메뉴 건너뛰기




Volumn 26, Issue 11, 2014, Pages 637-646

Cathelicidin rCRAMP stimulates rat mast cells to generate cysteinyl leukotrienes, synthesize TNF and migrate: Involvement of PLC/A2, PI3K and MAPK signaling pathways

Author keywords

Anti microbial peptide; Host defense; Inflammation; Innate immunity; Mast cell functioning

Indexed keywords

CATHELICIDIN; CATHELICIDIN RELATED ANTI MICROBIAL PEPTIDE; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 1BETA; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; MONOCYTE CHEMOTACTIC PROTEIN 1; PEPTIDOLEUKOTRIENE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE A2; PHOSPHOLIPASE C; POLYPEPTIDE ANTIBIOTIC AGENT; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; CATHELICIDIN ANTIMICROBIAL PEPTIDE; CYSTEINE; CYSTEINYL-LEUKOTRIENE; CYTOKINE; LEUKOTRIENE; MESSENGER RNA; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE;

EID: 84911422228     PISSN: 09538178     EISSN: 14602377     Source Type: Journal    
DOI: 10.1093/intimm/dxu069     Document Type: Article
Times cited : (19)

References (47)
  • 2
    • 56549122816 scopus 로고    scopus 로고
    • Mast cells: multifaceted immune cells with diverse roles in health and disease
    • Rao, K. N. and Brown, M. A. 2008. Mast cells: multifaceted immune cells with diverse roles in health and disease. Ann. N. Y. Acad. Sci. 1143:83.
    • (2008) Ann. N. Y. Acad. Sci , vol.1143 , pp. 83
    • Rao, K.N.1    Brown, M.A.2
  • 3
  • 4
    • 77952868792 scopus 로고    scopus 로고
    • Mast cell-orchestrated immunity to pathogens
    • Abraham, S. N. and St John, A. L. 2010. Mast cell-orchestrated immunity to pathogens. Nat. Rev. Immunol. 10:440.
    • (2010) Nat. Rev. Immunol , vol.10 , pp. 440
    • Abraham, S.N.1    St John, A.L.2
  • 5
    • 84861218220 scopus 로고    scopus 로고
    • The role of mast cells in the defence against pathogens
    • Urb, M. and Sheppard, D. C. 2012. The role of mast cells in the defence against pathogens. PLoS Pathog. 8:e1002619.
    • (2012) PLoS Pathog , vol.8 , pp. e1002619
    • Urb, M.1    Sheppard, D.C.2
  • 6
    • 84858766200 scopus 로고    scopus 로고
    • Mast cells as critical effectors of host immune defense against Gram-negative bacteria
    • Matsuguchi, T. 2012. Mast cells as critical effectors of host immune defense against Gram-negative bacteria. Curr. Med. Chem. 19:1432.
    • (2012) Curr. Med. Chem , vol.19 , pp. 1432
    • Matsuguchi, T.1
  • 9
    • 0031796119 scopus 로고    scopus 로고
    • Phagocytic and tumor necrosis factor alpha response of human mast cells following exposure to gram-negative and gram-positive bacteria
    • Arock, M., Ross, E., Lai-Kuen, R., Averlant, G., Gao, Z. and Abraham, S. N. 1998. Phagocytic and tumor necrosis factor alpha response of human mast cells following exposure to gram-negative and gram-positive bacteria. Infect. Immun. 66:6030.
    • (1998) Infect. Immun , vol.66 , pp. 6030
    • Arock, M.1    Ross, E.2    Lai-Kuen, R.3    Averlant, G.4    Gao, Z.5    Abraham, S.N.6
  • 10
    • 84873543949 scopus 로고    scopus 로고
    • Mast cells act as phagocytes against the periodontopathogen Aggregatibacter actinomycetemcomitans
    • Lima, H. G., Pinke, K. H., Gardizani, T. P. et al. 2013. Mast cells act as phagocytes against the periodontopathogen Aggregatibacter actinomycetemcomitans. J. Periodontol. 84:265.
    • (2013) J. Periodontol , vol.84 , pp. 265
    • Lima, H.G.1    Pinke, K.H.2    Gardizani, T.P.3
  • 11
    • 42449155517 scopus 로고    scopus 로고
    • Phagocytosis-independent antimicrobial activity of mast cells by means of extracellular trap formation
    • von Köckritz-Blickwede, M., Goldmann, O., Thulin, P. et al. 2008. Phagocytosis-independent antimicrobial activity of mast cells by means of extracellular trap formation. Blood 111:3070.
