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Congenital Sucrase-Isomaltase Deficiency

Asta Literature Retrieval: Pathophysiology and clinical mechanisms of Congenital Sucrase-Isomaltase Deficiency. Core disease mechanisms, molecul...

2026-04-14
Asta MONDO:0009114 Model: Asta Scientific Corpus Retrieval 15 citations

Asta Literature Retrieval: Pathophysiology and clinical mechanisms of Congenital Sucrase-Isomaltase Deficiency. Core disease mechanisms, molecul...

This report is retrieval-only and is generated directly from Asta results.

  • Papers retrieved: 15
  • Snippets retrieved: 20

Relevant Papers

[1] The genetics of monogenic intestinal epithelial disorders

  • Authors: Stephen J. Babcock, David Flores-Marin, Jay R. Thiagarajah
  • Year: 2022
  • Venue: Human Genetics
  • URL: https://www.semanticscholar.org/paper/9b0676b2e9805c377256b2b9e7f52547baf99670
  • DOI: 10.1007/s00439-022-02501-5
  • PMID: 36422736
  • PMCID: 10182130
  • Citations: 35
  • Influential citations: 3
  • Summary: The genetics, clinical presentation, and known pathophysiology for specific disorders, including a historical perspective of the field and relationship to other monogenic disorders of the intestine, are described.
  • Evidence snippets:
  • Snippet 1 (score: 0.669) > The sucrase-isomaltase (SI) gene, mapped to chromosome 3q26.1, codes for sucrase-isomaltase, a heterodimeric protein with two subunits, sucrase and isomaltase. Sucraseisomaltase is a type II transmembrane disaccharidase glycoprotein expressed in the intestinal brush border (Naim et al. 1988). Initially, the protein encoded by the SI gene is a precursor protein that is later cleaved by pancreatic proteases into sucrase and isomaltase. While sucrase hydrolyzes sucrose, isomaltase processes starch, isomaltose, and maltose. Therefore, patients with biallelic mutations of the SI gene are unable to metabolize these carbohydrates, and their consumption leads to a diet-induced diarrhea accompanied by different degrees of abdominal bloating and pain. This condition, congenital sucrase-isomaltase deficiency (CSID), was initially identified and described in the 1960s (Weijers et al. 1960). > There is still no clear consensus on the worldwide prevalence of congenital sucrase-isomaltase deficiency, due to the nonspecific nature of symptoms and variation in disease severity. Estimates place the mutation at around 0.2% in individuals of European descent, 5-10% in Greenland Innuits, and 3-7% in Canadian and Alaskan Innuits (Treem 2012). Four mutations are estimated to represent over 80% of CSID in European populations: p.Gly1073Asp, p.Val577Gly, p.Phe1745Cys, and p.Arg1124* (Gericke et al. 2017). A molecular and cellular analysis of 13 missense mutations has allowed for their classification into three major phenotypes based on whether protein trafficking, enzymatic activity, or lipid raft association is affected (Gericke et al. 2017). In general terms, however, these mutations result in some degree of improper targeting to the plasma membrane and a combined deficiency of both sucrase and isomaltase (Naim et al. 1988).
  • Snippet 2 (score: 0.405) > Although they are commonly linked and defined by altered intestinal epithelial function, CoDE disorders exhibit a wide variety of cell and tissue level pathophysiological mechanisms. Despite this heterogeneity some broad categories have emerged to classify specific genes. As the specific causative genes for many cases of non-acquired severe infantile-onset chronic diarrhea can now be established, it has become important to shift away from syndromic or clinically defined naming of disorders to more specific designation by affected gene (e.g., SPINT2 deficiency vs syndromic congenital sodium diarrhea). This is particularly relevant for current and future studies that aim to correlate specific mutations with phenotype, prognosis, and treatment. As with any attempt to classify such a heterogenous group of disorders there are specific genes/disorders that do not fit well in any one category. In some cases, such as the recently discovered WNT2B deficiency, this has allowed expansion or development of new categories. As new causative genes (e.g., PERCC1, UNC45A, AGR2) and new information on disease mechanisms continue to emerge, these categories will need ongoing revision and refinement. Disease can also be classified by other methods such as protein ontology (e.g., functional annotation) or clinical outcome (e.g., parenteral nutrition dependence). > Broadly, monogenic epithelial disorders can be classified into five major categories that comprise core modules of epithelial function. These are listed below (see also Fig. 1) and detailed descriptions of several disorders in each category follow: > • Epithelial transport

