메뉴 건너뛰기




Volumn 27, Issue 3, 2011, Pages 115-122

Extracellular Trypanosoma cruzi calreticulin in the host-parasite interplay

Author keywords

[No Author keywords available]

Indexed keywords

CALRETICULIN; COMPLEMENT COMPONENT C1; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; COMPLEMENT COMPONENT C4; DECAY ACCELERATING FACTOR;

EID: 79952102948     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2010.12.007     Document Type: Review
Times cited : (38)

References (78)
  • 1
    • 77954187759 scopus 로고    scopus 로고
    • Chagas disease: a new worldwide challenge
    • Rodrigues J., Albajar P. Chagas disease: a new worldwide challenge. Nature 2010, 465:S6-S7.
    • (2010) Nature , vol.465
    • Rodrigues, J.1    Albajar, P.2
  • 2
    • 77954199627 scopus 로고    scopus 로고
    • Chagas disease 101
    • Clayton J. Chagas disease 101. Nature 2010, 465:S4-S5.
    • (2010) Nature , vol.465
    • Clayton, J.1
  • 3
    • 77954207000 scopus 로고    scopus 로고
    • Chagas disease: pushing through the pipeline
    • Clayton J. Chagas disease: pushing through the pipeline. Nature 2010, 465:S12-S15.
    • (2010) Nature , vol.465
    • Clayton, J.1
  • 4
    • 0026072168 scopus 로고
    • Characterization of a Trypanosoma cruzi C3 binding protein with functional and genetic similarities to the human complement regulatory protein, decay-accelerating factor
    • Norris K.A., et al. Characterization of a Trypanosoma cruzi C3 binding protein with functional and genetic similarities to the human complement regulatory protein, decay-accelerating factor. J. Immunol. 1991, 147:2240-2247.
    • (1991) J. Immunol. , vol.147 , pp. 2240-2247
    • Norris, K.A.1
  • 5
    • 0028011930 scopus 로고
    • Biochemical analysis of the membrane and soluble forms of the complement regulatory protein of Trypanosoma cruzi
    • Norris K.A., Schrimpf J.E. Biochemical analysis of the membrane and soluble forms of the complement regulatory protein of Trypanosoma cruzi. Infect. Immun. 1994, 62:236-243.
    • (1994) Infect. Immun. , vol.62 , pp. 236-243
    • Norris, K.A.1    Schrimpf, J.E.2
  • 6
    • 0025314311 scopus 로고
    • Discrimination between activators and nonactivators of the alternative pathway of complement: regulation via a sialic acid/polyanion binding site on factor H
    • Meri S., Pangburn M.K. Discrimination between activators and nonactivators of the alternative pathway of complement: regulation via a sialic acid/polyanion binding site on factor H. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:3982-3986.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3982-3986
    • Meri, S.1    Pangburn, M.K.2
  • 7
    • 0032171720 scopus 로고    scopus 로고
    • Natural Human Immunity to Trypanosomes
    • Tomlinson S., Raper J. Natural Human Immunity to Trypanosomes. Parasitol. Today 1998, 14:354-359.
    • (1998) Parasitol. Today , vol.14 , pp. 354-359
    • Tomlinson, S.1    Raper, J.2
  • 8
    • 1342303386 scopus 로고    scopus 로고
    • The classical activation pathway of the human complement system is specifically inhibited by calreticulin from Trypanosoma cruzi
    • Ferreira V., et al. The classical activation pathway of the human complement system is specifically inhibited by calreticulin from Trypanosoma cruzi. J. Immunol. 2004, 172:3042-3050.
    • (2004) J. Immunol. , vol.172 , pp. 3042-3050
    • Ferreira, V.1
  • 9
    • 77957923202 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor effects of Trypanosoma cruzi Calreticulin
    • López N.C., et al. Antiangiogenic and antitumor effects of Trypanosoma cruzi Calreticulin. PLoS Negl. Trop. Dis. 2010, 4:e730.
