메뉴 건너뛰기




Volumn 106, Issue 4, 2011, Pages 475-485

Protective effect of β-(1,3→1,6)-d-glucan against irritant-induced gastric lesions

Author keywords

(1,3 1,6) d Glucan; Ethanol; Gastric lesions; Heat shock protein 70; Mucin

Indexed keywords

ALCOHOL; BETA 1,3 GLUCAN; BETA 1,6 GLUCAN; CELL ADHESION MOLECULE; CHEMOKINE; CHLORIDE; CYTOKINE; HEAT SHOCK PROTEIN 70; MUCIN; MYELOPEROXIDASE; PROSTAGLANDIN E2;

EID: 80052962695     PISSN: 00071145     EISSN: 14752662     Source Type: Journal    
DOI: 10.1017/S0007114511000365     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 0031921973 scopus 로고    scopus 로고
    • Neural emergency system in the stomach
    • DOI 10.1016/S0016-5085(98)70597-9
    • Holzer P (1998) Neural emergency system in the stomach. Gastroenterology 114, 823-839. (Pubitemid 28160418)
    • (1998) Gastroenterology , vol.114 , Issue.4 , pp. 823-839
    • Holzer, P.1
  • 3
    • 0031852375 scopus 로고    scopus 로고
    • Role of the heat-shock response in the life and death of proteins
    • DOI 10.1111/j.1749-6632.1998.tb08982.x
    • Mathew A & Morimoto RI (1998) Role of the heat-shock response in the life and death of proteins. Ann N Y Acad Sci 851, 99-111. (Pubitemid 28370369)
    • (1998) Annals of the New York Academy of Sciences , vol.851 , pp. 99-111
    • Mathew, A.1    Morimoto, R.I.2
  • 4
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ & Sambrook J (1992) Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 5
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • DOI 10.1016/S0163-7258(98)00028-X, PII S016372589800028X
    • Kiang JG & Tsokos GC (1998) Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 80, 183-201. (Pubitemid 28498227)
    • (1998) Pharmacology and Therapeutics , vol.80 , Issue.2 , pp. 183-201
    • Kiang, J.G.1    Tsokos, G.C.2
  • 6
    • 0030038266 scopus 로고    scopus 로고
    • Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa
    • DOI 10.1053/gast.1996.v111.pm8690199
    • Hirakawa T, Rokutan K, Nikawa T, et al. (1996) Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa. Gastroenterology 111, 345-357. (Pubitemid 26256722)
    • (1996) Gastroenterology , vol.111 , Issue.2 , pp. 345-357
    • Hirakawa, T.1    Rokutan, K.2    Nikawa, T.3    Kishi, K.4
  • 8
    • 67651063544 scopus 로고    scopus 로고
    • A role for HSP70 in protecting against indomethacin-induced gastric lesions
    • Suemasu S, Tanaka K, Namba T, et al. (2009) A role for HSP70 in protecting against indomethacin-induced gastric lesions. J Biol Chem 284, 19705-19715.
    • (2009) J Biol Chem , vol.284 , pp. 19705-19715
    • Suemasu, S.1    Tanaka, K.2    Namba, T.3
  • 10
    • 34447526486 scopus 로고    scopus 로고
    • Medicinal importance of fungal β-(1→3), (1→6)-glucans
    • DOI 10.1016/j.mycres.2007.02.011, PII S0953756207000573
    • Chen J & Seviour R (2007) Medicinal importance of fungal beta-(1 ! 3), (1 ! 6)-glucans. Mycol Res 111, 635-652. (Pubitemid 47082471)
    • (2007) Mycological Research , vol.111 , Issue.6 , pp. 635-652
    • Chen, J.1    Seviour, R.2
  • 11
    • 0141495001 scopus 로고    scopus 로고
    • Fungal beta-glucans and mammalian immunity
    • Brown GD & Gordon S (2003) Fungal beta-glucans and mammalian immunity. Immunity 19, 311-315.
