메뉴 건너뛰기




Volumn 59, Issue 2, 1998, Pages 233-240

Ovine allantoic fluid contains high concentrations of activin A: Partial dissociation of immunoactivity and bioactivity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN A;

EID: 0031879737     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod59.2.233     Document Type: Article
Times cited : (10)

References (43)
  • 2
    • 0022470831 scopus 로고
    • Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin
    • Ling N, Ying S-Y, Ueno N, Shimasaki S, Esch F, Hotta M, Guillemin R. Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin. Nature 1986; 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
  • 4
    • 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, Ueno N. Molecular cloning and functional analysis of a new activin β subunit: a dorsal mesoderm-inducing activity in Xenopus. Biochem Biophys Res Commun 1995; 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
  • 6
    • 0025016517 scopus 로고
    • Activins arc expressed early in Xenopus embryogenesis and can induce axial mesoderm and anterior structures
    • Thomsen G, Woolf T, Whitman M, Sokol S, Vaughan J, Vale W, Melton DA. Activins arc expressed early in Xenopus embryogenesis and can induce axial mesoderm and anterior structures. Cell 1990; 63: 485-493.
    • (1990) Cell , vol.63 , pp. 485-493
    • Thomsen, G.1    Woolf, T.2    Whitman, M.3    Sokol, S.4    Vaughan, J.5    Vale, W.6    Melton, D.A.7
  • 7
    • 0025685417 scopus 로고
    • Activin stimulates spermatogonial proliferation in germ-Sertoli cell cocultures from immature rat testis
    • Mather JP, Attie KM, Woodruff TK, Rice GC, Phillips DM. Activin stimulates spermatogonial proliferation in germ-Sertoli cell cocultures from immature rat testis. Endocrinology 1990; 127:3206-3214.
    • (1990) Endocrinology , vol.127 , pp. 3206-3214
    • Mather, J.P.1    Attie, K.M.2    Woodruff, T.K.3    Rice, G.C.4    Phillips, D.M.5
  • 8
    • 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, Tokogawa Y, Shibai H. Purification and characterization of erythroid differentiation factor (EDF) isolated from human leukemia cell line THP-1. Biochem Biophys Res Commun 1987; 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    Tokogawa, Y.5    Shibai, H.6
  • 9
    • 0028237670 scopus 로고
    • Inhibin and follistatin concentrations in fetal tissues and fluids during gestation in sheep: Evidence for activin in amniotic fluid
    • Wongprasartsuk S, Jenkin G, McFarlane JR, Goodman M, de Kretser DM. Inhibin and follistatin concentrations in fetal tissues and fluids during gestation in sheep: evidence for activin in amniotic fluid. J Endocrinol 1994; 141:219-229.
    • (1994) J Endocrinol , vol.141 , pp. 219-229
    • Wongprasartsuk, S.1    Jenkin, G.2    McFarlane, J.R.3    Goodman, M.4    De Kretser, D.M.5
  • 11
    • 0023193513 scopus 로고
    • Localization, secretion, and action of inhibin in human placenta
    • Petraglia F, Swachenko PE, Lim ATW, Rivier J, Vale W. Localization, secretion, and action of inhibin in human placenta. Science 1987; 237: 187-189.
    • (1987) Science , vol.237 , pp. 187-189
    • Petraglia, F.1    Swachenko, P.E.2    Lim, A.T.W.3    Rivier, J.4    Vale, W.5
  • 15
    • 0028122696 scopus 로고
    • Activin at parturition: Changes of maternal serum levels and evidence for binding sites in placenta and fetal membranes
    • Petraglia F, Gallinelli A, De Vita D, Lewis K, Mathews L, Vale W. Activin at parturition: changes of maternal serum levels and evidence for binding sites in placenta and fetal membranes. Obstet Gynecol 1994; 84:278-281.
    • (1994) Obstet Gynecol , vol.84 , pp. 278-281
    • Petraglia, F.1    Gallinelli, A.2    De Vita, D.3    Lewis, K.4    Mathews, L.5    Vale, W.6
  • 16
    • 0031057206 scopus 로고    scopus 로고
    • Activin A and follistatin are dynamically regulated during human pregnancy
    • Woodruff TK, Sluss P, Wang E, Janssen I, Mersol-Barg MS. Activin A and follistatin are dynamically regulated during human pregnancy. J Endocrinol 1997; 152:167-174.