    • (2010) PLoS Negl. Trop. Dis. , vol.4
    • López, N.C.1
  • 10
    • 0030139652 scopus 로고    scopus 로고
    • Presence of calreticulin in vector fleas (Siphonaptera)
    • Jaworski D.C., et al. Presence of calreticulin in vector fleas (Siphonaptera). J. Med. Entomol. 1996, 33:482-489.
    • (1996) J. Med. Entomol. , vol.33 , pp. 482-489
    • Jaworski, D.C.1
  • 11
    • 0035078139 scopus 로고    scopus 로고
    • A calreticulin-like molecule from the human hookworm Necator americanus interacts with C1q and the cytoplasmic signalling domains of some integrins
    • Kasper G., et al. A calreticulin-like molecule from the human hookworm Necator americanus interacts with C1q and the cytoplasmic signalling domains of some integrins. Parasite Immunol. 2001, 23:141-152.
    • (2001) Parasite Immunol. , vol.23 , pp. 141-152
    • Kasper, G.1
  • 12
    • 0032918454 scopus 로고    scopus 로고
    • Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins
    • Labriola C., et al. Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins. Mol. Biol. Cell 1999, 10:1381-1394.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1381-1394
    • Labriola, C.1
  • 13
    • 0141521671 scopus 로고    scopus 로고
    • The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum
    • Conte I., et al. The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum. Mol. Biol. Cell 2003, 14:3529-3540.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3529-3540
    • Conte, I.1
  • 14
    • 60949092870 scopus 로고    scopus 로고
    • Trypanosoma cruzi calreticulin: a possible role in Chagas' disease autoimmunity
    • Ribeiro C.H., et al. Trypanosoma cruzi calreticulin: a possible role in Chagas' disease autoimmunity. Mol. Immunol. 2009, 46:1092-1099.
    • (2009) Mol. Immunol. , vol.46 , pp. 1092-1099
    • Ribeiro, C.H.1
  • 15
    • 12944251185 scopus 로고    scopus 로고
    • Immunocytochemical localisation of calreticulin in Trypanosoma cruzi
    • Souto-Padron T., et al. Immunocytochemical localisation of calreticulin in Trypanosoma cruzi. Histochem. Cell Biol. 2004, 122:563-569.
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 563-569
    • Souto-Padron, T.1
  • 16
    • 0031459567 scopus 로고    scopus 로고
    • The C1q and collectin binding site within C1q receptor (cell surface calreticulin)
    • Stuart G.R., et al. The C1q and collectin binding site within C1q receptor (cell surface calreticulin). Immunopharmacology 1997, 38:73-80.
    • (1997) Immunopharmacology , vol.38 , pp. 73-80
    • Stuart, G.R.1
  • 17
    • 0030592735 scopus 로고    scopus 로고
    • Localisation of the C1q binding site within C1q receptor/calreticulin
    • Stuart G.R., et al. Localisation of the C1q binding site within C1q receptor/calreticulin. FEBS Lett. 1996, 397:245-249.
    • (1996) FEBS Lett. , vol.397 , pp. 245-249
    • Stuart, G.R.1
  • 18
    • 15044359599 scopus 로고    scopus 로고
    • Does Trypanosoma cruzi calreticulin modulate the complement system and angiogenesis?
    • Ferreira V., et al. Does Trypanosoma cruzi calreticulin modulate the complement system and angiogenesis?. Trends Parasitol. 2005, 21:169-174.
    • (2005) Trends Parasitol. , vol.21 , pp. 169-174
    • Ferreira, V.1
  • 19
    • 1142285366 scopus 로고    scopus 로고
    • Role of calreticulin from parasites in its interaction with vertebrate hosts
    • Ferreira V., et al. Role of calreticulin from parasites in its interaction with vertebrate hosts. Mol. Immunol. 2004, 40:1279-1291.
