Purification and Functional Characterization of the Chloroform/Methanol-Soluble Protein 3 (CM3) From Triticum aestivum in Drosophila melanogaster
Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity...
Uloženo v:
| Vydáno v: | Frontiers in nutrition (Lausanne) Ročník 7; s. 607937 |
|---|---|
| Hlavní autoři: | , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
Switzerland
Frontiers Media S.A
23.12.2020
|
| Témata: | |
| ISSN: | 2296-861X, 2296-861X |
| On-line přístup: | Získat plný text |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity of amylase trypsin inhibitors (ATIs) in modern wheat is suggested to be major trigger of NCWS, while underlying mechanisms still remain elusive. Here, we aimed to generate and functionally characterize the most abundant ATI in modern wheat, chloroform/methanol-soluble protein 3 (CM3),
in vitro
and in
Drosophila melanogaster
. We demonstrate that CM3 displays α-glucosidase but not α-amylase or trypsin inhibitory activity
in vitro
. Moreover, fruit flies fed a sucrose-containing diet together with CM3 displayed significant overgrowth of intestinal bacteria in a sucrose-dependent manner while the consumption of α-amylase and α-glucosidase inhibitors was sufficient to limit bacterial quantities in the intestine. Notably, both CM3 and acarbose-treated flies showed a reduced lifespan. However, this effect was absent in amylase inhibitor (AI) treated flies. Together, given α-glucosidase is a crucial requirement for disaccharide digestion, we suggest that inhibition of α-glucosidase by CM3 enhances disaccharide load in the distal gastrointestinal tract, thereby promoting intestinal bacteria overgrowth. However, it remains speculative if this here described former unknown function of CM3 might contribute to the development of gastrointestinal symptoms observed in NCWS patients which are very similar to symptoms of patients with small intestinal bacterial overgrowth. |
|---|---|
| AbstractList | Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity of amylase trypsin inhibitors (ATIs) in modern wheat is suggested to be major trigger of NCWS, while underlying mechanisms still remain elusive. Here, we aimed to generate and functionally characterize the most abundant ATI in modern wheat, chloroform/methanol-soluble protein 3 (CM3), in vitro and in Drosophila melanogaster. We demonstrate that CM3 displays α-glucosidase but not α-amylase or trypsin inhibitory activity in vitro. Moreover, fruit flies fed a sucrose-containing diet together with CM3 displayed significant overgrowth of intestinal bacteria in a sucrose-dependent manner while the consumption of α-amylase and α-glucosidase inhibitors was sufficient to limit bacterial quantities in the intestine. Notably, both CM3 and acarbose-treated flies showed a reduced lifespan. However, this effect was absent in amylase inhibitor (AI) treated flies. Together, given α-glucosidase is a crucial requirement for disaccharide digestion, we suggest that inhibition of α-glucosidase by CM3 enhances disaccharide load in the distal gastrointestinal tract, thereby promoting intestinal bacteria overgrowth. However, it remains speculative if this here described former unknown function of CM3 might contribute to the development of gastrointestinal symptoms observed in NCWS patients which are very similar to symptoms of patients with small intestinal bacterial overgrowth. Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity of amylase trypsin inhibitors (ATIs) in modern wheat is suggested to be major trigger of NCWS, while underlying mechanisms still remain elusive. Here, we aimed to generate and functionally characterize the most abundant ATI in modern wheat, chloroform/methanol-soluble protein 3 (CM3), in vitro and in Drosophila melanogaster. We demonstrate that CM3 displays α-glucosidase but not α-amylase or trypsin inhibitory activity in vitro. Moreover, fruit flies fed a sucrose-containing diet together with CM3 displayed significant overgrowth of intestinal bacteria in a sucrose-dependent manner while the consumption of α-amylase and α-glucosidase inhibitors was sufficient to limit bacterial quantities in the intestine. Notably, both