Functional Variants in the Sucrase–Isomaltase Gene Associate With
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Sucrase-Isomaltase Deficiency Causing Persistent Bloating and Diarrhea in an Adult Female
Open Access Case Report DOI: 10.7759/cureus.14349 Sucrase-Isomaltase Deficiency Causing Persistent Bloating and Diarrhea in an Adult Female Varsha Chiruvella 1 , Ayesha Cheema 1 , Hafiz Muhammad Sharjeel Arshad 2 , Jacqueline T. Chan 3 , John Erikson L. Yap 2 1. Internal Medicine, Medical College of Georgia at Augusta University, Augusta, USA 2. Gastroenterology and Hepatology, Medical College of Georgia at Augusta University, Augusta, USA 3. Pediatric Endocrinology, Medical College of Georgia at Augusta University, Augusta, USA Corresponding author: Varsha Chiruvella, [email protected] Abstract Congenital sucrase isomaltase deficiency (CSID) is an autosomal recessive disorder which leads to chronic intestinal malabsorption of nutrients from ingested starch and sucrose. Symptoms usually present after consumption of fruits, juices, grains, and starches, leading to failure to thrive and malnutrition. Diagnosis is suspected on detailed patient history and confirmed by a disaccharidase assay using small intestinal biopsies or sucrose hydrogen breath test. Treatment of CSID consists of limiting sucrose in diet and replacement therapy with sacrosidase. Due to its nonspecific symptoms, CSID may be undiagnosed in many patients for several years. We present a case of a 50-year-old woman with persistent symptoms of bloating in spite of extensive evaluation and treatment. Categories: Endocrinology/Diabetes/Metabolism, Gastroenterology Keywords: sucrase-isomaltase, starch intolerance, disaccharidase assay, ibs, hydrogen breath test Introduction Congenital sucrase isomaltase deficiency (CSID), also known as genetic sucrase deficiency, is a multifaceted intestinal malabsorption disorder with an autosomal recessive mutation in the sucrase-isomaltase (SI) gene on chromosome 3 (3q25-q26). Sucrase-isomaltase is a type II membrane enzyme complex and member of the disaccharidase family required for the breakdown of α-glycosidic linkages in sucrose and maltose. -
Disaccharidase Deficiencies
J Clin Pathol: first published as 10.1136/jcp.s3-5.1.22 on 1 January 1971. Downloaded from J. clin. Path., 24, Suppl. (Roy. Coll. Path.), 5, 22-28 Disaccharidase deficiencies G. NEALE From the Department ofMedicine, Royal Postgraduate Medical School, Du Cane Road, London Up to 12 years ago the absorption of disaccharides capable of hydrolysing maltose, which may explain was a problem in physiology which attracted little why maltase deficiency is not found as an isolated attention and which appeared to be unrelated to the defect of the enterocyte. Isomaltase and sucrase problems of clinical medicine. Indeed, most text- appear to be distinct but linked entities, and hence books stated incorrectly that the disaccharides were they are absent together in the hereditary condition hydrolysed to monosaccharides in the lumen of the of sucrase-isomaltase deficiency (Dahlquist and small intestine despite the evidence of half a century Telenius, 1969). Lactase activity consists of at least before, which had suggested that they were digested two separate enzymes, one of which is not in the by the mucosal surface (Reid, 1901). The renewal of brush border but within the cell (Zoppi, Hadom, interest in the subject of disaccharide absorption Gitzelmann, Kistler, and Prader, 1966). The signifi- occurred after the description of congenital lactase cance of intracellular lactase activity is uncertain. It deficiency by Holzel, Schwarz, and Sutcliffe (1959) cannot play any part in the normal digestion of and of sucrase-isomaltase deficiency by Weijers, lactose which is a function of the brush border of the van de Kamer, Mossel, and Dicke (1960). -
Intestinal Sucrase Deficiency Presenting As Sucrose Intolerance in Adult Life
BRnUTE 20 November 1965 MEDICAL JOURNAL 1223 Br Med J: first published as 10.1136/bmj.2.5472.1223 on 20 November 1965. Downloaded from Intestinal Sucrase Deficiency Presenting as Sucrose Intolerance in Adult Life G. NEALE,* M.B., M.R.C.P.; M. CLARKt M.B., M.R.C.P.; B. LEVIN,4 M.D., PH.D., F.C.PATH. Brit. med. J., 1965, 2, 1223-1225 Diarrhoea due to failure of the small intestine to hydrolyse studies of the jejunal mucosa. He was discharged from hospital a certain dietary disaccharides is now a well-recognized congenital week after starting a sucrose-free and restricted starch diet and has disorder of infants and children. It was first suggested for since remained well. lactose (Durand, 1958) and later for sucrose (Weijers et al., 1960) and for isomaltose in association with sucrose (Auricchio Methods et al., 1962). It has been confirmed for lactose and for sucrose intolerance by quantitative estimation of enzyme activities in Initially the patient was on a normal ward diet estimated to the intestinal mucosa (Auricchio et al., 1963b; Dahlqvist et al., contain 50-80 g. of sucrose a day. After 10 days sucrose was 1963 ; Burgess et al., 1964; Levin, 1964). In all cases present- eliminated from the diet, and after a further three days starch ing in childhood there is a history of diarrhoea when food intake was restricted to 150 g. a day. Carbohydrate tolerance yielding the relevant disaccharide is introduced into the diet. was determined after an overnight fast by estimating blood Symptoms decrease with age, so that older children may be glucose levels, using a specific glucose oxidase method, after asymptomatic (Burgess et al., 1964) and are able to tolerate ingestion of 50 g. -