    • (2003) Immunity , vol.19 , pp. 311-315
    • Brown, G.D.1    Gordon, S.2
  • 12
    • 0030665179 scopus 로고    scopus 로고
    • Enhanced production of inducible nitric oxide synthase by β-glucans in mice
    • DOI 10.1016/S0928-8244(97)00078-3, PII S0928824497000783
    • Hashimoto T, Ohno N, Adachi Y, et al. (1997) Enhanced production of inducible nitric oxide synthase by beta-glucans in mice. FEMS Immunol Med Microbiol 19, 131-135. (Pubitemid 27467066)
    • (1997) FEMS Immunology and Medical Microbiology , vol.19 , Issue.2 , pp. 131-135
    • Hashimoto, T.1    Ohno, N.2    Adachi, Y.3    Yadomae, T.4
  • 13
    • 0036802550 scopus 로고    scopus 로고
    • The effect of soluble β-1,3-glucan and lipopolysaccharide on cytokine production and coagulation activation in whole blood
    • DOI 10.1016/S1567-5769(02)00134-0, PII S1567576902001340
    • Engstad CS, Engstad RE, Olsen JO, et al. (2002) The effect of soluble beta-1,3-glucan and lipopolysaccharide on cytokine production and coagulation activation in whole blood. Int Immunopharmacol 2, 1585-1597. (Pubitemid 35223239)
    • (2002) International Immunopharmacology , vol.2 , Issue.11 , pp. 1585-1597
    • Engstad, C.S.1    Engstad, R.E.2    Olsen, J.-O.3    Osterud, B.4
  • 14
    • 33845934933 scopus 로고    scopus 로고
    • Antitumor and antimetastatic activity of a novel water-soluble low molecular weight β-1, 3-D-glucan (branch β-1,6) isolated from Aureobasidium pullulans 1A1 strain black yeast
    • Kimura Y, Sumiyoshi M, Suzuki T, et al. (2006) Antitumor and antimetastatic activity of a novel water-soluble low molecular weight beta-1, 3-D-glucan (branch beta-1,6) isolated from Aureobasidium pullulans 1A1 strain black yeast. Anticancer Res 26, 4131-4141. (Pubitemid 46031482)
    • (2006) Anticancer Research , vol.26 , Issue.6 , pp. 4131-4141
    • Kimura, Y.1    Sumiyoshi, M.2    Suzuki, T.3    Sakanaka, M.4
  • 17
    • 33746001411 scopus 로고    scopus 로고
    • β-glucan ameliorates methotrexate-induced oxidative organ injury via its antioxidant and immunomodulatory effects
    • DOI 10.1016/j.ejphar.2006.02.056, PII S0014299906005073
    • Sener G, Eksioglu-Demiralp E, Cetiner M, et al. (2006) Betaglucan ameliorates methotrexate-induced oxidative organ injury via its antioxidant and immunomodulatory effects. Eur J Pharmacol 542, 170-178. (Pubitemid 44066363)
    • (2006) European Journal of Pharmacology , vol.542 , Issue.1-3 , pp. 170-178
    • Sener, G.1    Eksioglu-Demiralp, E.2    Cetiner, M.3    Ercan, F.4    Yegen, B.C.5
  • 18
    • 34247159151 scopus 로고    scopus 로고
    • Beta-glucan attenuates inflammatory cytokine release and prevents acute lung injury in an experimental model of sepsis
    • DOI 10.1097/01.shk.0000245030.24235.f1, PII 0002438220070400000010
