메뉴 건너뛰기




Volumn 9, Issue 9, 2018, Pages

Combination of Gluten-Digesting Enzymes Improved Symptoms of Non-Celiac Gluten Sensitivity: A Randomized Single-blind, Placebo-controlled Crossover Study

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; DEUTEROLYSIN; ENZYME; INTERLEUKIN 8; PEPTIDASE; PLACEBO; RANTES; SEMI ALKALINE PROTEASE; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; ALKALINE PROTEINASE; BACTERIAL PROTEIN; CYTOKINE; GLUTEN; PEPTIDE HYDROLASE; PROTEINASE;

EID: 85053477022     PISSN: None     EISSN: 2155384X     Source Type: Journal    
DOI: 10.1038/s41424-018-0052-1     Document Type: Article
Times cited : (13)

References (29)
  • 1
    • 84926420816 scopus 로고    scopus 로고
    • Systematic review: noncoeliac gluten sensitivity
    • Molina-Ifante, J. et al. Systematic review: noncoeliac gluten sensitivity. Aliment. Pharmacol. Ther. 41, 807–820 (2015).
    • (2015) Aliment. Pharmacol. Ther. , vol.41 , pp. 807-820
    • Molina-Ifante, J.1
  • 2
    • 70649112647 scopus 로고    scopus 로고
    • A validated disease-specific symptom index for adults with celiac disease
    • Leffler, D. A. et al. A validated disease-specific symptom index for adults with celiac disease. Clin. Gastroenterol. Hepatol. 7, 1328–1334 (2009).
    • (2009) Clin. Gastroenterol. Hepatol. , vol.7 , pp. 1328-1334
    • Leffler, D.A.1
  • 3
    • 0037183929 scopus 로고    scopus 로고
    • Structural basis for gluten intolerance in celiac sprue
    • COI: 1:CAS:528:DC%2BD38XntlWlt70%3D
    • Shan, L. et al. Structural basis for gluten intolerance in celiac sprue. Science 297, 2275–2279 (2002).
    • (2002) Science , vol.297 , pp. 2275-2279
    • Shan, L.1
  • 4
    • 40349098215 scopus 로고    scopus 로고
    • Parallels between pathogens and gluten peptides in celiac sprue
    • Bethune, M. T. & Khosla, C. Parallels between pathogens and gluten peptides in celiac sprue. PLoS Pathog. 4, e34 (2008).
    • (2008) PLoS Pathog. , vol.4
    • Bethune, M.T.1    Khosla, C.2
  • 5
    • 67349226415 scopus 로고    scopus 로고
    • Between celiac disease and irritable bowel syndrome: the “no man’s land” of gluten sensitivity
    • Verdu, E. F., Armstrong, D. & Murray, J. A. Between celiac disease and irritable bowel syndrome: the “no man’s land” of gluten sensitivity. Am. J. Gastroenterol. 104, 1587–1594 (2009).
    • (2009) Am. J. Gastroenterol. , vol.104 , pp. 1587-1594
    • Verdu, E.F.1    Armstrong, D.2    Murray, J.A.3
  • 6
    • 85021084444 scopus 로고    scopus 로고
    • Celiac disease: from etiological factors to evolving diagnostic approaches
    • COI: 1:CAS:528:DC%2BC2sXhtVOjs7nO
    • Kaur, A., Shimoni, O. & Wallach, M. Celiac disease: from etiological factors to evolving diagnostic approaches. J. Gastroenterol. 52, 1001–1012 (2017).
    • (2017) J. Gastroenterol. , vol.52 , pp. 1001-1012
    • Kaur, A.1    Shimoni, O.2    Wallach, M.3
  • 7
    • 79952362194 scopus 로고    scopus 로고
    • Gluten causes gastrointestinal symptoms in subjects without celiac disease: a double-blind randomized placebo-controlled trial
    • COI: 1:CAS:528:DC%2BC3MXislOls78%3D
    • Biesiekierski, J. R. et al. Gluten causes gastrointestinal symptoms in subjects without celiac disease: a double-blind randomized placebo-controlled trial. Am. J. Gastroenterol. 106, 508–514 (2011).