SI Gene Sucrase-Isomaltase
SI gene sucrase-isomaltase Normal Function The SI gene provides instructions for producing the enzyme sucrase-isomaltase. This enzyme is found in the intestinal tract, where it is involved in breaking down the sugars sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains). Sucrose and maltose are called disaccharides because they are each made up of two simple sugar molecules. Disaccharides must be broken down into simple sugar molecules to be digested properly. The sucrase-isomaltase enzyme is found on the surface of the intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. The role of the sucrase-isomaltase enzyme is to break down sucrose and maltose into simple sugars so that they can be absorbed by microvilli into intestinal epithelial cells. Health Conditions Related to Genetic Changes Congenital sucrase-isomaltase deficiency At least 10 mutations in the SI gene have been found to cause congenital sucrase- isomaltase deficiency. These mutations disrupt the folding and processing of the sucrose-isomaltase enzyme, transportation of the enzyme within the intestinal epithelial cells, the orientation of the enzyme to the cell surface, or its normal functioning. An impairment in any of these cell processes results in a sucrase-isomaltase enzyme that cannot effectively break down sucrose, maltose, or other compounds made from these sugar molecules (carbohydrates). -
Is There Hidden Sugar in Your Drink?
Is There Hidden Sugar in Your Drink? Anjali Shankar 9th Grade Moravian Academy Upper School June 5th, 2020 Motivation - I have a big passion for the medical field, showed by last year’s project. - Food labels and nutrition have caught my eye and are important when eating. How do glucose levels Research in different drinks change after adding Question an invertase enzyme? Given that the invertase enzyme breaks down sucrose, glucose levels will rise after adding the enzyme because the sucrose will convert to Hypothesis glucose and fructose. Coca Cola will have the most glucose because it has the most calories of each drink. Glucose - Chemical compound in the body - C6H12O6 - Comes from food and drink - Generally rich in sugars/carbohydrates - Used for many purposes: - Used to make energy (ATP) in cellular respiration - Stores energy - Used to build carbohydrates Chemical Reaction - A chemical reaction transfers a set of compounds into another - Reactants: Enter into a chemical reaction - Products: Compounds produced by the reaction - Catalyst: Speeds up the rate of a chemical reaction - Enzyme: Biological catalysts; usually proteins The formula for this experiment is: Invertase Sucrose + Water Glucose + Fructose Invertase C12H22O11 + H20 C6H12O6 + C6H12O6 In the Body - The most common sugar is eaten as sucrose. - Also known as table sugar - It is broken down in the body into glucose and fructose through a chemical reaction during digestion. - Fructose: Contains the same elements as glucose, but has a different chemical construction - Often used to make more glucose - The reaction is catalyzed by an enzyme named sucrase. - Modeled by invertase in experiment - The pancreas monitors blood sugar, or amount of glucose in the body. -
Ep 2 246 408 A2
(19) & (11) EP 2 246 408 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 03.11.2010 Bulletin 2010/44 C09K 8/60 (2006.01) (21) Application number: 10158819.2 (22) Date of filing: 13.11.2000 (84) Designated Contracting States: • Norman, Monica AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU Houston, TX 77041 (US) MC NL PT • Symes, Kenneth C. Designated Extension States: Bradford, RO Yorkshire BD14 6LR (GB) • Mistry, Kishor K. (30) Priority: 12.11.1999 US 165393 P Keighley, East Moton, BD20 5UU (GB) (62) Document number(s) of the earlier application(s) in • Ballard, David A. accordance with Art. 76 EPC: Stonehaven, 00980356.0 / 1 232 329 Aberdeenshire AB39 3PQ (GB) (27) Previously filed application: (74) Representative: Hull, John Philip 13.11.2000 PCT/US03/01106 Beck Greener Fulwood House (71) Applicant: M-I L.L.C. 12 Fulwood Place Houston, TX 77072 (US) London WC1V 6HR (GB) (72) Inventors: Remarks: • Freeman, Michael A. This application was filed on 31-03-2010 as a Kingwood, TX 77345 (US) divisional application to the application mentioned • Jiang, Ping under INID code 62. 3400 Sandnes (NO) (54) Method and composition f or the triggered release of polymer-degrading agents for oil field use (57) Disclosed are methods and related composi- tions for altering the physical and chemical properties of a substrate used in hydrocarbon exploitation, such as in downhole drilling operations. In a preferred embodiment a method involves formulating a fluid, tailored to the spe- cific drilling conditions, that contains one or more inacti- vated enzymes. -