[2] Molecular Basis of Aberrant Apical Protein Transport in an Intestinal Enzyme Disorder*

  • Authors: N. Spodsberg, R. Jacob, Marwan Alfalah, K. Zimmer, H. Naim
  • Year: 2001
  • Venue: The Journal of Biological Chemistry
  • URL: https://www.semanticscholar.org/paper/839b8194012c3cf0aceebe90e4ee7cb53ae9b7da
  • DOI: 10.1074/jbc.C100219200
  • PMID: 11340066
  • Citations: 43
  • Influential citations: 1
  • Summary: The impaired sorting profile to the apical membrane of human intestinal sucrase-isomaltase is the underlying cause in the pathogenesis of a novel phenotype of intestinal congenital sucrase-isomaltase deficiency. Molecular characterization of this novel phenotype reveals a point mutation in the coding region of the sucrase-isomaltase (SI) gene that results in an amino acid substitution of a glutamine by arginine at residue 117 of the isomaltase subunit. This substitution is located in a domain...
  • Evidence snippets:
  • Snippet 1 (score: 0.585) > Investigating the molecular basis of naturally occurring mutant protein phenotypes in diseases constitutes therefore a powerful means to unravel the molecular mechanisms underlying intracellular protein transport and sorting. A small intestinal disorder directly associated with a folding mutant and defective intracellular protein transport is congenital sucrase-isomaltase defi-ciency (CSID). 1 CSID is an autosomal recessive disease that is characterized by an absent sucrase activity within the sucraseisomaltase (SI) enzyme complex, while the isomaltase activity can vary from absent to normal. The disease is clinically manifested as an osmotic-fermentative diarrhea upon ingestion of di-and oligosaccharides (4). Several phenotypes of the disease have been characterized on the basis of cellular mislocalization or aberrant function of the SI mutant protein. SI is a type II membrane-bound glycoprotein of the intestinal brush border comprising two strongly homologous subunits, sucrase and isomaltase (5)(6)(7)(8). These two domains originate from a large polypeptide precursor, pro-SI, by tryptic cleavage occurring in the intestinal lumen and ultimately maintain a strong association through noncovalent ionic interactions (9,10). This enzyme complex is a heavily N-and O-glycosylated protein (10). > Particularly O-glycosylation is critical for targeting of SI to the apical membrane through direct association in detergent-insoluble lipid rafts (11). > In this paper we describe a novel phenotype of CSID and the corresponding mutation, which results in a random distribution of the SI protein at the apical and basolateral membrane. Here a point mutation, an adenine to glutamine at nucleotide 412 in the coding region of the isomaltase subunit, results in a substitution of glutamine to arginine at amino acid residue 117. Defects in polarized protein sorting implicated in the pathogenesis of diseases have been rarely observed, perhaps because such defects have lethal consequences during early stages of development.
  • Snippet 2 (score: 0.447) > The impaired sorting profile to the apical membrane of human intestinal sucrase-isomaltase is the underlying cause in the pathogenesis of a novel phenotype of intestinal congenital sucrase-isomaltase deficiency. Molecular characterization of this novel phenotype reveals a point mutation in the coding region of the sucraseisomaltase (SI) gene that results in an amino acid substitution of a glutamine by arginine at residue 117 of the isomaltase subunit. This substitution is located in a domain revealing features of a trefoil motif or a P-domain in immediate vicinity of the heavily O-glycosylated stalk domain. Expression of the mutant SI phenotype in epithelial Madin-Darby canine kidney cells reveals a randomly targeted SI protein to the apical and basolateral membranes confirming an exclusive role of the Q117R mutation in generating this phenotype. Unlike wild type SI, the mutant protein is completely extractable with Triton X-100 despite the presence of O-glycans that serve in the wild type protein as an apical sorting signal and are required for the association of SI with detergent-insoluble lipid microdomains. Obviously the O-glycans are not adequately recognized in the context of the mutant SI, most likely due to altered folding of the Pdomain that ultimately affects the access of the O-glycans to a putative sorting element. > The composition and function of the plasma membrane of polarized cells are maintained by a complex intracellular traffic moving cell surface glycoproteins between organelles. This requires the recognition and sorting of different classes of proteins not only during biosynthesis, but also during distributive events to the diverse cellular compartments (1). Oftentimes altered and defective intracellular trafficking of proteins due to single point or deletion mutations in the coding region of the gene result in pathological disorders (2,3). Investigating the molecular basis of naturally occurring mutant protein phenotypes in diseases constitutes therefore a powerful means to unravel the molecular mechanisms underlying intracellular protein transport and sorting.