CM3 and acarbose-treated flies showed a reduced lifespan. However, this effect was absent in amylase inhibitor (AI) treated flies. Together, given α-glucosidase is a crucial requirement for disaccharide digestion, we suggest that inhibition of α-glucosidase by CM3 enhances disaccharide load in the distal gastrointestinal tract, thereby promoting intestinal bacteria overgrowth. However, it remains speculative if this here described former unknown function of CM3 might contribute to the development of gastrointestinal symptoms observed in NCWS patients which are very similar to symptoms of patients with small intestinal bacterial overgrowth.Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity of amylase trypsin inhibitors (ATIs) in modern wheat is suggested to be major trigger of NCWS, while underlying mechanisms still remain elusive. Here, we aimed to generate and functionally characterize the most abundant ATI in modern wheat, chloroform/methanol-soluble protein 3 (CM3), in vitro and in Drosophila melanogaster. We demonstrate that CM3 displays α-glucosidase but not α-amylase or trypsin inhibitory activity in vitro. Moreover, fruit flies fed a sucrose-containing diet together with CM3 displayed significant overgrowth of intestinal bacteria in a sucrose-dependent manner while the consumption of α-amylase and α-glucosidase inhibitors was sufficient to limit bacterial quantities in the intestine. Notably, both CM3 and acarbose-treated flies showed a reduced lifespan. However, this effect was absent in amylase inhibitor (AI) treated flies. Together, given α-glucosidase is a crucial requirement for disaccharide digestion, we suggest that inhibition of α-glucosidase by CM3 enhances disaccharide load in the distal gastrointestinal tract, thereby promoting intestinal bacteria overgrowth. However, it remains speculative if this here described former unknown function of CM3 might contribute to the development of gastrointestinal symptoms observed in NCWS patients which are very similar to symptoms of patients with small intestinal bacterial overgrowth. Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity of amylase trypsin inhibitors (ATIs) in modern wheat is suggested to be major trigger of NCWS, while underlying mechanisms still remain elusive. Here, we aimed to generate and functionally characterize the most abundant ATI in modern wheat, chloroform/methanol-soluble protein 3 (CM3), and in . We demonstrate that CM3 displays α-glucosidase but not α-amylase or trypsin inhibitory activity . Moreover, fruit flies fed a sucrose-containing diet together with CM3 displayed significant overgrowth of intestinal bacteria in a sucrose-dependent manner while the consumption of α-amylase and α-glucosidase inhibitors was sufficient to limit bacterial quantities in the intestine. Notably, both CM3 and acarbose-treated flies showed a reduced lifespan. However, this effect was absent in amylase inhibitor (AI) treated flies. Together, given α-glucosidase is a crucial requirement for disaccharide digestion, we suggest that inhibition of α-glucosidase by CM3 enhances disaccharide load in the distal gastrointestinal tract, thereby promoting intestinal bacteria overgrowth. However, it remains speculative if this here described former unknown function of CM3 might contribute to the development of gastrointestinal symptoms observed in NCWS patients which are very similar to symptoms of patients with small intestinal bacterial overgrowth. Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain, flatulence) and extra-intestinal symptoms (e.g., headache, fatigue), which are propagated following the ingestion of wheat products. Increased activity of amylase trypsin inhibitors (ATIs) in modern wheat is suggested to be major trigger of NCWS, while underlying mechanisms still remain elusive. Here, we aimed to generate and functionally characterize the most abundant ATI in modern wheat, chloroform/methanol-soluble protein 3 (CM3), in vitro and in Drosophila melanogaster . We demonstrate that CM3 displays α-glucosidase but not α-amylase or trypsin inhibitory activity in vitro . Moreover, fruit flies fed a sucrose-containing diet