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Volumn 57, Issue 4, 1997, Pages 856-864

Molecular characterization of a ribonucleic acid transcript that is highly up-regulated at the time of ovulation in the brook trout (Salvelinus fontinalis) ovary

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; RNA;

EID: 0030886806     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod57.4.856     Document Type: Article
Times cited : (59)

References (39)
  • 1
    • 0018827831 scopus 로고
    • Ovulation as an inflammatory reaction - A hypothesis
    • Espey LL. Ovulation as an inflammatory reaction - a hypothesis. Biol Reprod 1980; 22:73-106.
    • (1980) Biol Reprod , vol.22 , pp. 73-106
    • Espey, L.L.1
  • 4
    • 0342737591 scopus 로고
    • Ovulation specific transcription of antileukoproteinase-like mRNAs in the brook trout ovary
    • Fujimoto S, Hsueh AJW, Strauss JF, Tanaka T (eds.). Rome, Italy: Ares-Serono Symposia Publications
    • Hsu S-Y, Goetz FW. Ovulation specific transcription of antileukoproteinase-like mRNAs in the brook trout ovary. In: Fujimoto S, Hsueh AJW, Strauss JF, Tanaka T (eds.), New Achievements in Research of Ovarian Function. Rome, Italy: Ares-Serono Symposia Publications; 1995: 183-190.
    • (1995) New Achievements in Research of Ovarian Function , pp. 183-190
    • Hsu, S.-Y.1    Goetz, F.W.2
  • 6
    • 0020198703 scopus 로고
    • The effects of prostaglandins, phosphodiesterase inhibitors, and cyclic AMP on ovulation of brook trout (Salvelinus fontinalis) oocytes
    • Goetz FW, Smith DC, Krickl SP The effects of prostaglandins, phosphodiesterase inhibitors, and cyclic AMP on ovulation of brook trout (Salvelinus fontinalis) oocytes. Gen Comp Endocrinol 1982; 48:154-160.
    • (1982) Gen Comp Endocrinol , vol.48 , pp. 154-160
    • Goetz, F.W.1    Smith, D.C.2    Krickl, S.P.3
  • 7
    • 77956796902 scopus 로고
    • Fish cell and tissue culture
    • Hoar WS, Randall DJ (eds.). New York, NY: Academic Press
    • Wolf K, Quimby MC. Fish cell and tissue culture. In: Hoar WS, Randall DJ (eds.), Fish Physiology. New York, NY: Academic Press; 1969: 253-305.
    • (1969) Fish Physiology , pp. 253-305
    • Wolf, K.1    Quimby, M.C.2
  • 9
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162:156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 0027169767 scopus 로고
    • A reagent for the single-step simultaneous isolation of RNA, DNA, and proteins from cell and tissue samples
    • Chomczynski P. A reagent for the single-step simultaneous isolation of RNA, DNA, and proteins from cell and tissue samples. Biotechniques 1993; 15:532-537.
    • (1993) Biotechniques , vol.15 , pp. 532-537
    • Chomczynski, P.1
  • 11
    • 0021856417 scopus 로고
    • Signal sequences: The limits of variation
    • Von Heijne G. Signal sequences: the limits of variation. J Mol Biol 1985; 184:99-105.
    • (1985) J Mol Biol , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 12
    • 0021248179 scopus 로고
    • SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins
    • Kaufmann E, Geisler N, Weber K. SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins. FEBS Lett 1984; 170:81-84.
    • (1984) FEBS Lett , vol.170 , pp. 81-84
    • Kaufmann, E.1    Geisler, N.2    Weber, K.3
  • 13
    • 0019406433 scopus 로고
    • The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E. coli K12
    • Burton Z, Burgess RR, Lin J, Moore D, Holder S, Gross CA. The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E. coli K12. Nucleic Acids Res 1981; 9:2889-2903.
    • (1981) Nucleic Acids Res , vol.9 , pp. 2889-2903
    • Burton, Z.1    Burgess, R.R.2    Lin, J.3    Moore, D.4    Holder, S.5    Gross, C.A.6
  • 14
    • 34249928081 scopus 로고
    • Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis
    • Wu DW, Duman JG, Cheng C-HC, Castellino FJ. Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis. J Comp Physiol B 1991; 161:271-278.
    • (1991) J Comp Physiol B , vol.161 , pp. 271-278
    • Wu, D.W.1    Duman, J.G.2    Cheng, C.-H.C.3    Castellino, F.J.4
  • 15
    • 0017911968 scopus 로고
    • Measurements of molecular weights by gel globular proteins
    • Hirs CHW, Timasheff SN (eds.). New York: Academic Press
    • Nielsen TB, Reynolds JA. Measurements of molecular weights by gel globular proteins. In: Hirs CHW, Timasheff SN (eds.), Methods in Enzymology. New York: Academic Press; 1978: 3-10.