[3] Altered Folding, Turnover, and Polarized Sorting Act in Concert to Define a Novel Pathomechanism of Congenital Sucrase-Isomaltase Deficiency*

  • Authors: M. Keiser, Marwan Alfalah, M. Pröpsting, D. Castelletti, H. Naim
  • Year: 2006
  • Venue: Journal of Biological Chemistry
  • URL: https://www.semanticscholar.org/paper/d9d6b2e9f7396a8f3b728c64ff1a1af829c29441
  • DOI: 10.1074/jbc.M513631200
  • PMID: 16543230
  • Citations: 26
  • Influential citations: 1
  • Summary: The combined effects of the C635R mutation on the turnover rate, function, polarized sorting, and detergent solubility of SI constitute a unique and novel pathomechanism of CSID.
  • Evidence snippets:
  • Snippet 1 (score: 0.543) > The utilization of misfolding-related diseases has proven to be invaluable in dissection of the molecular mechanisms of protein transport and has unraveled several intriguing cell biological phenomena, such as in cases of congenital sucrase-isomaltase deficiency (CSID). 3 This intestinal autosomal recessive disorder is characterized by the absence of the sucrase and most of the maltase digestive activity within the sucraseisomaltase (SI) enzyme complex. The isomaltase activity varies from absent to normal (1). Clinically, the disease is manifested as an osmotic-fermentative diarrhea upon ingestion of disaccharides and oligosaccharides (2). Analysis of this disorder at the molecular and subcellular levels has unraveled a number of phenotypes of CSID, which are characterized by perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI (3)(4)(5). A few examples have been also reported, in which the misfolded protein products may escape the quality control system, instead of being either degraded or retained in the ER. A mutation at the position 620 of SI (L620P), for example, has been identified as one of the possible genetic modifications occurring in the CSID (6). Although this mutant is mainly found to be localized in the ER, it can be at least partially expressed also on the cell surface. Moreover, Propsting et al. (7) reported on the Q1098P mutation of SI causing an incomplete folding of the protein, which is however insufficient to trigger the complete protein block into the ER. In fact, the protein can exit the ER and reach the cis-Golgi compartment eluding partially the quality control in the ER. > SI is a type II transmembrane glycoprotein of two highly homologous subunits, sucrase and isomaltase (5,8), that is expressed at the intestine brush-border membrane, where it serves as a catalyst for the cleavage of sugar and starch (9,10).
  • Snippet 2 (score: 0.462) > Altered Folding, Turnover, and Polarized Sorting Act in Concert to Define a Novel Pathomechanism of Congenital Sucrase-Isomaltase Deficiency*