together with CM3 displayed significant overgrowth of intestinal bacteria in a sucrose-dependent manner while the consumption of α-amylase and α-glucosidase inhibitors was sufficient to limit bacterial quantities in the intestine. Notably, both CM3 and acarbose-treated flies showed a reduced lifespan. However, this effect was absent in amylase inhibitor (AI) treated flies. Together, given α-glucosidase is a crucial requirement for disaccharide digestion, we suggest that inhibition of α-glucosidase by CM3 enhances disaccharide load in the distal gastrointestinal tract, thereby promoting intestinal bacteria overgrowth. However, it remains speculative if this here described former unknown function of CM3 might contribute to the development of gastrointestinal symptoms observed in NCWS patients which are very similar to symptoms of patients with small intestinal bacterial overgrowth. |
| Author | Ragab, Mohab Derer, Stefanie Wagner, Anika E. Sina, Christian Thiel, Anna-Lena Divanovic, Senad |
| AuthorAffiliation | 6 Institute of Nutritional Medicine and 1st Department of Medicine, Section of Nutritional Medicine, University Hospital Schleswig-Holstein, Campus Lübeck , Lübeck , Germany 3 Department of Pediatrics, University of Cincinnati College of Medicine , Cincinnati, OH , United States 2 Institute of Nutritional Sciences, Nutrition and Immune System, Justus-Liebig University Giessen , Giessen , Germany 4 Division of Immunobiology, Cincinnati Children's Hospital Medical Center , Cincinnati, OH , United States 1 Institute of Nutritional Medicine, Molecular Gastroenterology, University Hospital Schleswig-Holstein, Campus Lübeck , Lübeck , Germany 5 Center for Inflammation and Tolerance, Cincinnati Children's Hospital Medical Center , Cincinnati, OH , United States |
| AuthorAffiliation_xml | – name: 3 Department of Pediatrics, University of Cincinnati College of Medicine , Cincinnati, OH , United States – name: 6 Institute of Nutritional Medicine and 1st Department of Medicine, Section of Nutritional Medicine, University Hospital Schleswig-Holstein, Campus Lübeck , Lübeck , Germany – name: 4 Division of Immunobiology, Cincinnati Children's Hospital Medical Center , Cincinnati, OH , United States – name: 2 Institute of Nutritional Sciences, Nutrition and Immune System, Justus-Liebig University Giessen , Giessen , Germany – name: 1 Institute of Nutritional Medicine, Molecular Gastroenterology, University Hospital Schleswig-Holstein, Campus Lübeck , Lübeck , Germany – name: 5 Center for Inflammation and Tolerance, Cincinnati Children's Hospital Medical Center , Cincinnati, OH , United States |
| Author_xml | – sequence: 1 givenname: Anna-Lena surname: Thiel fullname: Thiel, Anna-Lena – sequence: 2 givenname: Mohab surname: Ragab fullname: Ragab, Mohab – sequence: 3 givenname: Anika E. surname: Wagner fullname: Wagner, Anika E. – sequence: 4 givenname: Senad surname: Divanovic fullname: Divanovic, Senad – sequence: 5 givenname: Stefanie surname: Derer fullname: Derer, Stefanie – sequence: 6 givenname: Christian surname: Sina fullname: Sina, Christian |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33425975$$D View this record in MEDLINE/PubMed |
| BookMark | eNp1Uk1vEzEQXaEiWkrvnNAeyyGpP3b9cUFCgUClVlSiSNysiXecuPKug9dbCf4F_xinKVWLxMnjmTfvjWbey-pgiANW1WtK5pwrfeaGKc8ZYWQuiNRcPquOGNNipgT9fvAoPqxOxvGGEEI5axvavKgOOW9Yq2V7VP2-mpJ33kL2cahh6OrlNNjdB0K92EACmzH5X_t6dHXeYMmHmKKLqT-7xLyBIYbZ1ximVcD6KsWMfqh5fbq45G_rZYp9fZ189nbqa8Ax-9sSFMSHFMe43fgAdY-hkKxhLFqvqucOwogn9-9x9W358XrxeXbx5dP54v3FzDaC5VkHKGSnEJlTjW1d2zELimnQlBNnFTYNVVToRjvS2haILQGXK0QlQIiOH1fne94uwo3ZJt9D-mkieHOXiGltIJWpAxpECtgRyagUDScaOulU55BqpQWTq8L1bs-1nVY9dhaHnCA8IX1aGfzGrOOtkVK1ivBCcHpPkOKPqSzJ9H60GMpaME6jYY0UqiWtYAX65rHWg8jfmxYA2QNsWfCY0D1AKDE755idc8zOOWbvnNIi_mmxPt-dvEzrw_8b_wD2-8x9 |
| CitedBy_id | crossref_primary_10_3389_fmolb_2022_868568 crossref_primary_10_1016_j_ejphar_2025_178028 crossref_primary_10_1007_s11357_022_00722_0 |
