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...
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| Vydané v: | Frontiers in nutrition (Lausanne) Ročník 7; s. 607937 |
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| Hlavní autori: | , , , , , |
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| Jazyk: | English |
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Switzerland
Frontiers Media S.A
23.12.2020
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| ISSN: | 2296-861X, 2296-861X |
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| 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 |
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| 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 |
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| 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 |
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| 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. |
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| 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 |
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| Title | Purification and Functional Characterization of the Chloroform/Methanol-Soluble Protein 3 (CM3) From Triticum aestivum in Drosophila melanogaster |
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