Congenital Sucrase-Isomaltase Deficiency
Congenital sucrase-isomaltase deficiency Description Congenital sucrase-isomaltase deficiency is a disorder that affects a person's ability to digest certain sugars. People with this condition cannot break down the sugars sucrose and maltose. Sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains) are called disaccharides because they are made of two simple sugars. Disaccharides are broken down into simple sugars during digestion. Sucrose is broken down into glucose and another simple sugar called fructose, and maltose is broken down into two glucose molecules. People with congenital sucrase- isomaltase deficiency cannot break down the sugars sucrose and maltose, and other compounds made from these sugar molecules (carbohydrates). Congenital sucrase-isomaltase deficiency usually becomes apparent after an infant is weaned and starts to consume fruits, juices, and grains. After ingestion of sucrose or maltose, an affected child will typically experience stomach cramps, bloating, excess gas production, and diarrhea. These digestive problems can lead to failure to gain weight and grow at the expected rate (failure to thrive) and malnutrition. Most affected children are better able to tolerate sucrose and maltose as they get older. Frequency The prevalence of congenital sucrase-isomaltase deficiency is estimated to be 1 in 5, 000 people of European descent. This condition is much more prevalent in the native populations of Greenland, Alaska, and Canada, where as many as 1 in 20 people may be affected. Causes Mutations in the SI gene cause congenital sucrase-isomaltase deficiency. The SI gene provides instructions for producing the enzyme sucrase-isomaltase. -
Characterization of Substrate Binding and Catalytic Mechanisms of An
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1988 Characterization of substrate binding and catalytic mechanisms of an endoxylanase, amylosucrase, and porcine pancreatic alpha-amylase Bernard Yi Tao Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, and the Chemical Engineering Commons Recommended Citation Tao, Bernard Yi, "Characterization of substrate binding and catalytic mechanisms of an endoxylanase, amylosucrase, and porcine pancreatic alpha-amylase " (1988). Retrospective Theses and Dissertations. 8807. https://lib.dr.iastate.edu/rtd/8807 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS The most advanced technology has been used to photo graph and reproduce this manuscript from the microfilm master, UMI films the original text directly fi'om the copy submitted. Thus, some dissertation copies are in typewriter face, while others may be from a computer printer. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyrighted material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are re produced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. -
Digestion of Carbohydrates
Digestion of carbohydrates Alongside fat and protein, carbohydrates are one of the three macronutrients in our diet with their main function being to provide energy to the body. They occur in many different forms, like sugars and dietary fibre, and in many different foods, such as whole grains, fruit and vegetables. Digesting or metabolizing carbohydrates breaks foods down into sugars, which are also called saccharides. These molecules begin digesting in the mouth and continue through the body to be used for anything from normal cell functioning to cell growth and repair. It is also directly used as energy source in muscle, brain and other cells. Dietary carbohydrate principally consists of …. Polysaccharides: - Starch, glycogen and cellulose Disaccharides: - Sucrose and maltose Monosaccharide:-Glucose and fructose Out of these three types of carbohydrates, monosaccharide does not need digestion. Digestion of carbohydrates During digestion, carbohydrates that consist of more than one sugar get broken down into their monosaccharides by digestive enzymes, and then get directly absorbed causing a glycaemic response. Some of the carbohydrates cannot be broken down and they get either fermented by our gut bacteria or they transit through the gut without being changed. Digestive enzymes and their source Mouth: - Salivary amylase (α-amylase, Ptyalin) Stomach: - No enzymes Pancreas: - Pancreatic α-amylase Intestine: - Dextrinase, Maltase, Isomaltase, Sucrase, Lactase Digestion in mouth Digestion of carbohydrates starts at the mouth. In mouth, -
Disaccharidase Deficiency and Malabsorption of Carbohydrates