| Cites_doi | 10.1016/S0278-6915(99)00143-X 10.1016/S0889-8529(05)70266-8 10.1080/01140671.2012.722112 10.2165/00044011-200727060-00003 10.3390/ijms21165817 10.3748/wjg.v16.i24.2978 10.1016/S0149-2918(98)80089-1 10.1016/0305-0491(89)90387-8 10.1242/dmm.003970 10.1007/s005920050098 10.1084/jem.20102660 10.3791/50068 10.1016/0005-2744(81)90309-0 10.1097/ACI.0b013e32832aa5bc 10.1016/j.molimm.2017.08.003 10.1016/j.diabres.2010.12.033 10.1016/0305-0491(88)90275-1 10.1186/1756-0500-4-242 10.1152/advan.00094.2009 10.1016/j.chom.2009.10.001 10.3389/fnut.2020.00006 10.1007/978-94-011-4431-5_26 10.1136/openhrt-2015-000327 10.1186/s12263-019-0641-y 10.1016/j.jaci.2018.02.041 10.1053/j.gastro.2016.12.006 10.1016/j.gtc.2017.09.008 10.1007/112_2015_24 10.1016/0014-5793(90)80642-V 10.1007/BF00498936 10.1016/S0168-8227(01)00221-2 10.1146/annurev-genet-111212-133343 10.1021/jf305122s 10.1126/sciadv.aba0353 10.2147/DMSO.S28340 10.3748/wjg.v23.i40.7201 10.1016/j.celrep.2014.08.064 10.1007/978-94-011-4431-5_27 10.3389/fnut.2020.517313 10.18632/oncotarget.5215 10.1016/S0140-6736(02)08905-5 10.2165/00044011-200525100-00004 10.1371/journal.pone.0226478 10.1080/07853890.2017.1325968 10.3390/plants7040101 10.1016/j.metabol.2004.10.004 10.1186/1477-5956-9-10 10.1111/ijfs.13605 10.1016/S0981-9428(03)00113-X 10.1038/s41598-017-13709-1 |
| ContentType | Journal Article |
| Copyright | Copyright © 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina. Copyright © 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina. 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina |
| Copyright_xml | – notice: Copyright © 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina. – notice: Copyright © 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina. 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina |
| DBID | AAYXX CITATION NPM 7X8 5PM DOA |
| DOI | 10.3389/fnut.2020.607937 |
| DatabaseName | CrossRef PubMed MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
| DatabaseTitle | CrossRef PubMed MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic PubMed CrossRef |
| Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Diet & Clinical Nutrition |
| EISSN | 2296-861X |
| ExternalDocumentID | oai_doaj_org_article_ee1aed0721764309ad7f8dfe1989627b PMC7785803 33425975 10_3389_fnut_2020_607937 |
| Genre | Journal Article |
| GrantInformation_xml | – fundername: Deutsche Forschungsgemeinschaft grantid: IRTG1911-A6 |
| GroupedDBID | 53G 5VS 9T4 AAFWJ AAYXX ACGFS ADBBV ADRAZ AFPKN ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BCNDV CITATION DIK GROUPED_DOAJ HYE KQ8 M48 M~E OK1 PGMZT RPM ACXDI IAO ICW IEA IHR IHW IPNFZ NPM RIG 7X8 5PM |
| ID | FETCH-LOGICAL-c462t-dae67d8ee2f84c5f5d2ca829a9130fc8e441816949f05c5a0c9f037bee86a66d3 |
| IEDL.DBID | DOA |
| ISICitedReferencesCount | 3 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000604938200001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 2296-861X |
| IngestDate | Fri Oct 03 12:46:43 EDT 2025 Tue Sep 30 16:59:27 EDT 2025 Thu Oct 02 10:24:51 EDT 2025 Thu Jan 02 22:57:38 EST 2025 Sat Nov 29 06:26:37 EST 2025 Tue Nov 18 20:47:32 EST 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | CM3 non-celiac wheat sensitivity α-glucosidase ATIs Drosophila melanogaster |
| Language | English |
| License | Copyright © 2020 Thiel, Ragab, Wagner, Divanovic, Derer and Sina. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c462t-dae67d8ee2f84c5f5d2ca829a9130fc8e441816949f05c5a0c9f037bee86a66d3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors share senior authorship Reviewed by: Alberto Barbiroli, University of Milan, Italy; Alessio Scarafoni, University of Milan, Italy This article was submitted to Food Chemistry, a section of the journal Frontiers in Nutrition These authors have contributed equally to this work Edited by: Marcello Iriti, University of Milan, Italy Present address: Anika E. Wagner, Institute of Nutritional Sciences, Justus-Liebig-University Giessen, Giessen, Germany |
| OpenAccessLink | https://doaj.org/article/ee1aed0721764309ad7f8dfe1989627b |
| PMID | 33425975 |
| PQID | 2476850562 |
| PQPubID | 23479 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_ee1aed0721764309ad7f8dfe1989627b pubmedcentral_primary_oai_pubmedcentral_nih_gov_7785803 proquest_miscellaneous_2476850562 pubmed_primary_33425975 crossref_primary_10_3389_fnut_2020_607937 crossref_citationtrail_10_3389_fnut_2020_607937 |
