메뉴 건너뛰기




Volumn , Issue 5, 2012, Pages 51-59

Potential role of histamine releasing factor (HRF) as a therapeutic target for treating asthma and allergy

Author keywords

Human basophils; Human eosinophils; Inducible transgenic mouse; Interleukin 13; Interleukin 4; Translationally controlled tumor protein (TCTP)

Indexed keywords

DOXYCYCLINE; HISTAMINE DERIVATIVE; HISTAMINE RELEASING AGENT; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; INOSITOL 1 PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; TETRACYCLINE; TRANSLATIONALLY CONTROLLED TUMOR PROTEIN; TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84874785758     PISSN: 11786965     EISSN: None     Source Type: Journal    
DOI: 10.2147/JAA.S28868     Document Type: Review
Times cited : (25)

References (80)
  • 1
    • 0020965728 scopus 로고
    • Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide
    • Yenofsky R, Cereghini S, Krowczynska A, Brawerman G. Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide. Mol Cell Biol. 1983;3(7): 1197-1203.
    • (1983) Mol Cell Biol. , vol.3 , Issue.7 , pp. 1197-1203
    • Yenofsky, R.1    Cereghini, S.2    Krowczynska, A.3    Brawerman, G.4
  • 2
    • 0024296531 scopus 로고
    • Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells
    • Chitpatima ST, Makrides S, Bandyopadhyay R, Brawerman G. Nucleotide sequence of a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells. Nucleic Acids Res. 1988;16(5):2350.
    • (1988) Nucleic Acids Res. , vol.16 , Issue.5 , pp. 2350
    • Chitpatima, S.T.1    Makrides, S.2    Bandyopadhyay, R.3    Brawerman, G.4
  • 4
    • 0028982775 scopus 로고
    • Molecular identification of an IgE-dependent histamine releasing factor
    • MacDonald SM, Rafnar T, Langdon J, Lichtenstein LM. Molecular identification of an IgE-dependent histamine releasing factor. Science. 1995;269(5224):688-690.
    • (1995) Science. , vol.269 , Issue.5224 , pp. 688-690
    • McDonald, S.M.1    Rafnar, T.2    Langdon, J.3    Lichtenstein, L.M.4
  • 5
    • 0035845430 scopus 로고    scopus 로고
    • Immune mimicry in malaria: Plasmodium falciparum secretes a functional histamine-releasing factor homolog in vitro and in vivo
    • MacDonald SM, Bhisutthibhan J, Shapiro TA, etal. Immune mimicry in malaria: Plasmodium falciparum secretes a functional histamine-releasing factor homolog in vitro and in vivo. Proc Natl Acad Sci U S A. 2001;98(19):10829-10832.
    • (2001) Proc Natl Acad Sci U S A. , vol.98 , Issue.19 , pp. 10829-10832
    • McDonald, S.M.1    Bhisutthibhan, J.2    Shapiro, T.A.3
  • 6
    • 0037197743 scopus 로고    scopus 로고
    • Molecular characterization of a calcium binding translationally controlled tumor protein homologue from the filarial parasites Brugia malayi and Wuchereria bancrofti
    • Gnanasekar M, Rao KV, Chen L, etal. Molecular characterization of a calcium binding translationally controlled tumor protein homologue from the filarial parasites Brugia malayi and Wuchereria bancrofti. Mol Biochem Parasitol. 2002;121(1):107-118.
    • (2002) Mol Biochem Parasitol. , vol.121 , Issue.1 , pp. 107-118
    • Gnanasekar, M.1    Rao, K.V.2    Chen, L.3
  • 7
    • 0037163041 scopus 로고    scopus 로고
    • Cloning and characterization of a calcium-binding histamine-releasing protein from Schistosoma mansoni
    • Rao KV, Chen L, Gnanasekar M, Ramaswamy K. Cloning and characterization of a calcium-binding histamine-releasing protein from Schistosoma mansoni. J Biol Chem. 2002;277(34):31207-31213.
    • (2002) J Biol Chem. , vol.277 , Issue.34 , pp. 31207-31213
    • Rao, K.V.1    Chen, L.2    Gnanasekar, M.3    Ramaswamy, K.4
  • 8
    • 1842578213 scopus 로고    scopus 로고
    • Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta)
    • Langdon JM, Vonakis BM, MacDonald SM. Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta). Biochem Biophys Acta. 2004;1688(3):232-236.
    • (2004) Biochem Biophys Acta. , vol.1688 , Issue.3 , pp. 232-236
    • Langdon, J.M.1    Vonakis, B.M.2    McDonald, S.M.3
  • 9
    • 10744220545 scopus 로고    scopus 로고
    • Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A
    • Cans C, Passer BJ, Shalak V, etal. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Proc Natl Acad Sci U S A. 2003;100(24):13892-13897.
