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Volumn 68, Issue 4, 2003, Pages 1447-1454

Expression and regulation of interferon γ-inducible proteasomal subunits LMP7 and LMP10 in the bovine corpus luteum

Author keywords

Corpus luteum; Corpus luteum function; Immunology; Ovary

Indexed keywords

GAMMA INTERFERON; GAMMA INTERFERON INDUCIBLE PROTEASOME SUBUNIT; LUTEINIZING HORMONE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MESSENGER RNA; PROSTAGLANDIN F2 ALPHA; PROTEASOME; PROTEIN LMP10; PROTEIN LMP7; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 0037377916     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.102.010249     Document Type: Article
Times cited : (10)

References (50)
  • 1
    • 0033043352 scopus 로고    scopus 로고
    • Immune cells and cytokine production in the bovine corpus luteum throughout the oestrous cycle and after induced luteolysis
    • Penny LA, Armstrong D, Bramley TA, Webb R, Collins RA, Watson ED. Immune cells and cytokine production in the bovine corpus luteum throughout the oestrous cycle and after induced luteolysis. J Reprod Fertil 1999; 115:87-96.
    • (1999) J Reprod Fertil , vol.115 , pp. 87-96
    • Penny, L.A.1    Armstrong, D.2    Bramley, T.A.3    Webb, R.4    Collins, R.A.5    Watson, E.D.6
  • 2
    • 0036157383 scopus 로고    scopus 로고
    • Expression of monocyte chemoattractant protein-1 and distribution of immune cell populations in the bovine corpus luteum throughout the estrous cycle
    • Townson DH, O'Connor CL, Pru JK. Expression of monocyte chemoattractant protein-1 and distribution of immune cell populations in the bovine corpus luteum throughout the estrous cycle. Biol Reprod 2002; 66:361-366.
    • (2002) Biol Reprod , vol.66 , pp. 361-366
    • Townson, D.H.1    O'Connor, C.L.2    Pru, J.K.3
  • 3
    • 0032908440 scopus 로고    scopus 로고
    • Expression of cytokine messenger ribonucleic acids in the bovine corpus luteum
    • Petroff MG, Petroff BK, Pate JL. Expression of cytokine messenger ribonucleic acids in the bovine corpus luteum. Endocrinology 1999; 140:1018-1021.
    • (1999) Endocrinology , vol.140 , pp. 1018-1021
    • Petroff, M.G.1    Petroff, B.K.2    Pate, J.L.3
  • 4
    • 0002141941 scopus 로고
    • Localization of tumor necrosis factor (TNF) in the rat and bovine ovary using immunocytochemistry and cell blot: Evidence for granulosal production
    • Hirshfield AN (ed.), New York: Plenum
    • Roby KF, Terranova PF. Localization of tumor necrosis factor (TNF) in the rat and bovine ovary using immunocytochemistry and cell blot: evidence for granulosal production. In: Hirshfield AN (ed.), Growth Factors and the Ovary. New York: Plenum; 1989: 273-278.
    • (1989) Growth Factors and the Ovary , pp. 273-278
    • Roby, K.F.1    Terranova, P.F.2
  • 5
    • 0029112109 scopus 로고
    • Concentrations of tumor necrosis factor α and progesterone within the bovine corpus luteum sampled by continuousflow microdialysis during luteolysis in vivo
    • Shaw DW, Britt JH. Concentrations of tumor necrosis factor α and progesterone within the bovine corpus luteum sampled by continuousflow microdialysis during luteolysis in vivo. Biol Reprod 1995; 53: 847-854.
    • (1995) Biol Reprod , vol.53 , pp. 847-854
    • Shaw, D.W.1    Britt, J.H.2
  • 6
    • 0025815194 scopus 로고
    • Expression of major histocompatibility complex antigens on the bovine corpus luteum during the estrous cycle, luteolysis, and early pregnancy
    • Benyo D, Haibel GK, Laufman HB, Pate JL. Expression of major histocompatibility complex antigens on the bovine corpus luteum during the estrous cycle, luteolysis, and early pregnancy. Biol Reprod 1991; 45:229-234.