    • (1978) Methods in Enzymology , pp. 3-10
    • Nielsen, T.B.1    Reynolds, J.A.2
  • 16
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins DG, Sharp PM. CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 1988: 73:237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 17
    • 0025094355 scopus 로고
    • Complementary DNA cloning and regulation of expression of the mRNA encoding a pregnancy-associated porcine uterine protein related to human antileukoproteinase
    • Farmer SJ, Fliss AE, Simmen RCM. Complementary DNA cloning and regulation of expression of the mRNA encoding a pregnancy-associated porcine uterine protein related to human antileukoproteinase. Mol Endocrinol 1990; 4:1095-1104.
    • (1990) Mol Endocrinol , vol.4 , pp. 1095-1104
    • Farmer, S.J.1    Fliss, A.E.2    Simmen, R.C.M.3
  • 18
    • 0025826573 scopus 로고
    • A major human epididymis-specific cDNA encodes a protein with sequence homology to extra-cellular proteinase inhibitors
    • Kirchhoff C, Habben I, Ivell R, Krull N. A major human epididymis-specific cDNA encodes a protein with sequence homology to extra-cellular proteinase inhibitors. Biol Reprod 1991; 45:350-357.
    • (1991) Biol Reprod , vol.45 , pp. 350-357
    • Kirchhoff, C.1    Habben, I.2    Ivell, R.3    Krull, N.4
  • 20
    • 0026058053 scopus 로고
    • Skin-derived antileukoproteinase (SKALP), an elastase inhibitor from human keratinocytes. Purification and biochemical properties
    • Schalkwijk U, De Roo C. De Jongh GJ. Skin-derived antileukoproteinase (SKALP), an elastase inhibitor from human keratinocytes. Purification and biochemical properties. Biochim Biophys Acta 1991; 1096:148-154.
    • (1991) Biochim Biophys Acta , vol.1096 , pp. 148-154
    • Schalkwijk, U.1    De Roo, C.2    De Jongh, G.J.3
  • 21
    • 0020490765 scopus 로고
    • Comparative sequence analysis of the mRNAs coding for mouse and rat whey protein
    • Hennighausen LG, Sippel AE, Hobbs AA, Rosen JM. Comparative sequence analysis of the mRNAs coding for mouse and rat whey protein. Nucleic Acids Res 1982; 10:3733-3744.
    • (1982) Nucleic Acids Res , vol.10 , pp. 3733-3744
    • Hennighausen, L.G.1    Sippel, A.E.2    Hobbs, A.A.3    Rosen, J.M.4
  • 22
    • 0000597410 scopus 로고
    • Trypsin-subtilisin inhibitor from red sea turtle eggwhite consists of two tandem domains - One kunitz - one of a new family
    • Kato I, Tominaga N. Trypsin-subtilisin inhibitor from red sea turtle eggwhite consists of two tandem domains - one kunitz - one of a new family. Fed Proc 1979; 38:832.
    • (1979) Fed Proc , vol.38 , pp. 832
    • Kato, I.1    Tominaga, N.2
  • 23
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor
    • Thompson RC, Ohlsson K. Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor. Proc Natl Acad Sci USA 1986; 83:6692-6696.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6692-6696
    • Thompson, R.C.1    Ohlsson, K.2
  • 24
    • 0017605281 scopus 로고
    • Isolation and partial characterization of a low molecular weight acid stable protease inhibitor from human bronchial secretion
    • Ohlsson K, Tegner H, Akesson U. Isolation and partial characterization of a low molecular weight acid stable protease inhibitor from human bronchial secretion. Hoppe-Seyler's Z Physiol Chem 1977; 358:583-589.
    • (1977) Hoppe-Seyler's Z Physiol Chem , vol.358 , pp. 583-589
    • Ohlsson, K.1    Tegner, H.2    Akesson, U.3
  • 25
    • 0019423504 scopus 로고
    • Localization of low molecular weight protease inhibitor in serous secretory cells of the respiratory tract
    • Kramps JA, Franken C, Meyer CJL, Dijkman JH. Localization of low molecular weight protease inhibitor in serous secretory cells of the respiratory tract. Histochem Cytochem 1981; 29:712-716.
    • (1981) Histochem Cytochem , vol.29 , pp. 712-716
    • Kramps, J.A.1    Franken, C.2    Meyer, C.J.L.3    Dijkman, J.H.4
  • 27
    • 0026828925 scopus 로고
    • A comparative study of the low molecular mass serine proteinase inhibitors of human connective tissues
    • Andrews JL, Melrose J, Ghosh P. A comparative study of the low molecular mass serine proteinase inhibitors of human connective tissues. Biol Chem Hoppe-Seyler 1992; 373:111-118.
    • (1992) Biol Chem Hoppe-Seyler , vol.373 , pp. 111-118
    • Andrews, J.L.1    Melrose, J.2    Ghosh, P.3
  • 28
    • 0027132418 scopus 로고
    • Secretory leucocyte proteinase inhibitor is produced by human articular cartilage chondrocytes and intervertebral disc fibro-chondrocytes
    • Jacoby AS, Melrose J, Robinson BG, Hyland VJ, Ghosh P. Secretory leucocyte proteinase inhibitor is produced by human articular cartilage chondrocytes and intervertebral disc fibro-chondrocytes. Eur J Biochem 1993; 218:951-957.