    • (2003) Proc Natl Acad Sci U S A. , vol.100 , Issue.24 , pp. 13892-13897
    • Cans, C.1    Passer, B.J.2    Shalak, V.3
  • 10
    • 8544232810 scopus 로고    scopus 로고
    • TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway
    • Amzallag N, Passer BJ, Allanic D, etal. TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway. J Biol Chem. 2004;279(44):46104-46112.
    • (2004) J Biol Chem. , vol.279 , Issue.44 , pp. 46104-46112
    • Amzallag, N.1    Passer, B.J.2    Allanic, D.3
  • 11
    • 0035823573 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-induced adipose-related protein (TIARP), a cell-surface that is highly induced by tumor necrosis factor-alpha and adipose conversion
    • Moldes M, Lasnier F, Gauthereau X, etal. Tumor necrosis factor-alpha-induced adipose-related protein (TIARP), a cell-surface that is highly induced by tumor necrosis factor-alpha and adipose conversion. J Biol Chem. 2001;276(36):33938-33946.
    • (2001) J Biol Chem. , vol.276 , Issue.36 , pp. 33938-33946
    • Moldes, M.1    Lasnier, F.2    Gauthereau, X.3
  • 12
    • 0037184098 scopus 로고    scopus 로고
    • Molecular cloning and characterization of STAMP1, a highly prostate-specific six transmembrane protein that is overexpressed in prostate cancer
    • Korkmaz KS, Elbi C, Korkmaz CG, Loda M, Hager GL, Saatcioglu F. Molecular cloning and characterization of STAMP1, a highly prostate-specific six transmembrane protein that is overexpressed in prostate cancer. J Biol Chem. 2002;277(39):36689-36696.
    • (2002) J Biol Chem. , vol.277 , Issue.39 , pp. 36689-36696
    • Korkmaz, K.S.1    Elbi, C.2    Korkmaz, C.G.3    Loda, M.4    Hager, G.L.5    Saatcioglu, F.6
  • 13
    • 0029923419 scopus 로고    scopus 로고
    • An immunoglobulin E-dependent recombinant histamine releasing factor induces IL-4 secretion from human basophils
    • Schroeder JT, Lichtenstein LM, MacDonald SM. An immunoglobulin E-dependent recombinant histamine releasing factor induces IL-4 secretion from human basophils. J Exp Med. 1996;183(3):1265-1270.
    • (1996) J Exp Med. , vol.183 , Issue.3 , pp. 1265-1270
    • Schroeder, J.T.1    Lichtenstein, L.M.2    McDonald, S.M.3
  • 14
    • 0031178801 scopus 로고    scopus 로고
    • Recombinant histamine-releasing factor enhances IgE-dependent IL-4 and IL-13secretion by human basophils
    • Schroeder JT, Lichtenstein LM, MacDonald SM. Recombinant histamine-releasing factor enhances IgE-dependent IL-4 and IL-13secretion by human basophils. J Immunol. 1997;159(1):447-452.
    • (1997) J Immunol. , vol.159 , Issue.1 , pp. 447-452
    • Schroeder, J.T.1    Lichtenstein, L.M.2    McDonald, S.M.3
  • 16
    • 0033060468 scopus 로고    scopus 로고
    • The human recombinant histamine releasing factor: Functional evidence that it does not bind to the IgE molecule
    • Wantke F, MacGlashan DW Jr, Langdon JM, MacDonald SM. The human recombinant histamine releasing factor: functional evidence that it does not bind to the IgE molecule. J Allergy Clin Immunol. 1999;103(4):642-648.
    • (1999) J Allergy Clin Immunol. , vol.103 , Issue.4 , pp. 642-648
    • Wantke, F.1    McGlashan Jr., D.W.2    Langdon, J.M.3    McDonald, S.M.4
  • 17
    • 0034665666 scopus 로고    scopus 로고
    • Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line, AML14-13D10
    • Bheekha-Escura R, MacGlashan DW Jr, Langdon JM, MacDonald SM. Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line, AML14-13D10. Blood. 2000;96(6): 2191-2198.
    • (2000) Blood. , vol.96 , Issue.6 , pp. 2191-2198
    • Bheekha-Escura, R.1    McGlashan Jr., D.W.2    Langdon, J.M.3    McDonald, S.M.4
  • 18
    • 84855444627 scopus 로고    scopus 로고
    • Proinflammatory role of histamine-releasing factor in mouse models of asthma and allergy
    • Kashiwakura J, Ando T, Matsumoto K, etal. Proinflammatory role of histamine-releasing factor in mouse models of asthma and allergy. J Clin Invest. 2012;122(1):218-228.
    • (2012) J Clin Invest. , vol.122 , Issue.1 , pp. 218-228
    • Kashiwakura, J.1    Ando, T.2    Matsumoto, K.3
  • 19
    • 0141955097 scopus 로고    scopus 로고
    • Inhibition of cytokine gene transcription by the human recombinant histamine-releasing factor in human T lymphocytes
    • Vonakis BM, Sora R, Langdon JM, Casolaro V, MacDonald SM. Inhibition of cytokine gene transcription by the human recombinant histamine-releasing factor in human T lymphocytes. J Immunol. 2003;171(7):3742-3750.