    • (2008) Blood , vol.111 , pp. 3070
    • von Köckritz-Blickwede, M.1    Goldmann, O.2    Thulin, P.3
  • 12
    • 0027374971 scopus 로고
    • Antigendependent stimulation by bone marrow-derived mast cells of MHC class II-restricted T cell hybridoma
    • Frandji, P., Oskéritzian, C., Cacaraci, F. et al. 1993. Antigendependent stimulation by bone marrow-derived mast cells of MHC class II-restricted T cell hybridoma. J. Immunol. 151:6318.
    • (1993) J. Immunol , vol.151 , pp. 6318
    • Frandji, P.1    Oskéritzian, C.2    Cacaraci, F.3
  • 13
    • 79953314027 scopus 로고    scopus 로고
    • Notch1-mediated signaling induces MHC class II expression through activation of class II transactivator promoter III in mast cells
    • Nakano, N., Nishiyama, C., Yagita, H., Koyanagi, A., Ogawa, H. and Okumura, K. 2011. Notch1-mediated signaling induces MHC class II expression through activation of class II transactivator promoter III in mast cells. J. Biol. Chem. 286:12042.
    • (2011) J. Biol. Chem , vol.286 , pp. 12042
    • Nakano, N.1    Nishiyama, C.2    Yagita, H.3    Koyanagi, A.4    Ogawa, H.5    Okumura, K.6
  • 14
    • 0030043421 scopus 로고    scopus 로고
    • Mast cells process bacterial Ags through a phagocytic route for class I MHC presentation to T cells
    • Malaviya, R., Twesten, N. J., Ross, E. A., Abraham, S. N. and Pfeifer, J. D. 1996. Mast cells process bacterial Ags through a phagocytic route for class I MHC presentation to T cells. J. Immunol. 156:1490.
    • (1996) J. Immunol , vol.156 , pp. 1490
    • Malaviya, R.1    Twesten, N.J.2    Ross, E.A.3    Abraham, S.N.4    Pfeifer, J.D.5
  • 15
    • 79960900325 scopus 로고    scopus 로고
    • The mast cell in innate and adaptive immunity
    • Shelburne, C. P. and Abraham, S. N. 2011. The mast cell in innate and adaptive immunity. Adv. Exp. Med. Biol. 716:162.
    • (2011) Adv. Exp. Med. Biol , vol.716 , pp. 162
    • Shelburne, C.P.1    Abraham, S.N.2
  • 16
    • 84863331797 scopus 로고    scopus 로고
    • Cationic host defence peptides: multifaceted role in immune modulation and inflammation
    • Choi, K. Y., Chow, L. N. and Mookherjee, N. 2012. Cationic host defence peptides: multifaceted role in immune modulation and inflammation. J. Innate Immun. 4:361.
    • (2012) J. Innate Immun , vol.4 , pp. 361
    • Choi, K.Y.1    Chow, L.N.2    Mookherjee, N.3
  • 18
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti, M. 2005. The role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 7:179.
    • (2005) Curr. Issues Mol. Biol , vol.7 , pp. 179
    • Zanetti, M.1
  • 19
    • 0345074069 scopus 로고    scopus 로고
    • Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide
    • Di Nardo, A., Vitiello, A. and Gallo, R. L. 2003. Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide. J. Immunol. 170:2274.
    • (2003) J. Immunol , vol.170 , pp. 2274
    • Di Nardo, A.1    Vitiello, A.2    Gallo, R.L.3
  • 20
    • 84855415476 scopus 로고    scopus 로고
    • Skin mast cells protect mice against vaccinia virus by triggering mast cell receptor S1PR2 and releasing antimicrobial peptides
    • Wang, Z., Lai, Y., Bernard, J. J. et al. 2012. Skin mast cells protect mice against vaccinia virus by triggering mast cell receptor S1PR2 and releasing antimicrobial peptides. J. Immunol. 188:345.
    • (2012) J. Immunol , vol.188 , pp. 345
    • Wang, Z.1    Lai, Y.2    Bernard, J.J.3
  • 21
    • 84864816224 scopus 로고    scopus 로고
    • Commensal bacteria lipoteichoic acid increases skin mast cell antimicrobial activity against vaccinia viruses
    • Wang, Z., MacLeod, D. T. and Di Nardo, A. 2012. Commensal bacteria lipoteichoic acid increases skin mast cell antimicrobial activity against vaccinia viruses. J. Immunol. 189:1551.