[4] Congenital sucrase–isomaltase deficiency: A case report

  • Authors: Rita Santos-Silva, M. Tavares, E. Trindade, J. Amil-Dias
  • Year: 2014
  • Venue: GE Portuguese Journal of Gastroenterology
  • URL: https://www.semanticscholar.org/paper/8d3a3b0515f905d79731cc2fece2183699464bbf
  • DOI: 10.1016/J.JPGE.2014.07.004
  • Citations: 2
  • Summary: The case of a six-month-old male infant admitted for chronic profuse diarrhea and failure to thrive that began after food diversification showed that he had CSID and the therapeutic option was the addition of baker's yeast to the diet which was followed by complete resolution of symptoms and excellent weight recovery.
  • Evidence snippets:
  • Snippet 1 (score: 0.520) > Congenital sucrase–isomaltase deficiency: A case report
  • Snippet 2 (score: 0.431) > Congenital sucrase---isomaltase deficiency (OMIM #222900) is caused by homozygous or compound heterozygous mutation in the SI gene, which encodes sucrase---isomaltase on chromosome 3q26. > Sucrase---isomaltase is an enterocyte-specific small intestine brush-border membrane disaccharidase. It is required for hydrolysis of sucrose and some starches. Upon ingestion of disaccharides and oligosaccharides, the failure to breakdown sucrose into fructose and glucose results in osmotic-fermentative diarrhea. > CSID is the most common congenital disorder of carbohydrate metabolism. Its estimated prevalence in North America and Europe ranges from 0.05% to 0.2%, 1 although this diagnosis is believed to be frequently missed. > Onset usually occurs during infancy after weaning from breast milk or lactose-only formula onto foods containing sucrose or starch. Clinical manifestations include osmotic-fermentative diarrhea, abdominal distension and discomfort, flatulence, vomiting and diaper rash. 2 Severe symptoms may lead to failure to thrive, dehydration and malnutrition. Adolescents and adults may present with signs of 'irritable bowel syndrome'. Carbohydrates result in a dose-dependent acceleration of colonic transit 3 and therefore symptoms may only occur with the ingestion of large amounts of sucrose. 2 CSID is a heterogeneous disorder. Identified mutations lead to a range of posttranslational defects resulting in an absence of sucrase activity and varying degrees of isomaltase deficiency. Heterozygotes have intermediate enzyme values and are usually asymptomatic in adulthood, but may have mild symptoms in infancy. > Several tests can be used to diagnose CSID, with measurement of intestinal disaccharides' activities being the gold standard. 2 It will show complete or almost complete lack of sucrase/isomaltase activity with normal lactase activity and normal villous architecture. > The hydrogen breath test is a non-invasive method for detecting carbohydrate malabsor

[5] The patient journey to diagnosis and treatment of congenital sucrase-isomaltase deficiency

  • Authors: Heather Smith, B. Romero, E. Flood, A. Boney
  • Year: 2021
  • Venue: Quality of Life Research
  • URL: https://www.semanticscholar.org/paper/f228fbd0c2786b440fbc2a8fa4d1f9daa487be69
  • DOI: 10.1007/s11136-021-02819-z
  • PMID: 33772704
  • PMCID: 8298246
  • Citations: 13
  • Influential citations: 1
  • Summary: Patients with CSID reported considerable improvement in symptoms and health-related quality of life (HRQL), yet symptoms persist that continue to affect daily life, indicating areas of potential unmet need.
  • Evidence snippets:
  • Snippet 1 (score: 0.485) > The patient journey to diagnosis and treatment of congenital sucrase-isomaltase deficiency

[6] Congenital Sucrase–Isomaltase Deficiency: Same Mutation with Different Clinical Presentations

  • Authors: Fatma İssi Irlayıcı, Burcu Güven, Murat Çakır
  • Year: 2024
  • Venue: The Turkish Journal of Gastroenterology
  • URL: https://www.semanticscholar.org/paper/8409fe40c8e26f051972ac3162dec0d2b6a75c36
  • DOI: 10.5152/tjg.2024.23250
  • PMID: 39128102
  • PMCID: 11114242
  • Citations: 1
  • Summary: Despite its autosomal recessive inheritance, congenital sucrase–isomaltase deficiency can also be symptomatic in heterozygous individuals, and further studies are required to clarify the genotype–phenotype relationship and management of the disease.
  • Evidence snippets:
  • Snippet 1 (score: 0.466) > Congenital Sucrase–Isomaltase Deficiency: Same Mutation with Different Clinical Presentations