    • Bedirli A, Kerem M, Pasaoglu H, et al. (2007) Beta-glucan attenuates inflammatory cytokine release and prevents acute lung injury in an experimental model of sepsis. Shock 27, 397-401. (Pubitemid 46594971)
    • (2007) Shock , vol.27 , Issue.4 , pp. 397-401
    • Bedirli, A.1    Kerem, M.2    Pasaoglu, H.3    Akyurek, N.4    Tezcaner, T.5    Elbeg, S.6    Memis, L.7    Sakrak, O.8
  • 19
    • 14344250532 scopus 로고    scopus 로고
    • Glucan phosphate treatment attenuates burn-induced inflammation and improves resistance to Pseudomonas aeruginosa burn wound infection
    • DOI 10.1097/01.shk.0000151864.79293.41
    • Lyuksutova OI, Murphey ED, Toliver-Kinsky TE, et al. (2005) Glucan phosphate treatment attenuates burn-induced inflammation and improves resistance to Pseudomonas aeruginosa burn wound infection. Shock 23, 224-232. (Pubitemid 40293821)
    • (2005) Shock , vol.23 , Issue.3 , pp. 224-232
    • Lyuksutova, O.I.1    Murphey, E.D.2    Toliver-Kinsky, T.E.3    Lin, C.Y.4    Cui, W.5    Williams, D.L.6    Sherwood, E.R.7
  • 20
    • 0032919556 scopus 로고    scopus 로고
    • Modulation of endotoxin- and enterotoxin-induced cytokine release by in vivo treatment with β-(1,6)-branched β-(1,3)-glucan
    • Soltys J & Quinn MT (1999) Modulation of endotoxin-and enterotoxin-induced cytokine release by in vivo treatment with beta-(1,6)-branched beta-(1,3)-glucan. Infect Immun 67, 244-252. (Pubitemid 29021655)
    • (1999) Infection and Immunity , vol.67 , Issue.1 , pp. 244-252
    • Soltys, J.1    Quinn, M.T.2
  • 21
    • 33746214576 scopus 로고    scopus 로고
    • Acetaminophen-induced toxicity is prevented by β-d-glucan treatment in mice
    • DOI 10.1016/j.ejphar.2006.05.033, PII S0014299906005498
    • Toklu HZ, Sehirli AO, Velioglu-Ogunc A, et al. (2006) Acetaminophen-induced toxicity is prevented by beta-D-glucan treatment in mice. Eur J Pharmacol 543, 133-140. (Pubitemid 44092697)
    • (2006) European Journal of Pharmacology , vol.543 , Issue.1-3 , pp. 133-140
    • Toklu, H.Z.1    Sehirli, A.O.2    Velioglu-Ogunc, A.3    Cetinel, S.4    Sener, G.5
  • 22
    • 65549153732 scopus 로고    scopus 로고
    • Beta-Glucan attenuates TLR2-and TLR4-mediated cytokine production by microglia
    • Shah VB, Williams DL & Keshvara L (2009) beta-Glucan attenuates TLR2-and TLR4-mediated cytokine production by microglia. Neurosci Lett 458, 111-115.
    • (2009) Neurosci Lett , vol.458 , pp. 111-115
    • Shah, V.B.1    Williams, D.L.2    Keshvara, L.3
  • 23
    • 68849123464 scopus 로고    scopus 로고
    • Protective effects of water-soluble low-molecular-weight beta-(1, 3-1,6)Dglucan purified from Aureobasidium pullulans GM-NH-1A1 against UFT toxicity in mice
    • Sumiyoshi M, Suzuki T & Kimura Y (2009) Protective effects of water-soluble low-molecular-weight beta-(1,3-1,6)Dglucan purified from Aureobasidium pullulans GM-NH-1A1 against UFT toxicity in mice. J Pharm Pharmacol 61, 795-800.