    • (1997) J Endocrinol , vol.152 , pp. 167-174
    • Woodruff, T.K.1    Sluss, P.2    Wang, E.3    Janssen, I.4    Mersol-Barg, M.S.5
  • 17
    • 0029834358 scopus 로고    scopus 로고
    • Changes in peripheral serum levels of total activin A during the human menstrual cycle and pregnancy
    • Muttukrishna S, Fowler PA, George L, Groome NP, Knight PG. Changes in peripheral serum levels of total activin A during the human menstrual cycle and pregnancy. J Clin Endocrinol & Metab 1996; 81:3328-3334.
    • (1996) J Clin Endocrinol & Metab , vol.81 , pp. 3328-3334
    • Muttukrishna, S.1    Fowler, P.A.2    George, L.3    Groome, N.P.4    Knight, P.G.5
  • 18
    • 0022748006 scopus 로고
    • Anatomy, physiology and pathology of the amniotic and allantoic compartments in the sheep and cow
    • Wintour EM, Laurence BM, Lingwood BE. Anatomy, physiology and pathology of the amniotic and allantoic compartments in the sheep and cow. Austr Vet J 1986; 63:216-221.
    • (1986) Austr Vet J , vol.63 , pp. 216-221
    • Wintour, E.M.1    Laurence, B.M.2    Lingwood, B.E.3
  • 19
    • 0023696519 scopus 로고
    • Urethral and urachal urine output to the amniotic and allantoic sacs in fetal sheep
    • Wlodek ME, Challis JR, Patrick J. Urethral and urachal urine output to the amniotic and allantoic sacs in fetal sheep. J Dev Physiol 1988; 10:309-319.
    • (1988) J Dev Physiol , vol.10 , pp. 309-319
    • Wlodek, M.E.1    Challis, J.R.2    Patrick, J.3
  • 22
    • 0024066530 scopus 로고
    • Characterization of protein production by bovine chorionic and allantoic membranes
    • Godkin JD, Lifsey BJ Jr, Baumach GA. Characterization of protein production by bovine chorionic and allantoic membranes. Biol Reprod 1988; 39:195-204.
    • (1988) Biol Reprod , vol.39 , pp. 195-204
    • Godkin, J.D.1    Lifsey Jr., B.J.2    Baumach, G.A.3
  • 24
    • 0025823765 scopus 로고
    • Characterization of protein production by ovine placental membranes: Identification of a placental retinol-binding protein
    • Liu KH, Brewton RG, Baumbach GA, Godkin JD. Characterization of protein production by ovine placental membranes: identification of a placental retinol-binding protein. Endocrinology 1991; 129:126-132.
    • (1991) Endocrinology , vol.129 , pp. 126-132
    • Liu, K.H.1    Brewton, R.G.2    Baumbach, G.A.3    Godkin, J.D.4
  • 25
    • 0029063564 scopus 로고
    • Early gestational expression of transforming growth factor beta isoforms by the ovine placenta
    • Doré JJE Jr, Erby Wilkinson J, Godkin JD. Early gestational expression of transforming growth factor beta isoforms by the ovine placenta. Biol Reprod 1995; 53:143-152.
    • (1995) Biol Reprod , vol.53 , pp. 143-152
    • Doré Jr., J.J.E.1    Erby Wilkinson, J.2    Godkin, J.D.3
  • 26
    • 0026552189 scopus 로고
    • Inhibin/activin β subunit monomer: Isolation and characterization
    • Robertson DM, Foulds LM, Prisk M, Hedger MP. Inhibin/activin β subunit monomer: isolation and characterization. Endocrinology 1992; 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
  • 27
    • 0029990607 scopus 로고    scopus 로고
    • Measurement of activin in biological fluids by radioimmunoassay, utilizing dissociating agents to remove the interference of follistatin
    • McFarlane JR, Foulds LM, Pisciotta A, Robertson DM, de Kretser DM. Measurement of activin in biological fluids by radioimmunoassay, utilizing dissociating agents to remove the interference of follistatin. Eur J Endocrinol 1996; 134:481-489.
    • (1996) Eur J Endocrinol , vol.134 , pp. 481-489
    • McFarlane, J.R.1    Foulds, L.M.2    Pisciotta, A.3    Robertson, D.M.4    De Kretser, D.M.5
  • 31
    • 0030033697 scopus 로고    scopus 로고
    • Development and application of a two-site enzyme immunoassay for the determination of "total" activin-a concentrations in serum and follicular fluid
    • Knight PG, Muttukrishna S, Groome NP. Development and application of a two-site enzyme immunoassay for the determination of "total" activin-A concentrations in serum and follicular fluid. J Endocrinol 1996; 148:267-279.