    • (2004) Mol. Immunol. , vol.40 , pp. 1279-1291
    • Ferreira, V.1
  • 20
    • 77950610010 scopus 로고    scopus 로고
    • Molecular mechanisms involved in the inactivation of the first component of human complement by Trypanosoma cruzi calreticulin
    • Valck C., et al. Molecular mechanisms involved in the inactivation of the first component of human complement by Trypanosoma cruzi calreticulin. Mol. Immunol. 2010, 47:1516-1521.
    • (2010) Mol. Immunol. , vol.47 , pp. 1516-1521
    • Valck, C.1
  • 21
    • 68049129553 scopus 로고    scopus 로고
    • Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions
    • Gal P., et al. Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions. Mol. Immunol. 2009, 46:2745-2752.
    • (2009) Mol. Immunol. , vol.46 , pp. 2745-2752
    • Gal, P.1
  • 22
    • 70350041296 scopus 로고    scopus 로고
    • Paths reunited: Initiation of the classical and lectin pathways of complement activation
    • Wallis R., et al. Paths reunited: Initiation of the classical and lectin pathways of complement activation. Immunobiology 2010, 215:1-11.
    • (2010) Immunobiology , vol.215 , pp. 1-11
    • Wallis, R.1
  • 23
    • 48549093708 scopus 로고    scopus 로고
    • Calcineurin B of the human protozoan parasite Trypanosoma cruzi is involved in cell invasion
    • Araya J.E., et al. Calcineurin B of the human protozoan parasite Trypanosoma cruzi is involved in cell invasion. Microbes Infect. 2008, 10:892-900.
    • (2008) Microbes Infect. , vol.10 , pp. 892-900
    • Araya, J.E.1
  • 24
    • 46249124859 scopus 로고    scopus 로고
    • Trypanosoma cruzi: parasite and host cell signaling during the invasion process
    • Yoshida N., Cortez M. Trypanosoma cruzi: parasite and host cell signaling during the invasion process. Subcell. Biochem. 2008, 47:82-91.
    • (2008) Subcell. Biochem. , vol.47 , pp. 82-91
    • Yoshida, N.1    Cortez, M.2
  • 25
    • 0024851557 scopus 로고
    • Complement component C1q enhances invasion of human mononuclear phagocytes and fibroblasts by Trypanosoma cruzi trypomastigotes
    • Rimoldi M.T., et al. Complement component C1q enhances invasion of human mononuclear phagocytes and fibroblasts by Trypanosoma cruzi trypomastigotes. J. Clin. Invest. 1989, 84:1982-1989.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1982-1989
    • Rimoldi, M.T.1
  • 26
    • 78649498983 scopus 로고    scopus 로고
    • Trypanosoma cruzi calreticulin: A novel virulence factor that binds complement C1 on the parasite surface and promotes infectivity
    • Ramirez G., et al. Trypanosoma cruzi calreticulin: A novel virulence factor that binds complement C1 on the parasite surface and promotes infectivity. Immunobiology 2010, 216:265-273.
    • (2010) Immunobiology , vol.216 , pp. 265-273
    • Ramirez, G.1
  • 27
    • 33846057130 scopus 로고    scopus 로고
    • Calreticulin exposure dictates the immunogenicity of cancer cell death
    • Obeid M., et al. Calreticulin exposure dictates the immunogenicity of cancer cell death. Nat. Med. 2007, 13:54-61.
    • (2007) Nat. Med. , vol.13 , pp. 54-61
    • Obeid, M.1
  • 28
    • 27544473700 scopus 로고    scopus 로고
    • F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement
    • Aguilar L., et al. F(ab')2 antibody fragments against Trypanosoma cruzi calreticulin inhibit its interaction with the first component of human complement. Biol. Res. 2005, 38:187-195.
    • (2005) Biol. Res. , vol.38 , pp. 187-195
    • Aguilar, L.1
  • 29
    • 0034738015 scopus 로고    scopus 로고
    • Development of an immunoenzymatic assay for the detection of human antibodies against Trypanosoma cruzi calreticulin, an immunodominant antigen
    • Marcelain K., et al. Development of an immunoenzymatic assay for the detection of human antibodies against Trypanosoma cruzi calreticulin, an immunodominant antigen. Acta Trop. 2000, 75:291-300.