[7] Congenital Diarrheal Disorders: An Updated Diagnostic Approach

  • Authors: G. Terrin, R. Tomaiuolo, A. Passariello, A. Elce, F. Amato et al.
  • Year: 2012
  • Venue: International Journal of Molecular Sciences
  • URL: https://www.semanticscholar.org/paper/7cae68c68d2fabcd2ee0726efbbebe14095527ed
  • DOI: 10.3390/ijms13044168
  • PMID: 22605972
  • PMCID: 3344208
  • Citations: 69
  • Influential citations: 3
  • Summary: This work reviews CDDs on the basis of the genetic defect, focusing on the significant contribution of molecular analysis in the complex, multistep diagnostic work-up.
  • Evidence snippets:
  • Snippet 1 (score: 0.460) > This group can be further divided in various subgroups on the basis of the specific gene defect. The first subgroup includes the deficiency of brush border enzymes, and in particular congenital LD due to mutations within the gene encoding the protein with either lactase and phlorizin hydrolase activities [26]; congenital SID, due to mutations in the gene encoding the protein with both sucrase and isomaltase activity [8], and congenital maltase-glucoamylase deficiency (MGD), putatively due to the maltase-glucoamylase (MGAM) gene defect [8], even if some patients with the disease do not bear pathogenetic mutations in such gene. In fact, cases in which MGD was associated to the deficiency of other brush border enzymes were described, and it has been postulated that a pleiotropic regulator factor of such genes may be impaired in these patients [27]. > A large subgroup derives from mutations of genes encoding members of the super-family of solute carriers (SLC). These genes are structurally related and originated by mechanisms of duplication, but despite the homology of the gene sequence and the similarity of the protein architecture, the clinical picture and the outcome of these CDDs is heterogeneous. Most proteins encoded by SLC genes are expressed at intestinal level, thus the disease typically appears with diarrhea and selective malabsorption. In other cases the carrier is expressed also in other organs (i.e., the aminoacid transporter involved in LPI is expressed also in other tissues) and thus the disease could involves other organs or be systemic [7]. For some CDDs disease-genes are still unknown or more genes may be involved. For example, the disease gene for fructose malabsorption is still undefined [8,17,28]. There remains insufficient evidence that glucose transporter (GLUT) 5 represents the main fructose facilitative carrier in the intestine [17,28]. Recent studies have identified GLUT7 as a high affinity glucose and fructose carrier on the brush border membrane of the enterocyte located in the distal intestine.