    • (1991) Biol Reprod , vol.45 , pp. 229-234
    • Benyo, D.1    Haibel, G.K.2    Laufman, H.B.3    Pate, J.L.4
  • 7
    • 0030954827 scopus 로고    scopus 로고
    • Bovine luteal cells elicit major histocompatibility complex class II-dependent T-cell proliferation
    • Petroff MG, Coggeshall KM, Jones LS, Pate JL. Bovine luteal cells elicit major histocompatibility complex class II-dependent T-cell proliferation. Biol Reprod 1997; 57:887-893.
    • (1997) Biol Reprod , vol.57 , pp. 887-893
    • Petroff, M.G.1    Coggeshall, K.M.2    Jones, L.S.3    Pate, J.L.4
  • 8
    • 0025324091 scopus 로고
    • Structure, function, and diversity of class I major histocompatibility complex molecules
    • Bjorkman PJ, Parham P. Structure, function, and diversity of class I major histocompatibility complex molecules. Annu Rev Biochem 1990; 59:253-288.
    • (1990) Annu Rev Biochem , vol.59 , pp. 253-288
    • Bjorkman, P.J.1    Parham, P.2
  • 9
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock KL, Goldberg AL. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu Rev Immunol 1999; 17:739-779.
    • (1999) Annu Rev Immunol , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 10
    • 0033451923 scopus 로고    scopus 로고
    • Proteolysis and class I major histocompatibility complex antigen processing
    • York IA, Goldberg AL, Mo XY, Rock KL. Proteolysis and class I major histocompatibility complex antigen processing. Immunol Rev 1999; 172:49-66.
    • (1999) Immunol Rev , vol.172 , pp. 49-66
    • York, I.A.1    Goldberg, A.L.2    Mo, X.Y.3    Rock, K.L.4
  • 12
    • 0027707607 scopus 로고
    • Structural features of 26S and 20S proteasomes
    • Lupas A, Koster AJ, Baumeister W. Structural features of 26S and 20S proteasomes. Enzyme Protein 1993; 47:252-273.
    • (1993) Enzyme Protein , vol.47 , pp. 252-273
    • Lupas, A.1    Koster, A.J.2    Baumeister, W.3
  • 13
    • 0029878931 scopus 로고    scopus 로고
    • Identification of MECL-1 (LMP10) as the third IFN-γ-inducible proteasome subunit
    • Nandi D, Jiang H, Monaco JJ. Identification of MECL-1 (LMP10) as the third IFN-γ-inducible proteasome subunit. J Immunol 1996; 156: 2361-2364.
    • (1996) J Immunol , vol.156 , pp. 2361-2364
    • Nandi, D.1    Jiang, H.2    Monaco, J.J.3
  • 15
    • 0030898161 scopus 로고    scopus 로고
    • Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: Reciprocally regulated tissue expression of interferon-gamma- modulated proteasome subunits
    • Stohwasser R, Standera S, Peters I, Kloetzel PM, Groettrup M. Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: reciprocally regulated tissue expression of interferon-gamma- modulated proteasome subunits. Eur J Immunol 1997; 27:1182-1187.
    • (1997) Eur J Immunol , vol.27 , pp. 1182-1187
    • Stohwasser, R.1    Standera, S.2    Peters, I.3    Kloetzel, P.M.4    Groettrup, M.5
  • 16
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M, Rock KL, Goldberg AL. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 1993; 365:264-267.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 17
    • 0028136465 scopus 로고
    • Peptidase activities of the proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7
    • Gaczynska M, Rock KL, Spies T, Goldberg AL. Peptidase activities of the proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7. Proc Natl Acad Sci U S A 1994; 91:9213-9217.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9213-9217
    • Gaczynska, M.1    Rock, K.L.2    Spies, T.3    Goldberg, A.L.4
  • 18
    • 0030037846 scopus 로고    scopus 로고
    • Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-gamma induced subunits LMP2 and LMP7
    • Gaczynska M, Goldberg AL, Tanaka K, Hendil KB, Rock KL. Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-gamma induced subunits LMP2 and LMP7. J Biol Chem 1996; 271:17275-17280.