    • (2012) J. Immunol , vol.189 , pp. 1551
    • Wang, Z.1    MacLeod, D.T.2    Di Nardo, A.3
  • 22
    • 47249165576 scopus 로고    scopus 로고
    • Mast cell cathelicidin antimicrobial peptide prevents invasive group A Streptococcus infection of the skin
    • Di Nardo, A., Yamasaki, K., Dorschner, R. A., Lai, Y. and Gallo, R. L. 2008. Mast cell cathelicidin antimicrobial peptide prevents invasive group A Streptococcus infection of the skin. J. Immunol. 180:7565.
    • (2008) J. Immunol , vol.180 , pp. 7565
    • Di Nardo, A.1    Yamasaki, K.2    Dorschner, R.A.3    Lai, Y.4    Gallo, R.L.5
  • 23
    • 34248642536 scopus 로고    scopus 로고
    • STAT3-mediated anti-inflammatory signalling
    • Murray, P. J. 2006. STAT3-mediated anti-inflammatory signalling. Biochem. Soc. Trans. 34(Pt 6):1028.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1028
    • Murray, P.J.1
  • 24
    • 0036389804 scopus 로고    scopus 로고
    • Selective CCL5/ RANTES-induced mast cell migration through interactions with chemokine receptors CCR1 and CCR4
    • Juremalm, M., Olsson, N. and Nilsson, G. 2002. Selective CCL5/ RANTES-induced mast cell migration through interactions with chemokine receptors CCR1 and CCR4. Biochem. Biophys. Res. Commun. 297:480.
    • (2002) Biochem. Biophys. Res. Commun , vol.297 , pp. 480
    • Juremalm, M.1    Olsson, N.2    Nilsson, G.3
  • 25
    • 38849134035 scopus 로고    scopus 로고
    • Human cathelicidin CAP18/LL-37 changes mast cell function toward innate immunity
    • Yoshioka, M., Fukuishi, N., Kubo, Y. et al. 2008. Human cathelicidin CAP18/LL-37 changes mast cell function toward innate immunity. Biol. Pharm. Bull. 31:212.
    • (2008) Biol. Pharm. Bull , vol.31 , pp. 212
    • Yoshioka, M.1    Fukuishi, N.2    Kubo, Y.3
  • 26
    • 84455172954 scopus 로고    scopus 로고
    • Mas-related gene X2 (MrgX2) is a novel G protein-coupled receptor for the antimicrobial peptide LL-37 in human mast cells: resistance to receptor phosphorylation, desensitization, and internalization
    • Subramanian, H., Gupta, K., Guo, Q., Price, R. and Ali, H. 2011. Mas-related gene X2 (MrgX2) is a novel G protein-coupled receptor for the antimicrobial peptide LL-37 in human mast cells: resistance to receptor phosphorylation, desensitization, and internalization. J. Biol. Chem. 286:44739.
    • (2011) J. Biol. Chem , vol.286 , pp. 44739
    • Subramanian, H.1    Gupta, K.2    Guo, Q.3    Price, R.4    Ali, H.5
  • 27
    • 0035058454 scopus 로고    scopus 로고
    • Evaluation of the effects of peptide antibiotics human beta-defensins-1/-2 and LL-37 on histamine release and prostaglandin D(2) production from mast cells
    • Niyonsaba, F., Someya, A., Hirata, M., Ogawa, H. and Nagaoka, I. 2001. Evaluation of the effects of peptide antibiotics human beta-defensins-1/-2 and LL-37 on histamine release and prostaglandin D(2) production from mast cells. Eur. J. Immunol. 31:1066.
    • (2001) Eur. J. Immunol , vol.31 , pp. 1066
    • Niyonsaba, F.1    Someya, A.2    Hirata, M.3    Ogawa, H.4    Nagaoka, I.5
  • 28
    • 70149093034 scopus 로고    scopus 로고
    • The cathelicidin LL-37 activates human mast cells and is degraded by mast cell tryptase: counter-regulation by CXCL4
    • Schiemann, F., Brandt, E., Gross, R. et al. 2009. The cathelicidin LL-37 activates human mast cells and is degraded by mast cell tryptase: counter-regulation by CXCL4. J. Immunol. 183:2223.
    • (2009) J. Immunol , vol.183 , pp. 2223
    • Schiemann, F.1    Brandt, E.2    Gross, R.3
  • 29
    • 33744512882 scopus 로고    scopus 로고
    • Human cathelicidin LL-37 increases vascular permeability in the skin via mast cell activation, and phosphorylates MAP kinases p38 and ERK in mast cells
    • Chen, X., Niyonsaba, F., Ushio, H. et al. 2006. Human cathelicidin LL-37 increases vascular permeability in the skin via mast cell activation, and phosphorylates MAP kinases p38 and ERK in mast cells. J. Dermatol. Sci. 43:63.