    • (2000) Acta Trop. , vol.75 , pp. 291-300
    • Marcelain, K.1
  • 30
    • 0026657624 scopus 로고
    • Human antibody effector function
    • Burton D.R., Woof J.M. Human antibody effector function. Adv. Immunol. 1992, 51:1-84.
    • (1992) Adv. Immunol. , vol.51 , pp. 1-84
    • Burton, D.R.1    Woof, J.M.2
  • 31
    • 0027982403 scopus 로고
    • Residue at position 331 in the IgG1 and IgG4 CH2 domains contributes to their differential ability to bind and activate complement
    • Xu Y., et al. Residue at position 331 in the IgG1 and IgG4 CH2 domains contributes to their differential ability to bind and activate complement. J. Biol. Chem. 1994, 269:3469-3474.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3469-3474
    • Xu, Y.1
  • 32
    • 0036785658 scopus 로고    scopus 로고
    • Genetic immunization elicits antigen-specific protective immune responses and decreases disease severity in Trypanosoma cruzi infection
    • Garg N., Tarleton R.L. Genetic immunization elicits antigen-specific protective immune responses and decreases disease severity in Trypanosoma cruzi infection. Infect. Immun. 2002, 70:5547-5555.
    • (2002) Infect. Immun. , vol.70 , pp. 5547-5555
    • Garg, N.1    Tarleton, R.L.2
  • 33
    • 0036144369 scopus 로고    scopus 로고
    • Laminin binding to the calreticulin fragment vasostatin regulates endothelial cell function
    • Yao L., et al. Laminin binding to the calreticulin fragment vasostatin regulates endothelial cell function. J. Leukoc. Biol. 2002, 71:47-53.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 47-53
    • Yao, L.1
  • 34
    • 0032445492 scopus 로고    scopus 로고
    • Vasostatin, a calreticulin fragment, inhibits angiogenesis and suppresses tumor growth
    • Pike S.E., et al. Vasostatin, a calreticulin fragment, inhibits angiogenesis and suppresses tumor growth. J. Exp. Med. 1998, 188:2349-2356.
    • (1998) J. Exp. Med. , vol.188 , pp. 2349-2356
    • Pike, S.E.1
  • 35
    • 0033214331 scopus 로고    scopus 로고
    • Calreticulin and calreticulin fragments are endothelial cell inhibitors that suppress tumor growth
    • Pike S.E., et al. Calreticulin and calreticulin fragments are endothelial cell inhibitors that suppress tumor growth. Blood 1999, 94:2461-2468.
    • (1999) Blood , vol.94 , pp. 2461-2468
    • Pike, S.E.1
  • 36
    • 39049165759 scopus 로고    scopus 로고
    • Suppression of lung tumor growth and metastasis in mice by adeno-associated virus-mediated expression of vasostatin
    • Cai K.X., et al. Suppression of lung tumor growth and metastasis in mice by adeno-associated virus-mediated expression of vasostatin. Clin. Cancer Res. 2008, 14:939-949.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 939-949
    • Cai, K.X.1
  • 37
    • 33947610389 scopus 로고    scopus 로고
    • Combination of vasostatin and cyclophosphamide in the therapy of murine melanoma tumors
    • Jazowiecka-Rakus J., et al. Combination of vasostatin and cyclophosphamide in the therapy of murine melanoma tumors. Acta Biochim. Pol. 2007, 54:125-133.
    • (2007) Acta Biochim. Pol. , vol.54 , pp. 125-133
    • Jazowiecka-Rakus, J.1
  • 38
    • 0036036415 scopus 로고    scopus 로고
    • Anti-tumor activities of the angiogenesis inhibitors interferon-inducible protein-10 and the calreticulin fragment vasostatin
    • Yao L., et al. Anti-tumor activities of the angiogenesis inhibitors interferon-inducible protein-10 and the calreticulin fragment vasostatin. Cancer Immunol. Immunother. 2002, 51:358-366.