    • (1996) J Biol Chem , vol.271 , pp. 17275-17280
    • Gaczynska, M.1    Goldberg, A.L.2    Tanaka, K.3    Hendil, K.B.4    Rock, K.L.5
  • 19
    • 0027223877 scopus 로고
    • MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
    • Driscoll J, Brown MG, Finley D, Monaco JJ. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 1993; 365:262-264.
    • (1993) Nature , vol.365 , pp. 262-264
    • Driscoll, J.1    Brown, M.G.2    Finley, D.3    Monaco, J.J.4
  • 20
    • 0012579476 scopus 로고    scopus 로고
    • 2α-induced changes in bovine luteal cells result in increased ability of luteal cells to stimulate class II MHC-dependent lymphocyte proliferation in vitro
    • Pullman, WA. Abstract
    • 2α-induced changes in bovine luteal cells result in increased ability of luteal cells to stimulate class II MHC-dependent lymphocyte proliferation in vitro. In: Program of the 32nd annual meeting of the Society for the Study of Reproduction; 1997; Pullman, WA. Abstract 604.
    • (1997) Program of the 32nd annual meeting of the Society for the Study of Reproduction , pp. 604
    • Cannon, M.J.1    Petroff, M.G.2    Pate, J.L.3
  • 21
    • 0028004320 scopus 로고
    • Expression of HLA class II-associated peptide transporter and proteasome genes in human placentas and trophoblast cell lines
    • Roby KF, Fei K, Yang Y, Hunt JS. Expression of HLA class II-associated peptide transporter and proteasome genes in human placentas and trophoblast cell lines. Immunology 1994; 83:444-448.
    • (1994) Immunology , vol.83 , pp. 444-448
    • Roby, K.F.1    Fei, K.2    Yang, Y.3    Hunt, J.S.4
  • 22
    • 0035883047 scopus 로고    scopus 로고
    • Tumor necrosis factor-α induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface
    • Hallermalm K, Seki K, Wei C, Castelli C, Rivoltini L, Kiessling R, Levitskaya J. Tumor necrosis factor-α induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface. Blood 2001; 98:1108-1115.
    • (2001) Blood , vol.98 , pp. 1108-1115
    • Hallermalm, K.1    Seki, K.2    Wei, C.3    Castelli, C.4    Rivoltini, L.5    Kiessling, R.6    Levitskaya, J.7
  • 23
    • 0020385928 scopus 로고
    • Effects of serum and lipoproteins on steroidogenesis in cultured bovine luteal cells
    • Pate JL, Condon WA. Effects of serum and lipoproteins on steroidogenesis in cultured bovine luteal cells. Mol Cell Endocrinol 1982; 28: 551-562.
    • (1982) Mol Cell Endocrinol , vol.28 , pp. 551-562
    • Pate, J.L.1    Condon, W.A.2
  • 24
    • 0021645910 scopus 로고
    • 2α on agonist-induced progesterone production in cultured bovine luteal cells
    • 2α on agonist-induced progesterone production in cultured bovine luteal cells. Biol Reprod 1984; 31:427-435.
    • (1984) Biol Reprod , vol.31 , pp. 427-435
    • Pate, J.L.1    Condon, W.A.2
  • 25
    • 0024453439 scopus 로고
    • 2α and lipoproteins in bovine luteal cells
    • 2α and lipoproteins in bovine luteal cells. J Reprod Fertil 1989; 87:439-446.
    • (1989) J Reprod Fertil , vol.87 , pp. 439-446
    • Pate, J.L.1    Condon, W.A.2
  • 26
    • 0026520947 scopus 로고
    • Tumor necrosis factor-α alters bovine luteal cell synthetic capacity and viability
    • Benyo DF, Pate JL. Tumor necrosis factor-α alters bovine luteal cell synthetic capacity and viability. Endocrinology 1992; 130:854-860.