| PublicationCentury | 2000 |
| PublicationDate | 2020-12-23 |
| PublicationDateYYYYMMDD | 2020-12-23 |
| PublicationDate_xml | – month: 12 year: 2020 text: 2020-12-23 day: 23 |
| PublicationDecade | 2020 |
| PublicationPlace | Switzerland |
| PublicationPlace_xml | – name: Switzerland |
| PublicationTitle | Frontiers in nutrition (Lausanne) |
| PublicationTitleAlternate | Front Nutr |
| PublicationYear | 2020 |
| Publisher | Frontiers Media S.A |
| Publisher_xml | – name: Frontiers Media S.A |
| References | Inomata (B5) 2009; 9 Mertes (B48) 2001; 52 Gómez (B3) 1990; 261 Altenbach (B14) 2011; 4 DiNicolantonio (B32) 2015; 2 Khazaei (B45) 2020; 6 Hooton (B31) 2015; 168 Wagner (B29) 2015; 6 Apidianakis (B26) 2011; 4 Lebovitz (B23) 1997; 26 Fujisawa (B41) 2005; 54 Li (B51) 2011; 92 Sharma (B8) 2020; 7 Cuccioloni (B6) 2017; 7 Spengler (B49) 2005; 25 Rosak (B46) 2012; 5 Hickey (B36) 1982; 20 Chng (B39) 2014; 9 Valenti (B1) 2017; 49 Gélinas (B22) 2018; 53 García Olmedo (B17) 1987; 4 Pitsouli (B34) 2009; 6 Pan (B50) 2007; 27 Clemente (B7) 2019; 14 Priya (B12) 2013; 41 Sünderhauf (B30) 2017; 90 Kalunke (B20) 2020; 21 Tundo (B19) 2018; 7 Kusaba-Nakayama (B4) 2000; 38 Junker (B15) 2012; 209 Kasarda (B9) 2013; 61 Mancinelli (B33) 2003; 41 Bures (B43) 2010; 16 Igbinedion (B10) 2017; 23 Klarenberg (B37) 1988; 89 Zevallos (B27) 2017; 152 Chiasson (B40) 2002; 359 Milanovic (B38) 1989; 93 Buse (B47) 1998; 20 Lemaitre (B25) 2013; 47 Wieser (B2) 2020; 7 Santeusanio (B52) 1993; 6 Adike (B44) 2018; 47 Fischer (B53) 1998; 35 Carbonero (B13) 1999; 26 O'Connor (B16) 1981; 658 Domoney (B11) 1999; 27 Dukowicz (B42) 2007; 3 Goodman (B24) 2010; 34 Linford (B28) 2013; 71 Dupont (B18) 2011; 9 Baenas (B35) 2019; 14 Bellinghausen (B21) 2019; 143 |
| References_xml | – volume: 38 start-page: 179 year: 2000 ident: B4 article-title: CM3, one of the wheat α-amylase inhibitor subunits, and binding of IgE in sera from Japanese with atopic dermatitis related to wheat publication-title: Food Chem Toxicol doi: 10.1016/S0278-6915(99)00143-X – volume: 26 start-page: 539 year: 1997 ident: B23 article-title: Alpha-glucosidase inhibitors publication-title: Endocrinol Metab Clin North Am doi: 10.1016/S0889-8529(05)70266-8 – volume: 41 start-page: 49 year: 2013 ident: B12 article-title: Specificity of α-amylase and trypsin inhibitor proteins in wheat against insect pests publication-title: N Z J Crop Horticult Sci doi: 10.1080/01140671.2012.722112 – volume: 27 start-page: 397 year: 2007 ident: B50 article-title: Post-marketing surveillance of acarbose treatment in patients with type 2 diabetes mellitus and subjects with impaired glucose tolerance in China publication-title: Clin Drug Investig doi: 10.2165/00044011-200727060-00003 – volume: 21 start-page: 5817 year: 2020 ident: B20 article-title: Reduction of allergenic potential in bread wheat rnai transgenic lines silenced for cm3, cm16 and 0.28 ati genes publication-title: Int J Mol Sci doi: 10.3390/ijms21165817 – volume: 16 start-page: 2978 year: 2010 ident: B43 article-title: Small intestinal bacterial overgrowth syndrome publication-title: World J Gastroenterol doi: 10.3748/wjg.v16.i24.2978 – volume: 20 start-page: 257 year: 1998 ident: B47 article-title: The PROTECT study: final results of a large multicenter postmarketing study in patients with type 2 diabetes publication-title: Clin Ther doi: 10.1016/S0149-2918(98)80089-1 – volume: 93 start-page: 629 year: 1989 ident: B38 article-title: Adaptive significance of amylase polymorphism in Drosophila IV. A comparative study of biochemical properties of the alpha-amylase in publication-title: Drosophila melanogaster, D hydei doi: 10.1016/0305-0491(89)90387-8 – volume: 4 start-page: 21 year: 2011 ident: B26 article-title: Drosophila melanogaster as a model for human intestinal infection and pathology publication-title: Dis Model Mech doi: 10.1242/dmm.003970 – volume: 35 start-page: 34 year: 1998 ident: B53 article-title: European study on dose-response relationship of acarbose as a first-line drug in non-insulin-dependent diabetes mellitus: efficacy and safety of low and high doses publication-title: Acta Diabetol doi: 