    • (1993) Eur J Biochem , vol.218 , pp. 951-957
    • Jacoby, A.S.1    Melrose, J.2    Robinson, B.G.3    Hyland, V.J.4    Ghosh, P.5
  • 30
    • 0021960034 scopus 로고
    • Human bronchial leucocyte proteinase inhibitor
    • Smith CE, Johnson DA. Human bronchial leucocyte proteinase inhibitor. Biochem J 1985; 225:463-472.
    • (1985) Biochem J , vol.225 , pp. 463-472
    • Smith, C.E.1    Johnson, D.A.2
  • 32
    • 0024582695 scopus 로고
    • Mucus proteinase inhibitor: A fast-acting inhibitor of leucocyte elastase
    • Boudier C, Bieth JG. Mucus proteinase inhibitor: a fast-acting inhibitor of leucocyte elastase. Biochim Biophys Acta 1989; 995:36-41.
    • (1989) Biochim Biophys Acta , vol.995 , pp. 36-41
    • Boudier, C.1    Bieth, J.G.2
  • 33
    • 0026657360 scopus 로고
    • Heparin-induced conformational change and activation of mucus proteinase inhibitor
    • Faller B, Mely Y, Gerard D, Bieth JG. Heparin-induced conformational change and activation of mucus proteinase inhibitor. Biochemistry 1992; 31:8285-8290.
    • (1992) Biochemistry , vol.31 , pp. 8285-8290
    • Faller, B.1    Mely, Y.2    Gerard, D.3    Bieth, J.G.4
  • 34
    • 0025228671 scopus 로고
    • Proteinase inhibitory activities of antileukoprolease are represented by its second COOH-terminal domain
    • Kramps JA, van Twisk C, Appelhans H, Meckelhein B. Proteinase inhibitory activities of antileukoprolease are represented by its second COOH-terminal domain. Biochim Biophys Acta 1990; 1038:178-185.
    • (1990) Biochim Biophys Acta , vol.1038 , pp. 178-185
    • Kramps, J.A.1    Van Twisk, C.2    Appelhans, H.3    Meckelhein, B.4
  • 35
    • 0025247809 scopus 로고
    • The location of inhibitory specificities in human mucus proteinase inhibitor (MPI): Separate expression of the COOH-terminal domain yields an active inhibitor of three different proteinases
    • Meckelein B, Nikorov T, Clemen A, Appelhans H. The location of inhibitory specificities in human mucus proteinase inhibitor (MPI): separate expression of the COOH-terminal domain yields an active inhibitor of three different proteinases. Protein Eng 1990; 3:215-220.
    • (1990) Protein Eng , vol.3 , pp. 215-220
    • Meckelein, B.1    Nikorov, T.2    Clemen, A.3    Appelhans, H.4
  • 36
    • 0024114863 scopus 로고
    • Morphological studies of the microcirculatory system of periovulatory ovine follicles
    • Cavender JL, Murdoch WJ. Morphological studies of the microcirculatory system of periovulatory ovine follicles. Biol Reprod 1988; 39:989-997.
    • (1988) Biol Reprod , vol.39 , pp. 989-997
    • Cavender, J.L.1    Murdoch, W.J.2
  • 37
    • 0024415766 scopus 로고
    • Production of low molecular weight chemoattractants for leukocytes by periovulatory ovine follicles
    • Murdoch WJ, McCormick RJ. Production of low molecular weight chemoattractants for leukocytes by periovulatory ovine follicles. Biol Reprod 1989; 40:86-90.
    • (1989) Biol Reprod , vol.40 , pp. 86-90
    • Murdoch, W.J.1    McCormick, R.J.2
  • 38
    • 0030020551 scopus 로고    scopus 로고
    • Inhibition of human mast cell chymase by secretory leukocyte proteinase inhibitor: Enhancement of the interaction by heparin
    • Walter M, Plotnick M, Schechter NM. Inhibition of human mast cell chymase by secretory leukocyte proteinase inhibitor: enhancement of the interaction by heparin. Arch Biochem Biophys 1996; 327:81-88.
    • (1996) Arch Biochem Biophys , vol.327 , pp. 81-88
    • Walter, M.1    Plotnick, M.2    Schechter, N.M.3
  • 39
    • 0002696851 scopus 로고
    • Inhibition of chorion expansion and preservation of fertility in goldfish (Carassius auratus) eggs by protease inhibitors
    • Hsu S-Y, Goetz FW. Inhibition of chorion expansion and preservation of fertility in goldfish (Carassius auratus) eggs by protease inhibitors. Can J Fish Aquat Sci 1993; 50:932-935.
    • (1993) Can J Fish Aquat Sci , vol.50 , pp. 932-935
    • Hsu, S.-Y.1    Goetz, F.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.