    • (1992) Endocrinology , vol.130 , pp. 854-860
    • Benyo, D.F.1    Pate, J.L.2
  • 27
    • 0030296899 scopus 로고    scopus 로고
    • Mechanism of action of TNF-α-stimulated prostaglandin production in cultured bovine luteal cells
    • Townson DH, Pate JL. Mechanism of action of TNF-α-stimulated prostaglandin production in cultured bovine luteal cells. Prostaglandins 1996; 52:361-373.
    • (1996) Prostaglandins , vol.52 , pp. 361-373
    • Townson, D.H.1    Pate, J.L.2
  • 28
    • 0034098796 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor in the bovine corpus luteum: Characterization of steady-state messenger ribonucleic acid and immunohistochemical localization
    • Bove SE, Petroff MG, Nishibori M, Pate JL. Macrophage migration inhibitory factor in the bovine corpus luteum: characterization of steady-state messenger ribonucleic acid and immunohistochemical localization. Biol Reprod 2000; 62:879-885.
    • (2000) Biol Reprod , vol.62 , pp. 879-885
    • Bove, S.E.1    Petroff, M.G.2    Nishibori, M.3    Pate, J.L.4
  • 31
    • 0028865140 scopus 로고
    • Cellular distribution of proteasome subunit Lmp7 mRNA and protein in human placentas
    • Roby KF, Yang Y, Gershon D, Hunt JS. Cellular distribution of proteasome subunit Lmp7 mRNA and protein in human placentas. Immunology 1995; 86:469-474.
    • (1995) Immunology , vol.86 , pp. 469-474
    • Roby, K.F.1    Yang, Y.2    Gershon, D.3    Hunt, J.S.4
  • 32
    • 0032510347 scopus 로고    scopus 로고
    • Constitutive and interferonγ-induced expression of the human proteasome subunit multicatalytic endopeptidase complex-like 1
    • Foss GS, Larsen F, Solheim J, Prydz H. Constitutive and interferonγ-induced expression of the human proteasome subunit multicatalytic endopeptidase complex-like 1. Biochim Biophys Acta 1998; 1402:17-28.
    • (1998) Biochim Biophys Acta , vol.1402 , pp. 17-28
    • Foss, G.S.1    Larsen, F.2    Solheim, J.3    Prydz, H.4
  • 34
    • 0028326667 scopus 로고
    • Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing
    • Akiyama K, Kagawa S, Tamura T, Shimbara N, Takashina M, Kristenson P, Hendil KB, Tanaka K, Ichihara A. Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing. FEBS Lett 1994; 343:85-88.
    • (1994) FEBS Lett , vol.343 , pp. 85-88
    • Akiyama, K.1    Kagawa, S.2    Tamura, T.3    Shimbara, N.4    Takashina, M.5    Kristenson, P.6    Hendil, K.B.7    Tanaka, K.8    Ichihara, A.9
  • 37
    • 0028241569 scopus 로고
    • Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: A newly discovered mechanism for modulating the multicatalytic proteinase complex
    • Fruh K, Gossen M, Wang K, Bujard H, Peterson PA, Yang Y. Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J 1994; 13:3236-3244.
    • (1994) EMBO J , vol.13 , pp. 3236-3244
    • Fruh, K.1    Gossen, M.2    Wang, K.3    Bujard, H.4    Peterson, P.A.5    Yang, Y.6
  • 38
    • 0028097823 scopus 로고
    • Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • Boes B, Hengel H, Ruppert T, Multhaup G, Koszinowski UH, Kloetzel PM. Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J Exp Med 1994; 179:901-909.
    • (1994) J Exp Med , vol.179 , pp. 901-909
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaup, G.4    Koszinowski, U.H.5    Kloetzel, P.M.6
  • 41
    • 0025771623 scopus 로고
    • A proteasome-related gene between the two ABC transporter loci in the class lI region of the human MHC
    • Glynne R, Powis SH, Beck S, Kelly A, Kerr LA, Trowsdale J. A proteasome-related gene between the two ABC transporter loci in the class lI region of the human MHC. Nature 1991; 353:357-360.
    • (1991) Nature , vol.353 , pp. 357-360
    • Glynne, R.1    Powis, S.H.2    Beck, S.3    Kelly, A.4    Kerr, L.A.5    Trowsdale, J.6
  • 43
    • 0026040535 scopus 로고
    • Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene
    • Martinez CK, Monaco JJ. Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene. Nature 1991; 353: 664-667.