    • (2009) J Pharm Pharmacol , vol.61 , pp. 795-800
    • Sumiyoshi, M.1    Suzuki, T.2    Kimura, Y.3
  • 25
    • 34547943120 scopus 로고    scopus 로고
    • Effects of water-soluble low-molecular-weight β-1, 3-D-glucan (branch β-1, 6) isolated from Aureobasidium pullulans 1A1 strain black yeast on restraint stress in mice
    • DOI 10.1211/jpp.59.8.0012
    • Kimura Y, Sumiyoshi M, Suzuki T, et al. (2007) Effects of water-soluble low-molecular-weight beta-1,3-D-glucan (branch beta-1,6) isolated from Aureobasidium pullulans 1A1 strain black yeast on restraint stress in mice. J Pharm Pharmacol 59, 1137-1144. (Pubitemid 47265362)
    • (2007) Journal of Pharmacy and Pharmacology , vol.59 , Issue.8 , pp. 1137-1144
    • Kimura, Y.1    Sumiyoshi, M.2    Suzuki, T.3    Suzuki, T.4    Sakanaka, M.5
  • 26
    • 34247882689 scopus 로고    scopus 로고
    • Inhibitory effects of water-soluble low-molecular-weight β-(1,3-1,6) d-glucan purified from Aureobasidium pullulans GM-NH-1A1 strain on food allergic reactions in mice
    • DOI 10.1016/j.intimp.2007.03.003, PII S1567576907000835
    • Kimura Y, Sumiyoshi M, Suzuki T, et al. (2007) Inhibitory effects of water-soluble low-molecular-weight beta-(1,3-1,6) D-glucan purified from Aureobasidium pullulans GM-NH-1A1 strain on food allergic reactions in mice. Int Immunopharmacol 7, 963-972. (Pubitemid 46702846)
    • (2007) International Immunopharmacology , vol.7 , Issue.7 , pp. 963-972
    • Kimura, Y.1    Sumiyoshi, M.2    Suzuki, T.3    Suzuki, T.4    Sakanaka, M.5
  • 29
    • 0021742157 scopus 로고
    • Quantitative assay for acute intestinal inflammation based on myeloperoxidase activity. Assessment of inflammation in rat and hamster models
    • Krawisz JE, Sharon P & Stenson WF (1984) Quantitative assay for acute intestinal inflammation based on myeloperoxidase activity. Assessment of inflammation in rat and hamster models. Gastroenterology 87, 1344-1350. (Pubitemid 15201434)
    • (1984) Gastroenterology , vol.87 , Issue.6 , pp. 1344-1350
    • Krawisz, J.E.1    Sharon, P.2    Stenson, W.F.3
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0030043717 scopus 로고    scopus 로고
    • Coinduction of nitric oxide synthase, argininosuccinate synthetase, and argininosuccinate lyase in lipopolysaccharide-treated rats. RNA blot, immunoblot, and immunohistochemical analyses
    • Nagasaki A, Gotoh T, Takeya M, et al. (1996) Coinduction of nitric oxide synthase, argininosuccinate synthetase, and argininosuccinate lyase in lipopolysaccharide-treated rats. RNA blot, immunoblot, and immunohistochemical analyses. J Biol Chem 271, 2658-2662.
    • (1996) J Biol Chem , vol.271 , pp. 2658-2662
    • Nagasaki, A.1    Gotoh, T.2    Takeya, M.3
  • 35
    • 0033799905 scopus 로고    scopus 로고
    • Mucins and mucosal protection in the gastrointestinal tract: New prospects for mucins in the pathology of gastrointestinal disease
    • Corfield AP, Myerscough N, Longman R, et al. (2000) Mucins and mucosal protection in the gastrointestinal tract: new prospects for mucins in the pathology of gastrointestinal disease. Gut 47, 589-594.
    • (2000) Gut , vol.47 , pp. 589-594
    • Corfield, A.P.1    Myerscough, N.2    Longman, R.3
  • 36
    • 1242337458 scopus 로고    scopus 로고
    • Mucins and mucin binding proteins in colorectal cancer
    • DOI 10.1023/A:1025815113599
    • Byrd JC & Bresalier RS (2004) Mucins and mucin binding proteins in colorectal cancer. Cancer Metastasis Rev 23, 77-99. (Pubitemid 38221597)
    • (2004) Cancer and Metastasis Reviews , vol.23 , Issue.1-2 , pp. 77-99
    • Byrd, J.C.1    Bresalier, R.S.2
  • 37
    • 23444437384 scopus 로고    scopus 로고
    • Heat shock protein-70 mediates the cytoprotective effect of carbon monoxide: Involvement of p38β MAPK and heat shock factor-1
    • Kim HP, Wang X, Zhang J, et al. (2005) Heat shock protein-70 mediates the cytoprotective effect of carbon monoxide: involvement of p38 beta MAPK and heat shock factor-1. J Immunol 175, 2622-2629. (Pubitemid 41113876)
    • (2005) Journal of Immunology , vol.175 , Issue.4 , pp. 2622-2629
    • Kim, H.P.1    Wang, X.2    Zhang, J.3    Suh, G.Y.4    Benjamin, I.J.5    Ryter, S.W.6    Choi, A.M.K.7
  • 38
    • 33644872354 scopus 로고    scopus 로고
    • Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding
    • Wang X, Khaleque MA, Zhao MJ, et al. (2006) Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J Biol Chem 281, 782-791.