    • (2002) Cancer Immunol. Immunother. , vol.51 , pp. 358-366
    • Yao, L.1
  • 39
    • 0035348952 scopus 로고    scopus 로고
    • Anticancer properties of flagellate protozoan Trypanosoma cruzi Chagas, 1909
    • Kallinikova V.D., et al. Anticancer properties of flagellate protozoan Trypanosoma cruzi Chagas, 1909. Izv. Akad. Nauk Ser. Biol. 2001, 299-311.
    • (2001) Izv. Akad. Nauk Ser. Biol. , pp. 299-311
    • Kallinikova, V.D.1
  • 40
    • 0035033558 scopus 로고    scopus 로고
    • Chronic Trypanosoma cruzi infection associated with low incidence of 1,2-dimethylhydrazine-induced colon cancer in rats
    • Oliveira E.C., et al. Chronic Trypanosoma cruzi infection associated with low incidence of 1,2-dimethylhydrazine-induced colon cancer in rats. Carcinogenesis 2001, 22:737-740.
    • (2001) Carcinogenesis , vol.22 , pp. 737-740
    • Oliveira, E.C.1
  • 41
    • 0037131396 scopus 로고    scopus 로고
    • SREC-II, a new member of the scavenger receptor type F family, trans-interacts with SREC-I through its extracellular domain
    • Ishii J., et al. SREC-II, a new member of the scavenger receptor type F family, trans-interacts with SREC-I through its extracellular domain. J. Biol. Chem. 2002, 277:39696-39702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39696-39702
    • Ishii, J.1
  • 42
    • 36148970014 scopus 로고    scopus 로고
    • Inhibition of Lewis lung carcinoma growth by Toxoplasma gondii through induction of Th1 immune responses and inhibition of angiogenesis
    • Kim J.O., et al. Inhibition of Lewis lung carcinoma growth by Toxoplasma gondii through induction of Th1 immune responses and inhibition of angiogenesis. J. Korean Med. Sci. 2007, 22(Suppl.):S38-S46.
    • (2007) J. Korean Med. Sci. , vol.22 , Issue.SUPPL.
    • Kim, J.O.1
  • 43
    • 0034016499 scopus 로고    scopus 로고
    • The tumoricidal effect of Trypanosoma cruzi: its intracellular cycle and the immune response of the host
    • Cabral H.R. The tumoricidal effect of Trypanosoma cruzi: its intracellular cycle and the immune response of the host. Med. Hypotheses 2000, 54:1-6.
    • (2000) Med. Hypotheses , vol.54 , pp. 1-6
    • Cabral, H.R.1
  • 44
    • 0009798186 scopus 로고
    • Trypanosoma cruzi Endotoxin (KR) in the Treatment of Malignant Mouse Tumors
    • Hauschka T.S., Goodwin M.B. Trypanosoma cruzi Endotoxin (KR) in the Treatment of Malignant Mouse Tumors. Science 1948, 107:600-602.
    • (1948) Science , vol.107 , pp. 600-602
    • Hauschka, T.S.1    Goodwin, M.B.2
  • 45
    • 0037233190 scopus 로고    scopus 로고
    • Angiogenesis assays: a critical overview
    • Auerbach R., et al. Angiogenesis assays: a critical overview. Clin. Chem. 2003, 49:32-40.
    • (2003) Clin. Chem. , vol.49 , pp. 32-40
    • Auerbach, R.1
  • 46
    • 77957923202 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor effects of Trypanosoma cruzi Calreticulin
    • Lopez N.C., et al. Antiangiogenic and antitumor effects of Trypanosoma cruzi Calreticulin. PLoS Negl. Trop. Dis. 2010, 4:e730.
    • (2010) PLoS Negl. Trop. Dis. , vol.4
    • Lopez, N.C.1
  • 47
    • 0030978516 scopus 로고    scopus 로고
    • Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion
    • Coppolino M.G., et al. Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature 1997, 386:843-847.