    • (1991) Nature , vol.353 , pp. 664-667
    • Martinez, C.K.1    Monaco, J.J.2
  • 44
    • 0028829806 scopus 로고
    • Presence and localization of tumor necrosis factor α in the corpus luteum of nonpregnant and pregnant pigs
    • Hehnke-Vagnoni KE, Clark CL, Taylor MJ, Ford SP. Presence and localization of tumor necrosis factor α in the corpus luteum of nonpregnant and pregnant pigs. Biol Reprod 1995; 53:1339-1344.
    • (1995) Biol Reprod , vol.53 , pp. 1339-1344
    • Hehnke-Vagnoni, K.E.1    Clark, C.L.2    Taylor, M.J.3    Ford, S.P.4
  • 45
    • 0027527682 scopus 로고
    • Vascular development and heparin-binding growth factors in the bovine corpus luteum at several stages of the estrous cycle
    • Zheng J, Redmer DA, Reynolds LP. Vascular development and heparin-binding growth factors in the bovine corpus luteum at several stages of the estrous cycle. Biol Reprod 1993; 49:1177-1189.
    • (1993) Biol Reprod , vol.49 , pp. 1177-1189
    • Zheng, J.1    Redmer, D.A.2    Reynolds, L.P.3
  • 46
    • 0022843442 scopus 로고
    • Morphometric analysis of cell types in the ovine corpus luteum throughcut the estrous cycle
    • Farin CE, Moeller CL, Sawyer HR, Gamboni F, Niswender GD. Morphometric analysis of cell types in the ovine corpus luteum throughcut the estrous cycle. Biol Reprod 1986; 35:1299-1308.
    • (1986) Biol Reprod , vol.35 , pp. 1299-1308
    • Farin, C.E.1    Moeller, C.L.2    Sawyer, H.R.3    Gamboni, F.4    Niswender, G.D.5
  • 47
    • 0023905993 scopus 로고
    • Tumor necrosis factor (TNF-α) production and localization of macrophages and T lymphocytes in the rabbit corpus luteum
    • Bagavandoss P, Kunkel SL, Wiggins RC, Keyes PL. Tumor necrosis factor (TNF-α) production and localization of macrophages and T lymphocytes in the rabbit corpus luteum. Endocrinology 1988; 122: 1185-1187.
    • (1988) Endocrinology , vol.122 , pp. 1185-1187
    • Bagavandoss, P.1    Kunkel, S.L.2    Wiggins, R.C.3    Keyes, P.L.4
  • 48
    • 0031794472 scopus 로고    scopus 로고
    • Macrophages are the major source of tumor necrosis factor α in the porcine corpus luteum
    • Zhao Y, Burbach JA, Roby KF, Terranova PF, Brannian JD. Macrophages are the major source of tumor necrosis factor α in the porcine corpus luteum. Biol Reprod 1998; 59:1385-1391.
    • (1998) Biol Reprod , vol.59 , pp. 1385-1391
    • Zhao, Y.1    Burbach, J.A.2    Roby, K.F.3    Terranova, P.F.4    Brannian, J.D.5
  • 49
    • 0028924986 scopus 로고
    • Class II transactivator regulates the expression of multiple genes involved in antigen presentation
    • Chang CH, Flavell RA. Class II transactivator regulates the expression of multiple genes involved in antigen presentation. J Exp Med 1995; 181:765-767.
    • (1995) J Exp Med , vol.181 , pp. 765-767
    • Chang, C.H.1    Flavell, R.A.2
  • 50
    • 0032719226 scopus 로고    scopus 로고
    • The class II transactivator CIITA is a transcriptional integrator
    • Fontes JD, Kanazawa S, Nekrep N, Peterlin BM. The class II transactivator CIITA is a transcriptional integrator. Microbes Infect 1999; 1:863-869.
    • (1999) Microbes Infect , vol.1 , pp. 863-869
    • Fontes, J.D.1    Kanazawa, S.2    Nekrep, N.3    Peterlin, B.M.4


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