    • (2006) J Biol Chem , vol.281 , pp. 782-791
    • Wang, X.1    Khaleque, M.A.2    Zhao, M.J.3
  • 40
    • 33646580045 scopus 로고    scopus 로고
    • Hsp70 inhibits lipopolysaccharide-induced NF-κB activation by interacting with TRAF6 and inhibiting its ubiquitination
    • DOI 10.1016/j.febslet.2006.04.066, PII S0014579306005072
    • Chen H, Wu Y, Zhang Y, et al. (2006) Hsp70 inhibits lipopolysaccharide- induced NF-kappaB activation by interacting with TRAF6 and inhibiting its ubiquitination. FEBS Lett 580, 3145-3152. (Pubitemid 43729683)
    • (2006) FEBS Letters , vol.580 , Issue.13 , pp. 3145-3152
    • Chen, H.1    Wu, Y.2    Zhang, Y.3    Jin, L.4    Luo, L.5    Xue, B.6    Lu, C.7    Zhang, X.8    Yin, Z.9
  • 41
    • 34548292474 scopus 로고    scopus 로고
    • Enhanced heat shock protein 70 expression alters proteasomal degradation of IκB kinase in experimental acute respiratory distress syndrome
    • DOI 10.1097/01.CCM.0000278915.78030.74, PII 0000324620070900000017
    • Weiss YG, Bromberg Z, Raj N, et al. (2007) Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Crit Care Med 35, 2128-2138. (Pubitemid 47326450)
    • (2007) Critical Care Medicine , vol.35 , Issue.9 , pp. 2128-2138
    • Weiss, Y.G.1    Bromberg, Z.2    Raj, N.3    Raphael, J.4    Goloubinoff, P.5    Ben-Neriah, Y.6    Deutschman, C.S.7
  • 42
    • 67651024137 scopus 로고    scopus 로고
    • HSP70 confers protection against indomethacin-induced lesions of the small intestine
    • Asano T, Tanaka K, Yamakawa N, et al. (2009) HSP70 confers protection against indomethacin-induced lesions of the small intestine. J Pharmacol Exp Ther 330, 458-467.
    • (2009) J Pharmacol Exp Ther , vol.330 , pp. 458-467
    • Asano, T.1    Tanaka, K.2    Yamakawa, N.3
  • 43
    • 77949318845 scopus 로고    scopus 로고
    • Prevention of UVB radiation-induced epidermal damage by expression of heat shock protein 70
    • Matsuda M, Hoshino T, Yamashita Y, et al. (2010) Prevention of UVB radiation-induced epidermal damage by expression of heat shock protein 70. J Biol Chem 285, 5848-5858.
    • (2010) J Biol Chem , vol.285 , pp. 5848-5858
    • Matsuda, M.1    Hoshino, T.2    Yamashita, Y.3
  • 44
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana NR, Tanaka M, Wang G, et al. (2000) Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 9, 2009-2018. (Pubitemid 30642666)
    • (2000) Human Molecular Genetics , vol.9 , Issue.13 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.-H.3    Nukina, N.4
  • 45
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto RI & Santoro MG (1998) Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nat Biotechnol 16, 833-838. (Pubitemid 28405852)
    • (1998) Nature Biotechnology , vol.16 , Issue.9 , pp. 833-838
    • Morimoto, R.I.1    Gabriella Santoro, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.