    • (1996) J Endocrinol , vol.148 , pp. 267-279
    • Knight, P.G.1    Muttukrishna, S.2    Groome, N.P.3
  • 33
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray W, Boulikas T, Wray VP, Hancock R. Silver staining of proteins in polyacrylamide gels. Anal Biochem 1981; 118:197-203.
    • (1981) Anal Biochem , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 34
    • 0026088567 scopus 로고
    • Chromogenic substrates for horseradish peroxidase
    • Conyers SM, Kidwell DA. Chromogenic substrates for horseradish peroxidase. Anal Biochem 1991; 192:207-211.
    • (1991) Anal Biochem , vol.192 , pp. 207-211
    • Conyers, S.M.1    Kidwell, D.A.2
  • 35
    • 0027989817 scopus 로고
    • The primary structure of serum amyloid A protein in the sheep: Comparison with serum amyloid A in other species
    • Syversen PV, Juul J, Marhaug G, Husby G, Sletten K. The primary structure of serum amyloid A protein in the sheep: comparison with serum amyloid A in other species. Scand J Immunol 1994; 39:88-94.
    • (1994) Scand J Immunol , vol.39 , pp. 88-94
    • Syversen, P.V.1    Juul, J.2    Marhaug, G.3    Husby, G.4    Sletten, K.5
  • 37
    • 2642601320 scopus 로고
    • Isolation and characterisation of inhibin-related molecules from porcine ovarian follicular fluid
    • Burger HG, de Kretser DM, Findlay JK, Igarashi M (eds.), Serono Symposia Publications, New York: Raven Press
    • Ling N, Ueno N, Ying S-Y, Esgh F, Shimasaki S, Hotta M, Guillemin R. Isolation and characterisation of inhibin-related molecules from porcine ovarian follicular fluid. In: Burger HG, de Kretser DM, Findlay JK, Igarashi M (eds.), Inhibin-Non-Steroidal Regulation of Follicle Stimulating Hormone Secretion, Serono Symposia Publications, vol. 42. New York: Raven Press; 1987: 61-76.
    • (1987) Inhibin-Non-Steroidal Regulation of Follicle Stimulating Hormone Secretion , vol.42 , pp. 61-76
    • Ling, N.1    Ueno, N.2    Ying, S.-Y.3    Esgh, F.4    Shimasaki, S.5    Hotta, M.6    Guillemin, R.7
  • 38
    • 43949151585 scopus 로고
    • The major acute phase reactants: C-reactive protein, serum amyloid P component and serum amyloid A protein
    • Steel DM, Whitehead AS. The major acute phase reactants: C-reactive protein, serum amyloid P component and serum amyloid A protein. Immunol Today 1994; 15:81-88.
    • (1994) Immunol Today , vol.15 , pp. 81-88
    • Steel, D.M.1    Whitehead, A.S.2
  • 39
    • 0026352696 scopus 로고
    • The primary structure of serum amyloid A protein in the rabbit: Comparison with serum amyloid A proteins in other species
    • Liepnieks JJ, Dwulet FE, Benson MD, Kluve-Beckerman B, Kushner I. The primary structure of serum amyloid A protein in the rabbit: comparison with serum amyloid A proteins in other species. J Lab Clin Med 1991; 118:570-575.
    • (1991) J Lab Clin Med , vol.118 , pp. 570-575
    • Liepnieks, J.J.1    Dwulet, F.E.2    Benson, M.D.3    Kluve-Beckerman, B.4    Kushner, I.5
  • 40
  • 43
    • 0029384851 scopus 로고
    • Sandwich enzyme-linked immunosorbent assay for quantitative measurement of serum amyloid A protein in horses
    • Satoh M, Fujinaga T, Okumura M, Hagio M. Sandwich enzyme-linked immunosorbent assay for quantitative measurement of serum amyloid A protein in horses. Am J Vet Res 1995; 56:1286-1291.
    • (1995) Am J Vet Res , vol.56 , pp. 1286-1291
    • Satoh, M.1    Fujinaga, T.2    Okumura, M.3    Hagio, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.