    • (1997) Nature , vol.386 , pp. 843-847
    • Coppolino, M.G.1
  • 48
    • 0033562951 scopus 로고    scopus 로고
    • Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/dephosphorylation events
    • Coppolino M.G., Dedhar S. Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/dephosphorylation events. Biochem. J. 1999, 340(Pt 1):41-50.
    • (1999) Biochem. J. , vol.340 , Issue.PART 1 , pp. 41-50
    • Coppolino, M.G.1    Dedhar, S.2
  • 49
    • 8844244745 scopus 로고    scopus 로고
    • Anti-angiogenic activity of inositol hexaphosphate (IP6)
    • Vucenik I., et al. Anti-angiogenic activity of inositol hexaphosphate (IP6). Carcinogenesis 2004, 25:2115-2123.
    • (2004) Carcinogenesis , vol.25 , pp. 2115-2123
    • Vucenik, I.1
  • 50
    • 29044449005 scopus 로고    scopus 로고
    • Suppression of choroidal neovascularization by intramuscular polymer-based gene delivery of vasostatin
    • Sheu S.J., et al. Suppression of choroidal neovascularization by intramuscular polymer-based gene delivery of vasostatin. Exp. Eye Res. 2005, 81:673-679.
    • (2005) Exp. Eye Res. , vol.81 , pp. 673-679
    • Sheu, S.J.1
  • 51
    • 30944439067 scopus 로고    scopus 로고
    • Treatment of pancreatic carcinoma by adenoviral mediated gene transfer of vasostatin in mice
    • Li L., et al. Treatment of pancreatic carcinoma by adenoviral mediated gene transfer of vasostatin in mice. Gut 2006, 55:259-265.
    • (2006) Gut , vol.55 , pp. 259-265
    • Li, L.1
  • 52
    • 10944228434 scopus 로고    scopus 로고
    • SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin
    • Berwin B., et al. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J. Biol. Chem. 2004, 279:51250-51257.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51250-51257
    • Berwin, B.1
  • 53
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin B., et al. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J. 2003, 22:6127-6136.
    • (2003) EMBO J. , vol.22 , pp. 6127-6136
    • Berwin, B.1
  • 54
    • 0038107402 scopus 로고    scopus 로고
    • The heat shock protein Gp96 binds to human neutrophils and monocytes and stimulates effector functions
    • Radsak M.P., et al. The heat shock protein Gp96 binds to human neutrophils and monocytes and stimulates effector functions. Blood 2003, 101:2810-2815.
    • (2003) Blood , vol.101 , pp. 2810-2815
    • Radsak, M.P.1
  • 55
    • 0031451332 scopus 로고    scopus 로고
    • Expression cloning of a novel scavenger receptor from human endothelial cells
    • Adachi H., et al. Expression cloning of a novel scavenger receptor from human endothelial cells. J. Biol. Chem. 1997, 272:31217-31220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31217-31220
    • Adachi, H.1
  • 56
    • 20044363605 scopus 로고    scopus 로고
    • An in vivo role for Trypanosoma cruzi calreticulin in antiangiogenesis
    • Molina M.C., et al. An in vivo role for Trypanosoma cruzi calreticulin in antiangiogenesis. Mol. Biochem. Parasitol. 2005, 140:133-140.
    • (2005) Mol. Biochem. Parasitol. , vol.140 , pp. 133-140
    • Molina, M.C.1
  • 57
    • 33750491279 scopus 로고    scopus 로고
    • Complement proteins C1q and MBL are pattern recognition molecules that signal immediate and long-term protective immune functions
    • Bohlson S.S., et al. Complement proteins C1q and MBL are pattern recognition molecules that signal immediate and long-term protective immune functions. Mol. Immunol. 2007, 44:33-43.