    • (2003) J Immunol. , vol.171 , Issue.7 , pp. 3742-3750
    • Vonakis, B.M.1    Sora, R.2    Langdon, J.M.3    Casolaro, V.4    McDonald, S.M.5
  • 20
    • 0343337581 scopus 로고    scopus 로고
    • Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor
    • Kang HS, Lee MJ, Song H, etal. Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor. J Immunol. 2001;166(11):6545-6554.
    • (2001) J Immunol. , vol.166 , Issue.11 , pp. 6545-6554
    • Kang, H.S.1    Lee, M.J.2    Song, H.3
  • 22
    • 0033568290 scopus 로고    scopus 로고
    • Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level
    • Xu A, Bellamy AR, Taylor JA. Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level. Biochem J. 1999;342 Pt 3:683-689.
    • (1999) Biochem J. , vol.342 , Issue.PART 3 , pp. 683-689
    • Xu, A.1    Bellamy, A.R.2    Taylor, J.A.3
  • 23
    • 0032892605 scopus 로고    scopus 로고
    • The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle
    • Gachet Y, Tournier S, Lee M, Lazaris-Karatzas A, Poulton T, Bommer UA. The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J Cell Sci. 1999;112(Pt 8): 1257-1271.
    • (1999) J Cell Sci. , vol.112 , Issue.PART 8 , pp. 1257-1271
    • Gachet, Y.1    Tournier, S.2    Lee, M.3    Lazaris-Karatzas, A.4    Poulton, T.5    Bommer, U.A.6
  • 24
    • 72449155496 scopus 로고    scopus 로고
    • 2-dependent translocation of TCTP into the nucleus enables its interaction with VDR in human keratinocytes: TCTP as a further module in calcitriol signalling
    • 2-dependent translocation of TCTP into the nucleus enables its interaction with VDR in human keratinocytes: TCTP as a further module in calcitriol signalling. J Steroid Biochem Mol Biol. 2010;118(1-2):29-40.
    • (2010) J Steroid Biochem Mol Biol. , vol.118 , Issue.1-2 , pp. 29-40
    • Rid, R.1    Onder, K.2    Trost, A.3
  • 25
    • 77649314475 scopus 로고    scopus 로고
    • Expanding the substantial interactome of NEMO using protein microarrays
    • Fenner BJ, Scannell M, Prehn JH. Expanding the substantial interactome of NEMO using protein microarrays. PLoS One. 2010; 5(1):e8799.
    • (2010) PLoS One. , vol.5 , Issue.1
    • Fenner, B.J.1    Scannell, M.2    Prehn, J.H.3
  • 26
    • 0037020234 scopus 로고    scopus 로고
    • Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and Fortilin. The potential role of MCL1 as a fortilin chaperone
    • Zhang D, Li F, Weidner D, Mnjoyan ZH, Fujise K. Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and Fortilin. The potential role of MCL1 as a fortilin chaperone. J Biol Chem. 2002;277(40):37430-37438.
    • (2002) J Biol Chem. , vol.277 , Issue.40 , pp. 37430-37438
    • Zhang, D.1    Li, F.2    Weidner, D.3    Mnjoyan, Z.H.4    Fujise, K.5
  • 27
    • 23044467160 scopus 로고    scopus 로고
    • An N-terminal region of translationally controlled tumor protein is required for its antiapoptotic activity
    • Yang Y, Yang F, Xiong Z, etal. An N-terminal region of translationally controlled tumor protein is required for its antiapoptotic activity. Oncogene. 2005;24(30):4778-4788.
    • (2005) Oncogene. , vol.24 , Issue.30 , pp. 4778-4788
    • Yang, Y.1    Yang, F.2    Xiong, Z.3
  • 28
    • 2942533913 scopus 로고    scopus 로고
    • Translationally controlled tumor protein (TCTP) in the human prostate and prostate cancer cells: Expression, distribution, and calcium binding activity
    • Arcuri F, Papa S, Carducci A, etal. Translationally controlled tumor protein (TCTP) in the human prostate and prostate cancer cells: expression, distribution, and calcium binding activity. Prostate. 2004;60(2): 130-140.
    • (2004) Prostate. , vol.60 , Issue.2 , pp. 130-140
    • Arcuri, F.1    Papa, S.2    Carducci, A.3
  • 29
    • 0034770925 scopus 로고    scopus 로고
    • Proteomic detection of changes in protein synthesis induced by fibroblast growth factor-2in MCF-7 human breast cancer cells
    • Vercoutter-Edouart AS, Czeszak X, Crépin M, etal. Proteomic detection of changes in protein synthesis induced by fibroblast growth factor-2in MCF-7 human breast cancer cells. Exp Cell Res. 2001;262(1):59-68.