    • (2011) Am. J. Gastroenterol. , vol.106 , pp. 508-514
    • Biesiekierski, J.R.1
  • 8
    • 84928402782 scopus 로고    scopus 로고
    • Nonceliac gluten and wheat sensitivity nonceliac gluten sensitivity
    • COI: 1:CAS:528:DC%2BC2MXntVersb4%3D
    • Fasano, A. et al. Nonceliac gluten and wheat sensitivity nonceliac gluten sensitivity. Gastroenterology 148, 1195–1204 (2015).
    • (2015) Gastroenterology , vol.148 , pp. 1195-1204
    • Fasano, A.1
  • 9
    • 70450170412 scopus 로고    scopus 로고
    • Differential mucosal IL-17 expression in two gliadin-induced disorders: gluten sensitivity and the autoimmune enteropathy celiac disease
    • COI: 1:CAS:528:DC%2BC3cXkvVGiurc%3D
    • Sapone, A. et al. Differential mucosal IL-17 expression in two gliadin-induced disorders: gluten sensitivity and the autoimmune enteropathy celiac disease. Allergy Immunol. 152, 75–80 (2010).
    • (2010) Allergy Immunol. , vol.152 , pp. 75-80
    • Sapone, A.1
  • 10
    • 84885642584 scopus 로고    scopus 로고
    • Consumption of gluten with gluten-degrading enzyme by celiac patients: a pilot-study
    • COI: 1:CAS:528:DC%2BC2cXit1Skurc%3D
    • Tack, G. J. et al. Consumption of gluten with gluten-degrading enzyme by celiac patients: a pilot-study. World J. Gastroenterol. 19, 5837–5847 (2013).
    • (2013) World J. Gastroenterol. , vol.19 , pp. 5837-5847
    • Tack, G.J.1
  • 11
    • 85053483428 scopus 로고    scopus 로고
    • Glutalytic trial for normal consumption of gluten containing foods
    • Hudson, M. & King, C. Glutalytic trial for normal consumption of gluten containing foods. Fac. Publ. Kennesaw State Univ. 4, 3390 (2015).
    • (2015) Fac. Publ. Kennesaw State Univ. , vol.4 , pp. 3390
    • Hudson, M.1    King, C.2
  • 12
    • 84992052017 scopus 로고    scopus 로고
    • Properties of gluten intolerance: gluten structure, evolution, pathogenicity and detoxification capabilities
    • Balakireva, A. V. & Zamyatnin, A. A. Properties of gluten intolerance: gluten structure, evolution, pathogenicity and detoxification capabilities. Nutrients 8, 644 (2016).
    • (2016) Nutrients , vol.8 , pp. 644
    • Balakireva, A.V.1    Zamyatnin, A.A.2
  • 13
    • 84880637191 scopus 로고    scopus 로고
    • Gliadin does not induce mucosal inflammation or basophil activation in patients with nonceliac gluten sensitivity
    • COI: 1:CAS:528:DC%2BC3sXhsVyltb3P
    • Bucci, C. et al. Gliadin does not induce mucosal inflammation or basophil activation in patients with nonceliac gluten sensitivity. Clin. Gastroenterol. Hepatol. 11, 1294–1299 (2013).
    • (2013) Clin. Gastroenterol. Hepatol. , vol.11 , pp. 1294-1299
    • Bucci, C.1
  • 14
    • 0017485956 scopus 로고
    • Isolation and properties of leucine aminopeptidase from Aspergillus oryzae
    • COI: 1:CAS:528:DyaE2sXktlCru7s%3D, PID: 19097
    • Ivanova, N. M. et al. Isolation and properties of leucine aminopeptidase from Aspergillus oryzae. Biokhimiia 42, 843–849 (1977).