    • (2007) Mol. Immunol. , vol.44 , pp. 33-43
    • Bohlson, S.S.1
  • 58
    • 77955883153 scopus 로고    scopus 로고
    • Complement: a key system for immune surveillance and homeostasis
    • Ricklin D., et al. Complement: a key system for immune surveillance and homeostasis. Nat. Immunol. 2010, 11:785-797.
    • (2010) Nat. Immunol. , vol.11 , pp. 785-797
    • Ricklin, D.1
  • 59
    • 12244296445 scopus 로고    scopus 로고
    • Structural biology of C1
    • Arlaud G.J., et al. Structural biology of C1. Biochem. Soc. Trans. 2002, 30(Pt 6):1001-1006.
    • (2002) Biochem. Soc. Trans. , vol.30 , Issue.PART 6 , pp. 1001-1006
    • Arlaud, G.J.1
  • 60
    • 5144222255 scopus 로고    scopus 로고
    • Complement: a unique innate immune sensor for danger signals
    • Gasque P. Complement: a unique innate immune sensor for danger signals. Mol. Immunol. 2004, 41:1089-1098.
    • (2004) Mol. Immunol. , vol.41 , pp. 1089-1098
    • Gasque, P.1
  • 61
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak M., et al. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J. 2009, 417:651-666.
    • (2009) Biochem. J. , vol.417 , pp. 651-666
    • Michalak, M.1
  • 62
    • 50549102898 scopus 로고    scopus 로고
    • Immunogenic cancer cell death: a key-lock paradigm
    • Tesniere A., et al. Immunogenic cancer cell death: a key-lock paradigm. Curr. Opin. Immunol. 2008, 20:504-511.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 504-511
    • Tesniere, A.1
  • 63
    • 33748758967 scopus 로고    scopus 로고
    • Overview of the role for calreticulin in the enhancement of wound healing through multiple biological effects
    • Gold L.I., et al. Overview of the role for calreticulin in the enhancement of wound healing through multiple biological effects. J. Invest. Dermatol. Symp. Proc. 2006, 11:57-65.
    • (2006) J. Invest. Dermatol. Symp. Proc. , vol.11 , pp. 57-65
    • Gold, L.I.1
  • 64
    • 51349125733 scopus 로고    scopus 로고
    • Calreticulin enhances porcine wound repair by diverse biological effects
    • Nanney L.B., et al. Calreticulin enhances porcine wound repair by diverse biological effects. Am. J. Pathol. 2008, 173:610-630.
    • (2008) Am. J. Pathol. , vol.173 , pp. 610-630
    • Nanney, L.B.1
  • 65
    • 0035825129 scopus 로고    scopus 로고
    • Calreticulin is a receptor for nuclear export
    • Holaska J.M., et al. Calreticulin is a receptor for nuclear export. J. Cell Biol. 2001, 152:127-140.
    • (2001) J. Cell Biol. , vol.152 , pp. 127-140
    • Holaska, J.M.1
  • 66
    • 0027955571 scopus 로고
    • Modulation of gene expression by calreticulin binding to the glucocorticoid receptor
    • Burns K., et al. Modulation of gene expression by calreticulin binding to the glucocorticoid receptor. Nature 1994, 367:476-480.
    • (1994) Nature , vol.367 , pp. 476-480
    • Burns, K.1
  • 67
    • 0027976780 scopus 로고
    • Inhibition of nuclear hormone receptor activity by calreticulin
    • Dedhar S., et al. Inhibition of nuclear hormone receptor activity by calreticulin. Nature 1994, 367:480-483.
    • (1994) Nature , vol.367 , pp. 480-483
    • Dedhar, S.1
  • 68
    • 0037059518 scopus 로고    scopus 로고
    • Destabilization of AT(1) receptor mRNA by calreticulin
    • Nickenig G., et al. Destabilization of AT(1) receptor mRNA by calreticulin. Circ. Res. 2002, 90:53-58.
