of transcription factor AP-2-binding sites in the 5′-flanking regions by DNase I foot-printing. Eur. J. Biochem. 226, 751-764
    • (1994) Eur. J. Biochem. , vol.226 , pp. 751-764
    • Thompson, D.A.1    Cronin, C.N.2    Martin, F.3
  • 32
    • 0020068839 scopus 로고
    • Radioimmunoassay for an analog of thyrotrophin-releasing hormone, γ-butyrolactone-γ-carbonyl-L-histidyl-L-prolinamide (DN-1417)
    • Shiota, K., Miyake, A., Tsunoda, C., Oka, Y., Nagawa, Y., and Nakayama, R. (1982) Radioimmunoassay for an analog of thyrotrophin-releasing hormone, γ-butyrolactone-γ-carbonyl-L-histidyl-L-prolinamide (DN-1417). J. Immunol. Methods 51, 69-80
    • (1982) J. Immunol. Methods , vol.51 , pp. 69-80
    • Shiota, K.1    Miyake, A.2    Tsunoda, C.3    Oka, Y.4    Nagawa, Y.5    Nakayama, R.6
  • 33
    • 0018200168 scopus 로고
    • Use of staphylococcal Protein A as an immunological reagent
    • Goeding, J.W. (1978) Use of staphylococcal Protein A as an immunological reagent. J. Immunol. Methods 20, 241-243
    • (1978) J. Immunol. Methods , vol.20 , pp. 241-243
    • Goeding, J.W.1
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-Glycosidase F
    • Tarentino, A.L., Gomez, C.M., and Plummer, T.H., Jr. (1985) Deglycosylation of asparagine-linked glycans by peptide: N-Glycosidase F. Biochemistry 24, 4665-4671
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer Jr., T.H.3
  • 37
    • 0026599921 scopus 로고
    • Purification and characterization of high molecular weight forms of inhibin from bovine follicular fluid
    • Sugino, K., Nakamura, T., Takio, K., Miyamoto, K., Hasegawa, Y., Igarashi, M., Titani, K., and Sugino, H. (1992) Purification and characterization of high molecular weight forms of inhibin from bovine follicular fluid. Endocrinology 130, 789-796
    • (1992) Endocrinology , vol.130 , pp. 789-796
    • Sugino, K.1    Nakamura, T.2    Takio, K.3    Miyamoto, K.4    Hasegawa, Y.5    Igarashi, M.6    Titani, K.7    Sugino, H.8
  • 41
    • 0027201580 scopus 로고
    • Differential control of activin, inhibin and follistatin proteins in cultured rat granulosa cells
    • Miyanaga, K., Erickson, G.F., DePaolo, L.V., Ling, N., and Shimasaki, S. (1993) Differential control of activin, inhibin and follistatin proteins in cultured rat granulosa cells. Biochem. Biophys. Res. Commun. 194, 253-258
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 253-258
    • Miyanaga, K.1    Erickson, G.F.2    DePaolo, L.V.3    Ling, N.4    Shimasaki, S.5
  • 44
    • 0028226709 scopus 로고
    • Functional analysis of the cysteine residues of activin A
    • Mason, A.J. (1994) Functional analysis of the cysteine residues of activin A. Mol. Endocrinol. 8, 325-332
    • (1994) Mol. Endocrinol. , vol.8 , pp. 325-332
    • Mason, A.J.1
  • 45
    • 0026552189 scopus 로고
    • Inhibin/activin β-subunit monomer: Isolation and characterization
    • Robertson, D.M., Foulds, L.M., Prisk, M., and Hedger, M.P. (1992) Inhibin/activin β-subunit monomer: Isolation and characterization. Endocrinology 130, 1680-1687
    • (1992) Endocrinology , vol.130 , pp. 1680-1687
    • Robertson, D.M.1    Foulds, L.M.2    Prisk, M.3    Hedger, M.P.4
  • 46
    • 0026565263 scopus 로고
    • Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis
    • Shiozaki, M., Sakai, R., Tabuchi, M., Nakamura, T., Sugino, K., Sugino, H., and Eto, Y. (1992) Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis. Proc. Natl. Acad. Sci. USA 89, 1553-1556
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1553-1556
    • Shiozaki, M.1    Sakai, R.2    Tabuchi, M.3    Nakamura, T.4    Sugino, K.5    Sugino, H.6    Eto, Y.7
  • 47
    • 0026489924 scopus 로고
    • Interaction between activin and follicule-stimulating hormone-suppressing protein/follistatin in the regulation of basal inhibin production by culture rat granulosa cells
    • Xiao, S., Farnworth, P.G., and Findlay, J.K. (1992) Interaction between activin and follicule-stimulating hormone-suppressing protein/follistatin in the regulation of basal inhibin production by culture rat granulosa cells. Endocrinology 131, 2365-2370
    • (1992) Endocrinology , vol.131 , pp. 2365-2370
    • Xiao, S.1    Farnworth, P.G.2    Findlay, J.K.3
  • 48
    • 0021952192 scopus 로고
    • Heterogeneity of rat FSH by chromatofocusing: Studies on serum FSH, hormone released in vitro and metabolic clearance rates of its various forms
    • Blum, W.F.P. and Gupta, D. (1985) Heterogeneity of rat FSH by chromatofocusing: Studies on serum FSH, hormone released in vitro and metabolic clearance rates of its various forms. J. Endocrinol. 105, 29-37
    • (1985) J. Endocrinol. , vol.105 , pp. 29-37
    • Blum, W.F.P.1    Gupta, D.2
  • 49
    • 0022551868 scopus 로고
    • Metabolic clearance of biologically active luteinizing hormone in man
    • Veldhuis, J.D., Fraioli, F., Rogol, A.D., and Dufau, M.L. (1986) Metabolic clearance of biologically active luteinizing hormone in man. J. Clin. Invest. 77, 1122-1128
    • (1986) J. Clin. Invest. , vol.77 , pp. 1122-1128
    • Veldhuis, J.D.1    Fraioli, F.2    Rogol, A.D.3    Dufau, M.L.4
  • 52
    • 0022492598 scopus 로고
    • Deglycosylated human follitropin: Characterization and effects on adenosine cyclic 3′,5′-phosphate production in porcine granulosa cells
    • Calvo, F.O., Keutmann, H.T., Bergert, E.R., and Ryan, R.J. (1986) Deglycosylated human follitropin: Characterization and effects on adenosine cyclic 3′,5′-phosphate production in porcine granulosa cells. Biochemistry 25, 3938-3943
    • (1986) Biochemistry , vol.25 , pp. 3938-3943
    • Calvo, F.O.1    Keutmann, H.T.2    Bergert, E.R.3    Ryan, R.J.4
  • 53
    • 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
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.