    • (2006) J. Dermatol. Sci , vol.43 , pp. 63
    • Chen, X.1    Niyonsaba, F.2    Ushio, H.3
  • 30
    • 77951626078 scopus 로고    scopus 로고
    • Antimicrobial peptides human beta-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cells
    • Niyonsaba, F., Ushio, H., Hara, M. et al. 2010. Antimicrobial peptides human beta-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cells. J. Immunol. 184:3526.
    • (2010) J. Immunol , vol.184 , pp. 3526
    • Niyonsaba, F.1    Ushio, H.2    Hara, M.3
  • 31
    • 0036240209 scopus 로고    scopus 로고
    • A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis
    • Niyonsaba, F., Iwabuchi, K., Someya, A. et al. 2002. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology 106:20.
    • (2002) Immunology , vol.106 , pp. 20
    • Niyonsaba, F.1    Iwabuchi, K.2    Someya, A.3
  • 32
    • 34247528494 scopus 로고    scopus 로고
    • Mast cell homeostasis: a fundamental aspect of allergic disease
    • Ryan, J. J., Kashyap, M., Bailey, D. et al. 2007. Mast cell homeostasis: a fundamental aspect of allergic disease. Crit. Rev. Immunol. 27:15.
    • (2007) Crit. Rev. Immunol , vol.27 , pp. 15
    • Ryan, J.J.1    Kashyap, M.2    Bailey, D.3
  • 33
    • 0035105759 scopus 로고    scopus 로고
    • The role of Th2 cytokines in mast cell homeostasis
    • Shelburne, C. P. and Ryan, J. J. 2001. The role of Th2 cytokines in mast cell homeostasis. Immunol. Rev. 179:82.
    • (2001) Immunol. Rev , vol.179 , pp. 82
    • Shelburne, C.P.1    Ryan, J.J.2
  • 34
    • 63749105529 scopus 로고    scopus 로고
    • Interleukin (IL)-10 inhibits RANTES-, tumour necrosis factor (TNF)- and nerve growth factor (NGF)-induced mast cell migratory response but is not a mast cell chemoattractant
    • Pietrzak, A., Misiak-Tłoczek, A. and Brzezińska-Blaszczyk, E. 2009. Interleukin (IL)-10 inhibits RANTES-, tumour necrosis factor (TNF)- and nerve growth factor (NGF)-induced mast cell migratory response but is not a mast cell chemoattractant. Immunol. Lett. 123:46.
    • (2009) Immunol. Lett , vol.123 , pp. 46
    • Pietrzak, A.1    Misiak-Tłoczek, A.2    Brzezińska-Blaszczyk, E.3
  • 35
    • 66349132738 scopus 로고    scopus 로고
    • Alterations in vitamin D status and anti-microbial peptide levels in patients in the intensive care unit with sepsis
    • Jeng, L., Yamshchikov, A. V., Judd, S. E. et al. 2009. Alterations in vitamin D status and anti-microbial peptide levels in patients in the intensive care unit with sepsis. J. Transl. Med. 7:28.
    • (2009) J. Transl. Med , vol.7 , pp. 28
    • Jeng, L.1    Yamshchikov, A.V.2    Judd, S.E.3
  • 36
    • 12444337486 scopus 로고    scopus 로고
    • Expression and activity of beta-defensins and LL-37 in the developing human lung
    • Starner, T. D., Agerberth, B., Gudmundsson, G. H. and McCray, P. B. Jr. 2005. Expression and activity of beta-defensins and LL-37 in the developing human lung. J. Immunol. 174:1608.
    • (2005) J. Immunol , vol.174 , pp. 1608
    • Starner, T.D.1    Agerberth, B.2    Gudmundsson, G.H.3    McCray, P.B.Jr.4
  • 37
    • 77951946876 scopus 로고    scopus 로고
    • Maternal plasma level of antimicrobial peptide LL37 is a major determinant factor of neonatal plasma LL37 level
    • Mandic Havelka, A., Yektaei-Karin, E., Hultenby, K. et al. 2010. Maternal plasma level of antimicrobial peptide LL37 is a major determinant factor of neonatal plasma LL37 level. Acta Paediatr. 99:836.
    • (2010) Acta Paediatr , vol.99 , pp. 836
    • Mandic Havelka, A.1    Yektaei-Karin, E.2    Hultenby, K.3
  • 38
    • 27144462218 scopus 로고    scopus 로고
    • Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation
    • Xiao, W., Hsu, Y. P., Ishizaka, A., Kirikae, T. and Moss, R. B. 2005. Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation. Chest 128:2316.