    • (2002) Circ. Res. , vol.90 , pp. 53-58
    • Nickenig, G.1
  • 69
    • 0028606112 scopus 로고
    • Identification of calreticulin as a rubella virus RNA binding protein
    • Singh N.K., et al. Identification of calreticulin as a rubella virus RNA binding protein. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:12770-12774.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12770-12774
    • Singh, N.K.1
  • 70
    • 0036787010 scopus 로고    scopus 로고
    • Calreticulin interacts with C/EBPalpha and C/EBPbeta mRNAs and represses translation of C/EBP proteins
    • Timchenko L.T., et al. Calreticulin interacts with C/EBPalpha and C/EBPbeta mRNAs and represses translation of C/EBP proteins. Mol. Cell Biol. 2002, 22:7242-7257.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 7242-7257
    • Timchenko, L.T.1
  • 71
    • 1542320700 scopus 로고    scopus 로고
    • Competition of CUGBP1 and calreticulin for the regulation of p21 translation determines cell fate
    • Iakova P., et al. Competition of CUGBP1 and calreticulin for the regulation of p21 translation determines cell fate. EMBO J. 2004, 23:406-417.
    • (2004) EMBO J. , vol.23 , pp. 406-417
    • Iakova, P.1
  • 72
    • 27944477788 scopus 로고    scopus 로고
    • Calreticulin destabilizes glucose transporter-1 mRNA in vascular endothelial and smooth muscle cells under high-glucose conditions
    • Totary-Jain H., et al. Calreticulin destabilizes glucose transporter-1 mRNA in vascular endothelial and smooth muscle cells under high-glucose conditions. Circ. Res. 2005, 97:1001-1008.
    • (2005) Circ. Res. , vol.97 , pp. 1001-1008
    • Totary-Jain, H.1
  • 73
    • 78049299128 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium regulates the retrotranslocation of Trypanosoma cruzi calreticulin to the cytosol
    • Labriola C.A., et al. Endoplasmic reticulum calcium regulates the retrotranslocation of Trypanosoma cruzi calreticulin to the cytosol. PLoS One 2010, 5.
    • (2010) PLoS One , vol.5
    • Labriola, C.A.1
  • 74
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: from the ER lumen to the extracellular space
    • Johnson S., et al. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol. 2001, 11:122-129.
    • (2001) Trends Cell Biol. , vol.11 , pp. 122-129
    • Johnson, S.1
  • 75
    • 13444261932 scopus 로고    scopus 로고
    • The crucial role of vascular permeability factor/vascular endothelial growth factor in angiogenesis: a historical review
    • Ribatti D. The crucial role of vascular permeability factor/vascular endothelial growth factor in angiogenesis: a historical review. Br. J. Haematol. 2005, 128:303-309.
    • (2005) Br. J. Haematol. , vol.128 , pp. 303-309
    • Ribatti, D.1
  • 76
    • 17444374974 scopus 로고    scopus 로고
    • Angiogenesis: a curse or cure?
    • Gupta K., Zhang J. Angiogenesis: a curse or cure?. Postgrad. Med. J. 2005, 81:236-242.
    • (2005) Postgrad. Med. J. , vol.81 , pp. 236-242
    • Gupta, K.1    Zhang, J.2
  • 77
    • 0034090097 scopus 로고    scopus 로고
    • Angiogenesis: potentials for pharmacologic intervention in the treatment of cancer, cardiovascular diseases, and chronic inflammation
    • Griffioen A.W., Molema G. Angiogenesis: potentials for pharmacologic intervention in the treatment of cancer, cardiovascular diseases, and chronic inflammation. Pharmacol. Rev. 2000, 52:237-268.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 237-268
    • Griffioen, A.W.1    Molema, G.2
  • 78
    • 78650053837 scopus 로고    scopus 로고
    • Comparative antiangiogenic effects of Trypanosoma cruzi and Homo sapiens sapiens calreticulins
    • Toledo V., et al. Comparative antiangiogenic effects of Trypanosoma cruzi and Homo sapiens sapiens calreticulins. Biol. Res. 2010, 43:287-289.
    • (2010) Biol. Res. , vol.43 , pp. 287-289
    • Toledo, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.