    • (2001) Exp Cell Res. , vol.262 , Issue.1 , pp. 59-68
    • Vercoutter-Edouart, A.S.1    Czeszak, X.2    Crépin, M.3
  • 30
    • 0034637709 scopus 로고    scopus 로고
    • Expression of translationally controlled tumor protein mRNA in human colon cancer
    • Chung S, Kim M, Choi W, Chung J, Lee K. Expression of translationally controlled tumor protein mRNA in human colon cancer. Cancer Lett. 2000;156(2):185-190.
    • (2000) Cancer Lett. , vol.156 , Issue.2 , pp. 185-190
    • Chung, S.1    Kim, M.2    Choi, W.3    Chung, J.4    Lee, K.5
  • 31
    • 7444246058 scopus 로고    scopus 로고
    • Translationally controlled tumor protein is a target of tumor reversion
    • Tuynder M, Fiucci G, Prieur S, etal. Translationally controlled tumor protein is a target of tumor reversion. Proc Natl Acad Sci U S A. 2004;101(43):15364-15369.
    • (2004) Proc Natl Acad Sci U S A. , vol.101 , Issue.43 , pp. 15364-15369
    • Tuynder, M.1    Fiucci, G.2    Prieur, S.3
  • 32
    • 0035861647 scopus 로고    scopus 로고
    • Characterization of fortilin, a novel antiapoptotic protein
    • Li F, Zhang D, Fujise K. Characterization of fortilin, a novel antiapoptotic protein. J Biol Chem. 2001;276(50):47542-47549.
    • (2001) J Biol Chem. , vol.276 , Issue.50 , pp. 47542-47549
    • Li, F.1    Zhang, D.2    Fujise, K.3
  • 33
    • 47249118484 scopus 로고    scopus 로고
    • TCTP protects from apoptotic cell death by antagonizing bax function
    • Susini L, Besse S, Duflaut D, etal. TCTP protects from apoptotic cell death by antagonizing bax function. Cell Death Differ. 2008;15(8): 1211-1220.
    • (2008) Cell Death Differ. , vol.15 , Issue.8 , pp. 1211-1220
    • Susini, L.1    Besse, S.2    Duflaut, D.3
  • 34
    • 78650873411 scopus 로고    scopus 로고
    • Anti-apoptotic protein TCTP controls the stability of the tumor suppressor p53
    • Rho SB, Lee JH, Park MS, etal. Anti-apoptotic protein TCTP controls the stability of the tumor suppressor p53. FEBS Lett. 2011;585(1):29-35.
    • (2011) FEBS Lett. , vol.585 , Issue.1 , pp. 29-35
    • Rho, S.B.1    Lee, J.H.2    Park, M.S.3
  • 35
    • 84855535930 scopus 로고    scopus 로고
    • Reciprocal repression between P53 and TCTP
    • Amson R, Pece S, Lespagnol A, etal. Reciprocal repression between P53 and TCTP. Nat Med. 2011;18(1):91-99.
    • (2011) Nat Med. , vol.18 , Issue.1 , pp. 91-99
    • Amson, R.1    Pece, S.2    Lespagnol, A.3
  • 36
    • 34347391544 scopus 로고    scopus 로고
    • A knockout mouse approach reveals that TCTP functions as an essential factor for cell proliferation and survival in a tissue-or cell type-specific manner
    • Chen SH, Wu PS, Chou CH, etal. A knockout mouse approach reveals that TCTP functions as an essential factor for cell proliferation and survival in a tissue-or cell type-specific manner. Mol Biol Cell. 2007;18(7): 2525-2533.
    • (2007) Mol Biol Cell. , vol.18 , Issue.7 , pp. 2525-2533
    • Chen, S.H.1    Wu, P.S.2    Chou, C.H.3
  • 37
    • 77956217977 scopus 로고    scopus 로고
    • The effects of overespression of histamine releasing factor (HRF) in a transgenic mouse model
    • Yueh-Chiao Y, Xie L, Langdon JM, etal. The effects of overespression of histamine releasing factor (HRF) in a transgenic mouse model. PloS ONE. 2010;5(6):e11077.
    • (2010) PloS ONE. , vol.5 , Issue.6
    • Yueh-Chiao, Y.1    Xie, L.2    Langdon, J.M.3
  • 38
    • 60449083521 scopus 로고    scopus 로고
    • Basophils: Beyond effector cells of allergic inflammation
    • Schroeder JT. Basophils: Beyond effector cells of allergic inflammation. Adv Immunol. 2009;101:123-161.
    • (2009) Adv Immunol. , vol.101 , pp. 123-161
    • Schroeder, J.T.1
  • 39
    • 0025753325 scopus 로고
    • Mouse splenic and bone marrow cell populations that express high-affinity Fc epsilon receptors and produce interleukin 4 are highly enriched in basophils
    • Seder RA, Paul WE, Dvorak AM, etal. Mouse splenic and bone marrow cell populations that express high-affinity Fc epsilon receptors and produce interleukin 4 are highly enriched in basophils. Proc Natl Acad Sci U S A. 1991;88(77):2835-2839.