SINGAPORE MEDICAL JOURNAL DISACCHARIDASE DEFICIENCY AND MALABSORPTION OF CARBOHYDRATES C K Lee SYNOPSIS A large proportion of man's caloric intake is carbohydrate and starch and sucrose account for over three-quarters of the total consumed. But the rapid change of the food industry from an art to a high specialised industry in recent years have made available a variety of rare food sugars, amongst which are various disacharides. Since the digestion or enzymic breakdown of carbohydrates is a normal initial requirement that precedes their absorption, and metabolism of carbohydrates varies according to their molecular structure, these rare sugars can cause diseases of carbohydrate intolerance and malabsorption. Intolerance and malabsorption can be due to polysaccharide intolerance because of amylase dy- sfunction (caused by the absence of pancreatic amylases) or malfunctioning of absorptive process (caused by damaged or atrophied absorptive mucosa as a result of another primary disease or a variety of other casautive agents or factors, thus resulting in the Department of Chemistry inability of carbohydrate absorption by the alimentary system). A National University of Singapore third type of intolerance is due to primary deficiency or impaired Kent Ridge activity of digestive disaccharidases of the small intestine. The Singapore 0511 physiological significance and the metabolic consequences of such a lactase, sucrase-isomaltase, mal- C K Lee, Ph.D., F.I.F.S.T., C.Chem. F.R.S.C. deficiency or impaired activity of Senior Lecturer tase and trehalase are discussed. 6 VOLUME 25 NO.1 FEBRUARY 19M INTRODUCTION abundance in the free state. It is a constituent of the important plant and animal reserve sugars, starch and Recent years have seen a considerable advance in all glycogen. -
Chrebp-Knockout Mice Show Sucrose Intolerance and Fructose Malabsorption
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 1 February 2018 doi:10.20944/preprints201802.0005.v1 1 Article 2 ChREBP-Knockout Mice Show Sucrose Intolerance 3 and Fructose Malabsorption 4 Takehiro Kato1, Katsumi Iizuka1,2,*, Ken Takao1, Yukio Horikawa1, Tadahiro Kitamura3, Jun Takeda1 5 1Department of Diabetes and Endocrinology, Graduate School of Medicine, Gifu University, Gifu 501-1194, 6 Japan; [email protected] (T.K.); [email protected] (K.I.); [email protected] (K.T.); 7 [email protected] (Y.H.); [email protected] (JT). 8 2Gifu University Hospital Center for Nutritional Support and Infection Control, Gifu 501-1194, Japan 9 3Metabolic Signal Research Center, Institute for Molecular and Cellular Regulation, Gunma University, 10 Gunma 371-8512, Japan; [email protected] (T.K.) 11 *Correspondence: [email protected]; Tel: +81-58-230-6564; Fax: +81-58-230-6376 12 13 Abstract: We have previously reported that 60% sucrose diet-fed ChREBP knockout mice (KO) 14 showed body weight loss resulting in lethality. We aimed to elucidate whether sucrose and 15 fructose metabolism are impaired in KO. Wild type mice (WT) and KO were fed a diet containing 16 30% sucrose with/without 0.08% miglitol, an α-glucosidase inhibitor, and these effects on 17 phenotypes were tested. Furthermore, we compared metabolic changes of oral and peritoneal 18 fructose injection. Thirty percent sucrose diet feeding did not affect phenotypes in KO. However, 19 miglitol induced lethality in 30% sucrose-fed KO. Thirty percent sucrose plus miglitol diet-fed KO 20 showed increased cecal contents, increased fecal lactate contents, increased growth of 21 lactobacillales and Bifidobacterium and decreased growth of clostridium cluster XIVa. -
Production of Carbohydrases for Developing Soy Meal As
PRODUCTION OF CARBOHYDRASES FOR DEVELOPING SOY MEAL AS PROTEIN SOURCE FOR ANIMAL FEED A Dissertation Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy Qian Li May, 2017 PRODUCTION OF CARBOHYDRASES FOR DEVELOPING SOY MEAL AS PROTEIN SOURCE FOR ANIMAL FEED Qian Li Dissertation Approved: Accepted: Advisor Department Chair Dr. Lu-Kwang Ju Dr. Michael H. Cheung Committee Member Dean of the College Dr. Jie Zheng Dr. Donald P. Visco Jr. Committee Member Dean of the Graduate School Dr. Lingyun Liu Dr. Chand Midha Committee Member Date Dr. Ge Zhang Committee Member Dr. Pei-Yang Liu ii ABSTRACT Global demand for seafood is growing rapidly and more than 40% of the demand is met by aquaculture. Conventional aquaculture diet used fishmeal as the protein source. The limited production of fishmeal cannot meet the increase of aquaculture production. Therefore, it is desirable to partially or totally replace fishmeal with less-expensive protein sources, such as poultry by-product meal, feather meal blood meal, or meat and bone meal. However, these feeds are deficient in one or more of the essential amino acids, especially lysine, isoleucine and methionine. And, animal protein sources are increasingly less acceptable due to health concerns. One option is to utilize a sustainable, economic and safe plant protein sources, such as soybean. The soybean industry has been very prominent in many countries in the last 20 years. The worldwide soybean production has increased 106% since 1996 to 2010[1]. Soybean protein is becoming the best choice of sustainable, economic and safe protein sources.