[8] Diagnosing and Treating Intolerance to Carbohydrates in Children

  • Authors: R. Berni Canani, V. Pezzella, Antonio Amoroso, T. Cozzolino, C. di Scala et al.
  • Year: 2016
  • Venue: Nutrients
  • URL: https://www.semanticscholar.org/paper/a5fdd2fdf0f680a72d998224c244d8854d4ffa4f
  • DOI: 10.3390/nu8030157
  • PMID: 26978392
  • PMCID: 4808885
  • Citations: 65
  • Influential citations: 1
  • Summary: The most up-to-date research on intolerance to carbohydrates is examined, controversies relating to the diagnostic approach are discussed, including the role of molecular analysis, and new insights into modern management in the pediatric age are provided.
  • Evidence snippets:
  • Snippet 1 (score: 0.448) > Congenital sucrose-isomaltase deficiency (CSID, OMIM #222900) is a rare autosomal recessive inherited disease of the small intestine resulting from genetic mutations in sucrase-isomaltase, an enzyme complex responsible for catalyzing the hydrolysis of dietary sucrose and starch [17]. Decreased or absent sucrase and/or isomaltase enzymatic activity has been found in patients with CSID, and investigations at the subcellular and molecular levels in intestinal biopsy specimens have led to the description of several phenotypes, differing in transport efficiency, processing, and sorting of the protein, which result in impaired physiologic functions [17][18][19][20]. In addition to the degree of enzyme deficiency, the appearance of overt clinical manifestations of CSID is partially determined by the amount of sugar and starch consumed [21]. The prevalence in the European population has been estimated at 1 in 5000, but it is higher among the indigenous populations of Alaska, Greenland, and Canada [22]. Gastrointestinal symptoms usually begin after an infant is weaned off breast milk and is first exposed to sucrose and starch [23]. Failure to absorb dietary disaccharides and starch has implications for the absorption of other nutrients and the hormonal regulation of gastrointestinal function. For these reasons, patients with CSID are at risk for chronic malnutrition and failure to thrive. In many cases, the symptoms of CSID are more severe in infants than in adults. It has been suggested that an increased susceptibility to symptoms in infants is related to a shorter length of the small intestine. Although intestinal biopsy is still adopted in many
  • Snippet 2 (score: 0.415) > Congenital sucrose-isomaltase deficiency (CSID, OMIM #222900) is a rare autosomal recessive inherited disease of the small intestine resulting from genetic mutations in sucrase-isomaltase, an enzyme complex responsible for catalyzing the hydrolysis of dietary sucrose and starch [17]. Decreased or absent sucrase and/or isomaltase enzymatic activity has been found in patients with CSID, and investigations at the subcellular and molecular levels in intestinal biopsy specimens have led to the description of several phenotypes, differing in transport efficiency, processing, and sorting of the protein, which result in impaired physiologic functions [17][18][19][20]. In addition to the degree of enzyme deficiency, the appearance of overt clinical manifestations of CSID is partially determined by the amount of sugar and starch consumed [21]. The prevalence in the European population has been estimated at 1 in 5000, but it is higher among the indigenous populations of Alaska, Greenland, and Canada [22]. Gastrointestinal symptoms usually begin after an infant is weaned off breast milk and is first exposed to sucrose and starch [23]. Failure to absorb dietary disaccharides and starch has implications for the absorption of other nutrients and the hormonal regulation of gastrointestinal function. For these reasons, patients with CSID are at risk for chronic malnutrition and failure to thrive. In many cases, the symptoms of CSID are more severe in infants than in adults. It has been suggested that an increased susceptibility to symptoms in infants is related to a shorter length of the small intestine. Although intestinal biopsy is still adopted in many tertiary centers for CSID diagnosis, genetic testing is now widely available. Molecular genetics has become helpful for obtaining an early and unequivocal diagnosis in infants with chronic diarrhea due to any of a variety of different disorders, thus permitting rapid and targeted therapeutic strategies and reducing repetitive, invasive, and expensive procedures. At least 80% of CSID patients have one of four common mutations [22,24].

[9] Our Cases with Sucrase Isomaltase Deficiency

  • Authors: Miray Karakoyun, Erhan Kilicoglu, Y. Şahan, M. Baran, F. Ünal et al.
  • Year: 2015
  • Venue: Journal of Gastrointestinal and Digestive System
  • URL: https://www.semanticscholar.org/paper/aced4166c3fe683d3c5f6f19bfaa0451ca588d2f
  • DOI: 10.4172/2161-069X.1000354
  • Citations: 7
  • Summary: It is suggested that sucrase isomaltase deficiency should be considered in pediatric patients presenting with chronic watery diarrhea, due to the actual prevalence of the disease in Turkey is unknown.
  • Evidence snippets:
  • Snippet 1 (score: 0.444) > Our Cases with Sucrase Isomaltase Deficiency

[10] Naturally occurring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunit [published erratum appears in J Cell Biol 1991 Dec;115(5):following 1473]