    • (1991) Proc Natl Acad Sci U S A. , vol.88 , Issue.77 , pp. 2835-2839
    • Seder, R.A.1    Paul, W.E.2    Dvorak, A.M.3
  • 40
    • 36549063557 scopus 로고    scopus 로고
    • Basophils and type 2 immunity
    • Min B, Paul W. Basophils and type 2 immunity. Curr Opin Hematol. 2008;15(1):59-63.
    • (2008) Curr Opin Hematol. , vol.15 , Issue.1 , pp. 59-63
    • Min, B.1    Paul, W.2
  • 41
    • 34547939503 scopus 로고    scopus 로고
    • Basophils are essential initiators of a novel type of chronic allergic inflammation
    • Obata K, Mukai K, Tsujimura Y, etal. Basophils are essential initiators of a novel type of chronic allergic inflammation. Blood. 2007;110(3):913-920.
    • (2007) Blood. , vol.110 , Issue.3 , pp. 913-920
    • Obata, K.1    Mukai, K.2    Tsujimura, Y.3
  • 42
    • 41149176997 scopus 로고    scopus 로고
    • Allergic pulmonary inflammation in mice is dependent on eosinophil-induced recruitment of effector T cells
    • Jacobsen EA, Ochkur SI, Pero RS, etal. Allergic pulmonary inflammation in mice is dependent on eosinophil-induced recruitment of effector T cells. J Exp Med. 2008;205(3):699-710.
    • (2008) J Exp Med. , vol.205 , Issue.3 , pp. 699-710
    • Jacobsen, E.A.1    Ochkur, S.I.2    Pero, R.S.3
  • 43
    • 4544304222 scopus 로고    scopus 로고
    • Defining a link with asthma in mice congenitally deficient in eosinophils
    • Lee JJ, Dimina D, Macias MP, etal. Defining a link with asthma in mice congenitally deficient in eosinophils. Science. 2004;305(5691):1773-1776.
    • (2004) Science. , vol.305 , Issue.5691 , pp. 1773-1776
    • Lee, J.J.1    Dimina, D.2    Macias, M.P.3
  • 44
    • 0037103162 scopus 로고    scopus 로고
    • IgE-dependent mast cell activation potentiates airway responses in murine asthma models
    • Mayr SI, Zuberi RI, Zhang M, etal. IgE-dependent mast cell activation potentiates airway responses in murine asthma models. J Immunol. 2002;169(4):2061-2068.
    • (2002) J Immunol. , vol.169 , Issue.4 , pp. 2061-2068
    • Mayr, S.I.1    Zuberi, R.I.2    Zhang, M.3
  • 48
    • 0033791959 scopus 로고    scopus 로고
    • The tyrosine kinases p563/56lyn and p72syk are differentially expressed at the protein level but not at the messenger RNA level in nonreleasing human basophils
    • Lavens-Phillips SE, MacGlashan DW Jr. The tyrosine kinases p563/56lyn and p72syk are differentially expressed at the protein level but not at the messenger RNA level in nonreleasing human basophils. Am J Respir Cell Mol Biol. 2000;23(4):566-571.
    • (2000) Am J Respir Cell Mol Biol. , vol.23 , Issue.4 , pp. 566-571
    • Lavens-Phillips, S.E.1    McGlashan Jr., D.W.2
  • 49
    • 23844470126 scopus 로고    scopus 로고
    • Acute IL-3 priming up-regulates the stimulus-induced Raf-1-Mek-Erk cascade independently of IL-3-induced activation of Erk
    • Vilariño N, Miura K, MacGlashan DW Jr. Acute IL-3 priming up-regulates the stimulus-induced Raf-1-Mek-Erk cascade independently of IL-3-induced activation of Erk. J Immunol. 2005;175(5): 3006-3014.
    • (2005) J Immunol. , vol.175 , Issue.5 , pp. 3006-3014
    • Vilariño, N.1    Miura, K.2    McGlashan Jr., D.W.3
  • 50
    • 0035179517 scopus 로고    scopus 로고
    • Src homology 2 domain-containing inositol 5' phosphatase is negatively associated with histamine release to human recombinant histamine releasing factor in human basophils
    • Vonakis BM, Gibbons S Jr, Sora R, Langdon JM, MacDonald SM. Src homology 2 domain-containing inositol 5' phosphatase is negatively associated with histamine release to human recombinant histamine releasing factor in human basophils. J Allergy Clin Immunol. 2001;108(5):822-831.