10.1007/s005920050098 – volume: 209 start-page: 2395 year: 2012 ident: B15 article-title: Wheat amylase trypsin inhibitors drive intestinal inflammation via activation of toll-like receptor 4 publication-title: J Exp Med doi: 10.1084/jem.20102660 – volume: 71 start-page: 50068 year: 2013 ident: B28 article-title: Measurement of lifespan in Drosophila melanogaster publication-title: J Vis Exp doi: 10.3791/50068 – volume: 658 start-page: 387 year: 1981 ident: B16 article-title: Isolation and characterization of four inhibitors from wheat flour which display differential inhibition specificities for human salivary and human pancreatic α-amylases publication-title: Biochim Biophys Acta doi: 10.1016/0005-2744(81)90309-0 – volume: 9 start-page: 238 year: 2009 ident: B5 article-title: Wheat allergy publication-title: Curr Opin Allergy Clin Immunol doi: 10.1097/ACI.0b013e32832aa5bc – volume: 90 start-page: 227 year: 2017 ident: B30 article-title: Regulation of epithelial cell expressed C3 in the intestine—relevance for the pathophysiology of inflammatory bowel disease? publication-title: Mol Immunol doi: 10.1016/j.molimm.2017.08.003 – volume: 4 start-page: 275 year: 1987 ident: B17 article-title: Plant proteinaceous inhibitors of proteinases and α-amylases publication-title: Oxf Surv Plant Mol Cell Biol. – volume: 92 start-page: 57 year: 2011 ident: B51 article-title: International non-interventional study of acarbose treatment in patients with type 2 diabetes mellitus publication-title: Diabetes Res Clin Pract doi: 10.1016/j.diabres.2010.12.033 – volume: 89 start-page: 143 year: 1988 ident: B37 article-title: Genetic and dietary regulation of tissue-specific expression patterns of α-amylase in larvae of Drosophila melanogaster publication-title: Comp Biochem Physiol doi: 10.1016/0305-0491(88)90275-1 – volume: 4 start-page: 242 year: 2011 ident: B14 article-title: The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86 publication-title: BMC Res Notes doi: 10.1186/1756-0500-4-242 – volume: 34 start-page: 44 year: 2010 ident: B24 article-title: Insights into digestion and absorption of major nutrients in humans publication-title: Adv Physiol Educ doi: 10.1152/advan.00094.2009 – volume: 6 start-page: 301 year: 2009 ident: B34 article-title: Homeostasis in infected epithelia: stem cells take the lead publication-title: Cell Host Microbe doi: 10.1016/j.chom.2009.10.001 – volume: 7 start-page: 6 year: 2020 ident: B8 article-title: Pathogenesis of celiac disease and other gluten related disorders in wheat and strategies for mitigating them publication-title: Front Nutr doi: 10.3389/fnut.2020.00006 – volume: 6 start-page: 147 year: 1993 ident: B52 article-title: Efficacy and safety of two different dosages of acarbose in non-insulin dependent diabetic patients treated by diet alone publication-title: Diabetes Nutr Metab – volume: 26 start-page: 617 year: 1999 ident: B13 article-title: A multigene family of trypsin/α-amylase inhibitors from cereals publication-title: Seed Proteins doi: 10.1007/978-94-011-4431-5_26 – volume: 3 start-page: 112 year: 2007 ident: B42 article-title: Small intestinal bacterial overgrowth: a comprehensive review publication-title: Gastroenterol Hepatol – volume: 2 start-page: e000327 year: 2015 ident: B32 article-title: Acarbose: safe and effective for lowering postprandial hyperglycaemia and improving cardiovascular outcomes publication-title: Open Heart doi: 10.1136/openhrt-2015-000327 – volume: 14 start-page: 14 year: 2019 ident: B35 article-title: Drosophila melanogaster as an alternative model organism in nutrigenomics publication-title: Genes Nutr doi: 10.1186/s12263-019-0641-y – volume: 143 start-page: 201 year: 2019 ident: B21 article-title: Wheat amylase-trypsin inhibitors exacerbate intestinal and airway allergic immune responses in humanized mice publication-title: J Allergy Clin Immunol doi: 10.1016/j.jaci.2018.02.041 – volume: 152 start-page: 1100 year: 2017 ident: B27 article-title: Nutritional wheat amylase-trypsin inhibitors promote intestinal inflammation via activation of myeloid cells publication-title: Gastroenterology doi: 10.1053/j.gastro.2016.12.006 – volume: 47 start-page: 