    • (1977) Biokhimiia , vol.42 , pp. 843-849
    • Ivanova, N.M.1
  • 15
    • 85053464653 scopus 로고
    • Alkaline protease of genus Aspergillus–the structure and the function
    • COI: 1:CAS:528:DyaE3sXktl2mur0%3D
    • Hayashi, K. Alkaline protease of genus Aspergillus–the structure and the function. Kagaku Seibutsu 11, 82–89 (1973).
    • (1973) Kagaku Seibutsu , vol.11 , pp. 82-89
    • Hayashi, K.1
  • 16
    • 84915944873 scopus 로고
    • Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteinase from Aspergillus sojae
    • COI: 1:CAS:528:DyaE3sXhtlajtA%3D%3D
    • Hayashi, K. & Terada, M. Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteinase from Aspergillus sojae. Agric. Biol. Chem. 36, 1755–1765 (1972).
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1755-1765
    • Hayashi, K.1    Terada, M.2
  • 17
    • 0014466633 scopus 로고
    • Arch. Comparison of the specificities of various serine proteinases from microorganisms
    • COI: 1:CAS:528:DyaF1MXmsVGltw%3D%3D
    • Morihara, K. & Tsuzuki, H. Arch. Comparison of the specificities of various serine proteinases from microorganisms. Biochem Biophys. 129, 620–634 (1969).
    • (1969) Biochem Biophys. , vol.129 , pp. 620-634
    • Morihara, K.1    Tsuzuki, H.2
  • 18
    • 0027651593 scopus 로고
    • Specificity and molecular properties of penicillolysin, a metalloproteinase from Penicillium citrinum
    • COI: 1:CAS:528:DyaK2cXjt1Ck
    • Yamaguchi, M. et al. Specificity and molecular properties of penicillolysin, a metalloproteinase from Penicillium citrinum. Phytochemistry 33, 1317–1321 (1993).
    • (1993) Phytochemistry , vol.33 , pp. 1317-1321
    • Yamaguchi, M.1
  • 19
    • 84946222480 scopus 로고    scopus 로고
    • The potential of papain and alcalase enzymes and process optimizations to reduce allergenic gliadins in wheat flour
    • Lia, Y. et al. The potential of papain and alcalase enzymes and process optimizations to reduce allergenic gliadins in wheat flour. Food Chem. 196, 1338–1345 (2016).
    • (2016) Food Chem. , vol.196 , pp. 1338-1345
    • Lia, Y.1
  • 20
    • 84856192092 scopus 로고    scopus 로고
    • Update on celiac disease - etiology, differential diagnosis, drug targets, and management advances
    • PID: 22235174
    • Scanlon, S. A. & Murray, J. A. Update on celiac disease - etiology, differential diagnosis, drug targets, and management advances. Clin. Exp. Gastroenterol. 4, 297–311 (2011).
    • (2011) Clin. Exp. Gastroenterol. , vol.4 , pp. 297-311
    • Scanlon, S.A.1    Murray, J.A.2
  • 21
    • 84964607666 scopus 로고    scopus 로고
    • Innate and adaptive immunity in self-reported nonceliac gluten sensitivity versus celiac disease
    • Di Sabatino, A. et al. Innate and adaptive immunity in self-reported nonceliac gluten sensitivity versus celiac disease. Dig. Liver Dis. 48, 745–752 (2016).
    • (2016) Dig. Liver Dis. , vol.48 , pp. 745-752
    • Di Sabatino, A.1
  • 22
    • 27744526778 scopus 로고    scopus 로고
    • Gliadin fragments induce phenotypic and functional maturation of human dendritic cells
    • Palová-Jelínková, L. et al. Gliadin fragments induce phenotypic and functional maturation of human dendritic cells. J. Immunol. 175, 7038–7045 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 7038-7045
    • Palová-Jelínková, L.1
  • 23
    • 71249096411 scopus 로고    scopus 로고
    • Serum cytokine elevations in celiac disease: association with disease presentation
    • COI: 1:CAS:528:DC%2BD1MXhsFGgsbzE
    • Manavalan, J. S. et al. Serum cytokine elevations in celiac disease: association with disease presentation. Hum. Immunol. 71, 50–57 (2010).