    • (2001) J Allergy Clin Immunol. , vol.108 , Issue.5 , pp. 822-831
    • Vonakis, B.M.1    Gibbons Jr., S.2    Sora, R.3    Langdon, J.M.4    McDonald, S.M.5
  • 51
    • 33846796264 scopus 로고    scopus 로고
    • Basophil FcepsilonRI histamine release parallels expression of Src-homology 2-containing inositol phosphatases in chronic idiopathic urticaria
    • Vonakis BM, Vasagar K, Gibbons SP Jr, etal. Basophil FcepsilonRI histamine release parallels expression of Src-homology 2-containing inositol phosphatases in chronic idiopathic urticaria. J Allergy Clin Immunol. 2007;119(2):441-448.
    • (2007) J Allergy Clin Immunol. , vol.119 , Issue.2 , pp. 441-448
    • Vonakis, B.M.1    Vasagar, K.2    Gibbons Jr., S.P.3
  • 52
    • 0033804532 scopus 로고    scopus 로고
    • Lipid phosphatases in the immune system
    • Krystal G. Lipid phosphatases in the immune system. Immunology. 2000;12(4):397-403.
    • (2000) Immunology. , vol.12 , Issue.4 , pp. 397-403
    • Krystal, G.1
  • 53
    • 0032530195 scopus 로고    scopus 로고
    • The src homology 2 containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation
    • Huber M, Helgason CD, Damen JE, etal. The src homology 2 containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation. Proc Natl Acad Sci U S A. 1998;95(19):11330-11335.
    • (1998) Proc Natl Acad Sci U S A. , vol.95 , Issue.19 , pp. 11330-11335
    • Huber, M.1    Helgason, C.D.2    Damen, J.E.3
  • 55
    • 0032503687 scopus 로고    scopus 로고
    • PtdIns-3,4,5-P3: A regulatory nexus between tyrosine kinases and sustained calcium signals
    • Scharenberg AM, Kinet J-P. PtdIns-3,4,5-P3: a regulatory nexus between tyrosine kinases and sustained calcium signals. Cell. 1998;94(1):5-8.
    • (1998) Cell. , vol.94 , Issue.1 , pp. 5-8
    • Scharenberg, A.M.1    Kinet, J.-P.2
  • 56
    • 0029665083 scopus 로고    scopus 로고
    • p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
    • Lioubin MN, Algate PA, Tsai S, Carlberg K, Aebersold A, Rohrschneider LR. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 1996,10(9): 1084-1095.
    • (1996) Genes Dev. , vol.10 , Issue.9 , pp. 1084-1095
    • Lioubin, M.N.1    Algate, P.A.2    Tsai, S.3    Carlberg, K.4    Aebersold, A.5    Rohrschneider, L.R.6
  • 57
    • 84860316777 scopus 로고    scopus 로고
    • The role of SHIP in the development and activation of mouse mucosal and connective tissue mast cells
    • Ruschmann J, Antignano F, Lam V, etal. The role of SHIP in the development and activation of mouse mucosal and connective tissue mast cells. J Immunol. 2012;188(8):3839-3850.
    • (2012) J Immunol. , vol.188 , Issue.8 , pp. 3839-3850
    • Ruschmann, J.1    Antignano, F.2    Lam, V.3
  • 58
    • 0033812025 scopus 로고    scopus 로고
    • Bilevel control of B-cell activation by the inositol 5-phosphatase SHIP
    • Brauweiler AM, Tamir I, Cambier JC. Bilevel control of B-cell activation by the inositol 5-phosphatase SHIP. Immunol Rev. 2000;176:69-74.
    • (2000) Immunol Rev. , vol.176 , pp. 69-74
    • Brauweiler, A.M.1    Tamir, I.2    Cambier, J.C.3
  • 59
    • 0035892874 scopus 로고    scopus 로고
    • 4 secretion following stimulation of human basophils with anti-IgE antibody
    • 4 secretion following stimulation of human basophils with anti-IgE antibody. J Immunol. 2001;167(12): 7027-7037.
    • (2001) J Immunol. , vol.167 , Issue.12 , pp. 7027-7037
    • Miura, K.1    Lavens-Phillips, S.2    McGlashan Jr, D.W.3
  • 60
    • 41349085369 scopus 로고    scopus 로고
    • Distinct characteristics of signal transduction events by histamine releasing factor/translationally controlled tumor protein (HRF/TCTP)-induced priming and activation of human basophils
    • Vonakis BM, MacGlashan Jr DW, Vilariño N, Langdon JM, Scott RS, MacDonald SM. Distinct characteristics of signal transduction events by histamine releasing factor/translationally controlled tumor protein (HRF/TCTP)-induced priming and activation of human basophils. Blood. 2008;111(4):1789-1796.
    • (2008) Blood. , vol.111 , Issue.4 , pp. 1789-1796
    • Vonakis, B.M.1    McGlashan Jr, D.W.2    Vilariño, N.3    Langdon, J.M.4    Scott, R.S.5    McDonald, S.M.6
  • 61
    • 12944299797 scopus 로고    scopus 로고
    • Transient transfection of human peripheral blood basophils
    • Vilariño N, MacGlashan Jr D. Transient transfection of human peripheral blood basophils. J Immunol Meth. 2005;296(1-2):11-18.