193 year: 2018 ident: B44 article-title: Small intestinal bacterial overgrowth: nutritional implications, diagnosis, and management publication-title: Gastroenterol Clin North Am doi: 10.1016/j.gtc.2017.09.008 – volume: 168 start-page: 59 year: 2015 ident: B31 article-title: The secretion and action of brush border enzymes in the mammalian small intestine publication-title: Rev Physiol Biochem Pharmacol doi: 10.1007/112_2015_24 – volume: 261 start-page: 85 year: 1990 ident: B3 article-title: Members of the α-amylase inhibitors family from wheat endosperm are major allergens associated with baker's asthma publication-title: FEBS Lett doi: 10.1016/0014-5793(90)80642-V – volume: 20 start-page: 1117 year: 1982 ident: B36 article-title: Regulation of amylase activity in Drosophila melanogaster: effects of dietary carbohydrate publication-title: Biochem Genet doi: 10.1007/BF00498936 – volume: 52 start-page: 193 year: 2001 ident: B48 article-title: Safety and efficacy of acarbose in the treatment of Type 2 diabetes: data from a 5-years surveillance study publication-title: Diabetes Res Clin Pract doi: 10.1016/S0168-8227(01)00221-2 – volume: 47 start-page: 377 year: 2013 ident: B25 article-title: The digestive tract of Drosophila melanogaster publication-title: Annu Rev Genet doi: 10.1146/annurev-genet-111212-133343 – volume: 61 start-page: 1155 year: 2013 ident: B9 article-title: Can an increase in celiac disease be attributed to an increase in the gluten content of wheat as a consequence of wheat breeding? publication-title: J Agric Food Chem doi: 10.1021/jf305122s – volume: 6 start-page: eaba0353 year: 2020 ident: B45 article-title: Metabolic multi-stability and hysteresis in a model aerobe-anaerobe microbiome community publication-title: Sci Adv doi: 10.1126/sciadv.aba0353 – volume: 5 start-page: 357 year: 2012 ident: B46 article-title: Critical evaluation of the role of acarbose in the treatment of diabetes: patient considerations publication-title: Diabetes Metab Syndr Obes doi: 10.2147/DMSO.S28340 – volume: 23 start-page: 7201 year: 2017 ident: B10 article-title: Non-celiac gluten sensitivity: all wheat attack is not celiac publication-title: World J Gastroenterol doi: 10.3748/wjg.v23.i40.7201 – volume: 9 start-page: 336 year: 2014 ident: B39 article-title: Transforming growth factor β/activin signaling functions as a sugar-sensing feedback loop to regulate digestive enzyme expression publication-title: Cell Rep doi: 10.1016/j.celrep.2014.08.064 – volume: 27 start-page: 635 year: 1999 ident: B11 article-title: Inhibitors of legume seeds publication-title: Seed Proteins doi: 10.1007/978-94-011-4431-5_27 – volume: 7 start-page: 517313 year: 2020 ident: B2 article-title: The two faces of wheat publication-title: Front Nutr doi: 10.3389/fnut.2020.517313 – volume: 6 start-page: 30568 year: 2015 ident: B29 article-title: Epigallocatechin gallate affects glucose metabolism and increases fitness and lifespan in Drosophila melanogaster publication-title: Oncotarget doi: 10.18632/oncotarget.5215 – volume: 359 start-page: 2072 year: 2002 ident: B40 article-title: Acarbose for prevention of type 2 diabetes mellitus: the STOP-NIDDM randomised trial publication-title: Lancet doi: 10.1016/S0140-6736(02)08905-5 – volume: 25 start-page: 651 year: 2005 ident: B49 article-title: Evaluation of the efficacy and tolerability of acarbose in patients with diabetes mellitus a postmarketing surveillance study publication-title: Clin Drug Investig doi: 10.2165/00044011-200525100-00004 – volume: 14 start-page: e0226478 year: 2019 ident: B7 article-title: An explorative study identifies miRNA signatures for the diagnosis of non-celiac wheat sensitivity publication-title: PLoS ONE doi: 10.1371/journal.pone.0226478 – volume: 49 start-page: 569 year: 2017 ident: B1 article-title: Gluten-related disorders: certainties, questions and doubts publication-title: Ann Med doi: 10.1080/07853890.2017.1325968 – volume: 7 start-page: 1 year: 2018 ident: B19 article-title: Wheat ati cm3, cm16 and 0.28 allergens produced in pichia pastoris display a different eliciting potential in food allergy to wheat publication-title: Plants doi: 10.3390/plants7040101 – volume: 54 start-page: 387 year: 2005 ident: B41 article-title: Effect of two α-glucosidase inhibitors, voglibose and acarbose, on postprandial hyperglycemia correlates with subjective abdominal symptoms publication-title: Metabolism doi: 10.1016/j.metabol.2004.10.004 – volume: 9 start-page: 10 year: 2011 ident: B18 article-title: Deciphering the complexities of the wheat flour proteome using quantitative two-dimensional electrophoresis, three proteases and tandem mass spectrometry publication-title: Proteome Sci doi: 10.1186/1477-5956-9-10 – volume: 53 start-page: 467 year: 2018 ident: B22 article-title: Inhibitory activity towards human α-amylase in wheat flour and gluten publication-title: Int J Food Sci Technol doi: 10.1111/ijfs.13605 – volume: 41 start-page: 705 year: 2003 ident: B33 article-title: The CM2 and CM3 types of α-amylase inhibitor are associated with Triticum aestivum seed chromatin publication-title: Plant Physiol Biochem doi: 10.1016/S0981-9428(03)00113-X – volume: 7 start-page: 4 year: 2017 ident: B6 article-title: Interfering with the high-affinity interaction between wheat amylase trypsin inhibitor CM3 and toll-like receptor 4: in silico and biosensor-based studies publication-title: Sci Rep doi: 10.1038/s41598-017-13709-1 |
| SSID | ssj0001325414 |
| Score | 2.1511698 |
| Snippet | Non-celiac wheat sensitivity (NCWS) has been proposed to be an independent disease entity that is characterized by intestinal (e.g., abdominal pain,... |
| SourceID | doaj pubmedcentral proquest pubmed crossref |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | 607937 |
| SubjectTerms | ATIs CM3 Drosophila melanogaster non-celiac wheat sensitivity Nutrition α-glucosidase |
| Title | Purification and Functional Characterization of the Chloroform/Methanol-Soluble Protein 3 (CM3) From Triticum aestivum in Drosophila melanogaster |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/33425975 https://www.proquest.com/docview/2476850562 https://pubmed.ncbi.nlm.nih.gov/PMC7785803 https://doaj.org/article/ee1aed0721764309ad7f8dfe1989627b |
| Volume | 7 |
| WOSCitedRecordID | wos000604938200001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVAON databaseName: DOAJ Directory of Open Access Journals customDbUrl: eissn: 2296-861X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001325414 issn: 2296-861X databaseCode: DOA dateStart: 20140101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVHPJ databaseName: ROAD: Directory of Open Access Scholarly Resources customDbUrl: eissn: 2296-861X dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001325414 issn: 2296-861X databaseCode: M~E dateStart: 20140101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lj9MwELZgxYEL4k14rIyEEHsITezEjyN0t-LSqodF6i1y4jFUSpNVt90j_4F_zIzTVluE4MIlshInsTyfMw9PvmHsnQXvgsldqlwt0sK5kDqERqqCVYVFh8WJOhab0LOZWSzs_FapL8oJG-iBh4kbAeQOPLF4aVSemXVeB-MDUK6PErqmry9aPbecqRhdkYLqWw_7kuiF2VHotpQ6KbKPKnLCHemhSNf_Jxvz91TJW7pn8pA92BmN_NMw2EfsDnSPWXK-hA1_z3fMni2f7Yn1n7Cf8-2acoDitHPXeT5B_TWE_fj4wNE8_ILJ-8DRDMTz6Lv3ZMSOpkAR9b5NKWpWt8DnROew7LjkH8ZTecYn637FL2OZhO2KO6LquMEG9jhfx8oIy9bxFbT4kG-OuBiesq-Ti8vxl3RXfCFtCiU2qXegtDcAIpiiKUPpReOMsM6i1guNAbSjTK5sYUNWNqXLGmxIXQMY5ZTy8hk76foOXjAO0JjMOyPrmrgpPYovlyX40hV57rM8YaO9KKpmx0xOBTLaCj0UEl5FwqtIeNUgvISdHe64Glg5_tL3M0n30I_4tOMJRFm1Q1n1L5Ql7O0eGxWuP9pUcR302-tKFOiwRTMyYc8HrBxeJSXC3uoyYfoIRUdjOb7SLb9Hjm-tTWky-fJ_DP4Vu0_zQUk4Qr5mJ5v1Ft6we83NZnm9PmV39cKcxuWDx-mPi1-BXiR2 |
| linkProvider | Directory of Open Access Journals |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Purification+and+Functional+Characterization+of+the+Chloroform%2FMethanol-Soluble+Protein+3+%28CM3%29+From+Triticum+aestivum+in+Drosophila+melanogaster&rft.jtitle=Frontiers+in+nutrition+%28Lausanne%29&rft.au=Thiel%2C+Anna-Lena&rft.au=Ragab%2C+Mohab&rft.au=Wagner%2C+Anika+E&rft.au=Divanovic%2C+Senad&rft.date=2020-12-23&rft.issn=2296-861X&rft.eissn=2296-861X&rft.volume=7&rft.spage=607937&rft_id=info:doi/10.3389%2Ffnut.2020.607937&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2296-861X&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2296-861X&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2296-861X&client=summon |