    • (2005) Chest , vol.128 , pp. 2316
    • Xiao, W.1    Hsu, Y.P.2    Ishizaka, A.3    Kirikae, T.4    Moss, R.B.5
  • 39
    • 1642405248 scopus 로고    scopus 로고
    • Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis
    • Chen, C. I., Schaller-Bals, S., Paul, K. P., Wahn, U. and Bals, R. 2009. Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis. J. Cyst. Fibros. 3:45.
    • (2004) J. Cyst. Fibros , vol.3 , pp. 45
    • Chen, C.I.1    Schaller-Bals, S.2    Paul, K.P.3    Wahn, U.4    Bals, R.5
  • 40
    • 70449363613 scopus 로고    scopus 로고
    • Evidence that cathelicidin peptide LL-37 may act as a functional ligand for CXCR2 on human neutrophils
    • Zhang, Z., Cherryholmes, G., Chang, F., Rose, D. M., Schraufstatter, I. and Shively, J. E. 2009. Evidence that cathelicidin peptide LL-37 may act as a functional ligand for CXCR2 on human neutrophils. Eur. J. Immunol. 39:3181.
    • (2009) Eur. J. Immunol , vol.39 , pp. 3181
    • Zhang, Z.1    Cherryholmes, G.2    Chang, F.3    Rose, D.M.4    Schraufstatter, I.5    Shively, J.E.6
  • 41
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang, D., Chen, Q., Schmidt, A. P. et al. 2000. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192:1069.
    • (2000) J. Exp. Med , vol.192 , pp. 1069
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3
  • 42
    • 33644511380 scopus 로고    scopus 로고
    • An antimicrobial cathelicidin peptide, human CAP18/LL-37, suppresses neutrophil apoptosis via the activation of formyl-peptide receptor-like 1 and P2X7
    • Nagaoka, I., Tamura, H. and Hirata, M. 2006. An antimicrobial cathelicidin peptide, human CAP18/LL-37, suppresses neutrophil apoptosis via the activation of formyl-peptide receptor-like 1 and P2X7. J. Immunol. 176:3044.
    • (2006) J. Immunol , vol.176 , pp. 3044
    • Nagaoka, I.1    Tamura, H.2    Hirata, M.3
  • 43
    • 84855968882 scopus 로고    scopus 로고
    • Identification of the cathelicidin peptide LL-37 as agonist for the type I insulin-like growth factor receptor
    • Girnita, A., Zheng, H., Grönberg, A., Girnita, L. and Ståhle, M. 2012. Identification of the cathelicidin peptide LL-37 as agonist for the type I insulin-like growth factor receptor. Oncogene 31:352.
    • (2012) Oncogene , vol.31 , pp. 352
    • Girnita, A.1    Zheng, H.2    Grönberg, A.3    Girnita, L.4    Ståhle, M.5
  • 44
    • 25444468300 scopus 로고    scopus 로고
    • Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37
    • Tokumaru, S., Sayama, K., Shirakata, Y. et al. 2005. Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37. J. Immunol. 175:4662.
    • (2005) J. Immunol , vol.175 , pp. 4662
    • Tokumaru, S.1    Sayama, K.2    Shirakata, Y.3
  • 45
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa, G. S., Aarbiou, J., Ninaber, D. K. et al. 2003. The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J. Immunol. 171:6690.
    • (2003) J. Immunol , vol.171 , pp. 6690
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3
  • 46
    • 1842581655 scopus 로고    scopus 로고
    • A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release
    • Elssner, A., Duncan, M., Gavrilin, M. and Wewers, M. D. 2004. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J. Immunol. 172:4987.
    • (2004) J. Immunol , vol.172 , pp. 4987
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 47
    • 79954880573 scopus 로고    scopus 로고
    • Involvement of P2X(7) purinergic receptor and MEK1/2 in interleukin-8 up-regulation by LL-37 in human gingival fibroblasts
    • Montreekachon, P., Chotjumlong, P., Bolscher, J. G., Nazmi, K., Reutrakul, V. and Krisanaprakornkit, S. 2011. Involvement of P2X(7) purinergic receptor and MEK1/2 in interleukin-8 up-regulation by LL-37 in human gingival fibroblasts. J. Periodontal Res. 46:327.
    • (2011) J. Periodontal Res , vol.46 , pp. 327
    • Montreekachon, P.1    Chotjumlong, P.2    Bolscher, J.G.3    Nazmi, K.4    Reutrakul, V.5    Krisanaprakornkit, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.