    • (2005) J Immunol Meth. , vol.296 , Issue.1-2 , pp. 11-18
    • Vilariño, N.1    McGlashan Jr, D.2
  • 62
    • 58149151542 scopus 로고    scopus 로고
    • IL-3induces a Pim1-dependent antiapototic pathway in primary human basophils
    • Didichenko SA, Spiegl N, Brunner T, Dahinden CA. IL-3induces a Pim1-dependent antiapototic pathway in primary human basophils. Blood. 2008;112(10):3949-3958.
    • (2008) Blood. , vol.112 , Issue.10 , pp. 3949-3958
    • Didichenko, S.A.1    Spiegl, N.2    Brunner, T.3    Dahinden, C.A.4
  • 63
    • 54249166694 scopus 로고    scopus 로고
    • Histamine-releasing factor/translationally controlled tumor protein (HRF/TCTP)-induced histamine release is enhanced with SHIP-1 knockdown in cultured human mast cell and basophil models
    • Langdon JM, Schroeder JT, Vonakis BM, Bieneman AP, Chichester K, MacDonald SM. Histamine-releasing factor/translationally controlled tumor protein (HRF/TCTP)-induced histamine release is enhanced with SHIP-1 knockdown in cultured human mast cell and basophil models. J Leukoc Biol. 2008;84(4):1151-1158.
    • (2008) J Leukoc Biol. , vol.84 , Issue.4 , pp. 1151-1158
    • Langdon, J.M.1    Schroeder, J.T.2    Vonakis, B.M.3    Bieneman, A.P.4    Chichester, K.5    McDonald, S.M.6
  • 64
    • 0027729893 scopus 로고
    • Abolition of anaphylaxis by targeted disruption of the high affinity immunoglobulin E receptor alpha chain gene
    • Dombrowicz D, Flamand V, Brigman KK, Koller BH, Kinet JP. Abolition of anaphylaxis by targeted disruption of the high affinity immunoglobulin E receptor alpha chain gene. Cell. 1993;75(5):969-976.
    • (1993) Cell. , vol.75 , Issue.5 , pp. 969-976
    • Dombrowicz, D.1    Flamand, V.2    Brigman, K.K.3    Koller, B.H.4    Kinet, J.P.5
  • 66
    • 0033120622 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases regulate leukotriene C4generation, but not histamine release or IL-4 production from human basophils
    • Miura K, Schroeder JT, Hubbard WC, MacGlashan DW Jr. Extracellular signal-regulated kinases regulate leukotriene C4generation, but not histamine release or IL-4 production from human basophils. J Immunol. 1999;162(7):4198-4206.
    • (1999) J Immunol. , vol.162 , Issue.7 , pp. 4198-4206
    • Miura, K.1    Schroeder, J.T.2    Hubbard, W.C.3    McGlashan Jr., D.W.4
  • 68
    • 0011307417 scopus 로고
    • Histamine releasing factors and IgE heterogeneity
    • In: Middleton E, Reed CE, Ellis EF, Adkinson NF, Yunginger JW, Buss WW, editors. 4th Edition
    • MacDonald SM. Histamine releasing factors and IgE heterogeneity. In: Middleton E, Reed CE, Ellis EF, Adkinson NF, Yunginger JW, Buss WW, editors. Allergy: Principles and Practice. 4th Edition, 1993:1-11.
    • (1993) Allergy: Principles and Practice. , pp. 1-11
    • McDonald, S.M.1
  • 69
    • 0021237737 scopus 로고
    • A mononuclear cell derived histamine releasing factor (HRF) in asthmatic patients. Histamine release from basophils in vitro
    • Alam R, Rozniecki J, Salmaj K. A mononuclear cell derived histamine releasing factor (HRF) in asthmatic patients. Histamine release from basophils in vitro. Ann Allergy. 1984;53(1):66-69.
    • (1984) Ann Allergy. , vol.53 , Issue.1 , pp. 66-69
    • Alam, R.1    Rozniecki, J.2    Salmaj, K.3
  • 70
    • 0022020791 scopus 로고
    • A mononuclear cell-derived histamine releasing factor in asthmatic patients. II. Activity in vivo
    • Alam R, Rozniecki J. A mononuclear cell-derived histamine releasing factor in asthmatic patients. II. Activity in vivo. Allergy. 1985;40(2):124-129.
    • (1985) Allergy. , vol.40 , Issue.2 , pp. 124-129
    • Alam, R.1    Rozniecki, J.2
  • 71
    • 0023126652 scopus 로고
    • The magnitude of the spontaneous production of histamine-releasing factor (HRF) by lymphocytes in vitro correlates with the state of bronchial hyperreactivity in patients with asthma
    • Alam R, Kuna P, Rozniecki J, Kuzminska B. The magnitude of the spontaneous production of histamine-releasing factor (HRF) by lymphocytes in vitro correlates with the state of bronchial hyperreactivity in patients with asthma. J Allergy Clin Immunol. 1987;79(1):103-108.