    • (2010) Hum. Immunol. , vol.71 , pp. 50-57
    • Manavalan, J.S.1
  • 24
    • 85021400055 scopus 로고    scopus 로고
    • Lymphocytic duodenitis or microscopic enteritis and gluten-related conditions: what needs to be explored?
    • PID: 28655974
    • Ierardi, E. et al. Lymphocytic duodenitis or microscopic enteritis and gluten-related conditions: what needs to be explored? Ann. Gastroenterol. 30, 380–392 (2017).
    • (2017) Ann. Gastroenterol. , vol.30 , pp. 380-392
    • Ierardi, E.1
  • 25
    • 34547892654 scopus 로고    scopus 로고
    • Serum IL-8 in patients with dermatitis herpetiformis is produced in response to dietary gluten
    • COI: 1:CAS:528:DC%2BD2sXptVWht7o%3D
    • Hall, R. P. 3rd et al. Serum IL-8 in patients with dermatitis herpetiformis is produced in response to dietary gluten. J. Invest. Dermatol. 127, 2158–2165 (2007).
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 2158-2165
    • Hall, R.P.1
  • 26
    • 37349016235 scopus 로고    scopus 로고
    • CC chemokine ligand-5 (CCL5/RANTES) and CC chemokine ligand-18 (CCL18/PARC) are specific markers of refractory unstable angina pectoris and are transiently raised during severe ischemic symptoms
    • COI: 1:CAS:528:DC%2BD2sXhtFKmu7fE
    • Kraaijeveld, A. O. et al. CC chemokine ligand-5 (CCL5/RANTES) and CC chemokine ligand-18 (CCL18/PARC) are specific markers of refractory unstable angina pectoris and are transiently raised during severe ischemic symptoms. Circulation 116, 1931–1941 (2007).
    • (2007) Circulation , vol.116 , pp. 1931-1941
    • Kraaijeveld, A.O.1
  • 27
    • 84868523138 scopus 로고    scopus 로고
    • Eotaxin/CCL11 in idiopathic retroperitoneal fibrosis
    • COI: 1:CAS:528:DC%2BC38Xhs1CqsLjJ
    • Mangieri, D. et al. Eotaxin/CCL11 in idiopathic retroperitoneal fibrosis. Nephrol. Dial. Transplant. 27, 3875–3884 (2012).
    • (2012) Nephrol. Dial. Transplant. , vol.27 , pp. 3875-3884
    • Mangieri, D.1
  • 28
    • 84956583081 scopus 로고    scopus 로고
    • Sensitivity to wheat, gluten and FODMAPs in IBS: facts or fiction?
    • De Giorgio, R., Volta, U. & Gibson, P. R. Sensitivity to wheat, gluten and FODMAPs in IBS: facts or fiction? Gut 65, 169–178 (2016).
    • (2016) Gut , vol.65 , pp. 169-178
    • De Giorgio, R.1    Volta, U.2    Gibson, P.R.3
  • 29
    • 85016173475 scopus 로고    scopus 로고
    • Nutrition wheat amylase-trypsin inhibitors promote intestinal inflammation via activation of myeloid cells
    • COI: 1:CAS:528:DC%2BC2sXltVWksro%3D
    • Zevallos, V. F. et al. Nutrition wheat amylase-trypsin inhibitors promote intestinal inflammation via activation of myeloid cells. Gastroenterol 152, 1100–1113 (2017).
    • (2017) Gastroenterol , vol.152 , pp. 1100-1113
    • Zevallos, V.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.