    • (1987) J Allergy Clin Immunol. , vol.79 , Issue.1 , pp. 103-108
    • Alam, R.1    Kuna, P.2    Rozniecki, J.3    Kuzminska, B.4
  • 72
    • 0024409868 scopus 로고
    • Spontaneous release of histamine from basophils and histamine-releasing factor in patients with atopic dermatitis and food hypersensitivity
    • Sampson HA, Broadbent KR, Bernhisel-Broadbent J. Spontaneous release of histamine from basophils and histamine-releasing factor in patients with atopic dermatitis and food hypersensitivity. N Engl J Med. 1989;321(4):228-232.
    • (1989) N Engl J Med. , vol.321 , Issue.4 , pp. 228-232
    • Sampson, H.A.1    Broadbent, K.R.2    Bernhisel-Broadbent, J.3
  • 73
    • 0024513122 scopus 로고
    • The effect of preseasonal immunotherapy on the production of histamine-releasing factor (HRF) by mononuclear cells from patients with seasonal asthma: Results of a double-blind, placebo-controlled, randomized study
    • Kuna P, Alam R, Kuzminska B, Rozniecki J. The effect of preseasonal immunotherapy on the production of histamine-releasing factor (HRF) by mononuclear cells from patients with seasonal asthma: results of a double-blind, placebo-controlled, randomized study. J Allergy Clin Immunol. 1989;83(4):816-882.
    • (1989) J Allergy Clin Immunol. , vol.83 , Issue.4 , pp. 816-882
    • Kuna, P.1    Alam, R.2    Kuzminska, B.3    Rozniecki, J.4
  • 74
    • 0026542103 scopus 로고
    • Allergic rhinitis to ragweed pollen. II. Modulation of histamine-releasing factor production by specific immunotherapy
    • Brunet C, Bédard PM, Lavoie A, Jobin M, Hébert J. Allergic rhinitis to ragweed pollen. II. Modulation of histamine-releasing factor production by specific immunotherapy. J Allergy Clin Immunol. 1992;89(1 Pt 1): 87-94.
    • (1992) J Allergy Clin Immunol. , vol.89 , Issue.1 PART 1 , pp. 87-94
    • Brunet, C.1    Bédard, P.M.2    Lavoie, A.3    Jobin, M.4    Hébert, J.5
  • 75
    • 0030457527 scopus 로고    scopus 로고
    • Histamine-releasing factors
    • MacDonald SM. Histamine-releasing factors. Curr Opi Immunol. 1996;8(6):778-783.
    • (1996) Curr Opi Immunol. , vol.8 , Issue.6 , pp. 778-783
    • McDonald, S.M.1
  • 76
    • 33847472382 scopus 로고
    • Atopics translate mRNA for the IgE-dependent histamine releasing factor (HRF) more effectively than normal
    • (Abstract)
    • Langdon J, Anders K, Lichtenstein LM, MacDonald SM. Atopics translate mRNA for the IgE-dependent histamine releasing factor (HRF) more effectively than normal. J Allergy Clin Immunol. 1995;95:336 (Abstract).
    • (1995) J Allergy Clin Immunol. , vol.95 , pp. 336
    • Langdon, J.1    Anders, K.2    Lichtenstein, L.M.3    McDonald, S.M.4
  • 77
    • 85034836990 scopus 로고    scopus 로고
    • Histamine releasing factor (HRF) in asthma and atopic dermatitis
    • (Abstract)
    • Ando T, Kashiwakura J, Kawakami Y, Kawakami T. Histamine releasing factor (HRF) in asthma and atopic dermatitis. J Immunol. 2012; 188:177.16 (Abstract).
    • (2012) J Immunol. , vol.188
    • Ando, T.1    Kashiwakura, J.2    Kawakami, Y.3    Kawakami, T.4
  • 78
    • 34548330713 scopus 로고    scopus 로고
    • Small-molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells
    • Ong CJ, Ming-Lum A, Nodwell M, etal. Small-molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells. Blood. 2007;110(6):1942-1949.
    • (2007) Blood. , vol.110 , Issue.6 , pp. 1942-1949
    • Ong, C.J.1    Ming-Lum, A.2    Nodwell, M.3
  • 80
    • 84861909634 scopus 로고    scopus 로고
    • Histamine releasing factor/translational controlled tumor protein: History, functions and clinical implications
    • MacDonald SM. Histamine releasing factor/translational controlled tumor protein: history, functions and clinical implications. Open Allergy Journal. 2012;5:12-18.
    • (2012) Open Allergy Journal. , vol.5 , pp. 12-18
    • McDonald, S.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.