  • Authors: Jack A.M. Fransen, H.-P. Hauri, L. Ginsel, H. Naim
  • Year: 1991
  • Venue: The Journal of Cell Biology
  • URL: https://www.semanticscholar.org/paper/9bc9d26e3d7b6897f94fa25fa487cca783f30855
  • DOI: 10.1083/JCB.115.1.45
  • PMID: 1717481
  • PMCID: 2289914
  • Citations: 60
  • Summary: It is concluded that structural features in the isomaltase region of pro-SI are required for transport and sorting of the sucrase-isomalase complex.
  • Evidence snippets:
  • Snippet 1 (score: 0.432) > Recent studies in an intestinal epithelial cell line, Caco-2, have suggested that proteins destined for the microvillar membrane are selectively sorted before their transport to that membrane (Hauri, 1988;Matter et al., 1990) ; basolateral proteins are on the other hand nonselectively sorted and reach their final destination by a default pathway (Rindler and Traber, 1988) . Although the molecular mechanisms underlying these events have not been unraveled yet, an attractive hypothesis is that selective sorting is accomplished by cellular recognition elements that recognize sorting signals or specific structural motifs in the mature protein and interact with them in a ligand/receptor fashion . Proteins that are not identified by these recognition elements are then translocated to the basolateral membrane . The nature and/or structure of putative sorting signals are unknown . > In accordance with this hypothesis, it is conceivable that slight alterations in the sorting signal of an otherwise sorted protein will disrupt its interaction with signal recognition elements leading to a protein that operates by default. Naturally occurring mutant phenotypes of proteins that are missorted have been rarely observed . > We have presented in this paper two novel phenotypes (phenotype IV and phenotype V) of sucrase-isomaltase in congenital sucrase-isomaltase deficiency (CSID) . One of these, phenotype IV, is the first identification of a protein that is missorted to the basolateral membrane in a naturally occurring mutant phenotype. > Figure 11. (a) Biosynthesis and maturation of aminopeptidase N (ApN) in intestinal mucosa of patient II . Biopsies were cultured for the indicated time periods in the presence of [35S]methionine. Immunoprecipitation was carried out with a single mAb against ApN from homogenates (H) or the culture medium (M) . One of two identical immunoprecipitates was treated with endo H to probe for high-mannose and complex-glycosylated forms.

[11] Congenital sucrase-isomaltase deficiency

[12] Sucrase-Isomaltase Deficiency Causing Persistent Bloating and Diarrhea in an Adult Female

  • Authors: Varsha Chiruvella, A. Cheema, H. Arshad, Jacqueline Chan, J. Yap
  • Year: 2021
  • Venue: Cureus
  • URL: https://www.semanticscholar.org/paper/5cd814695789b24a10c6beb6bc6b1725e61fc682
  • DOI: 10.7759/cureus.14349
  • PMID: 33972906
  • PMCID: 8105231
  • Citations: 7
  • Summary: A 50-year-old woman with persistent symptoms of bloating in spite of extensive evaluation and treatment is presented with CSID, an autosomal recessive disorder which leads to chronic intestinal malabsorption of nutrients from ingested starch and sucrose.
  • Evidence snippets:
  • Snippet 1 (score: 0.431) > 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. When this enzyme complex is deficient, nutrients from ingested starch and sucrose cannot be absorbed sufficiently. Infants and young children generally develop symptoms such as explosive watery diarrhea, abdominal distension, colic, and dehydration after consumption of fruits, juices, grains, modified milk formulas, and starches. These dietary symptoms reduce an individual's absorption of essential dietary nutrients and cause malnutrition. In infants and children, this commonly manifests as failure to gain appropriate weight and height and presents as low body weight in adults. However, starch intolerance often disappears during childhood, and symptoms of sucrose intolerance usually improve as the affected child ages [1]. A confirmatory CSID diagnosis can be made by a disaccharidase assay using a small bowel tissue biopsy or sucrose breath testing. Treatment for the condition consists of a combination approach of diet modification limiting sucrose and sucrase enzyme replacement therapy with sacrosidase, obtained from baker's yeast and glycerin, which is the only Food and Drug Administration (FDA) approved treatment for this condition [2]. However, due to CSID's nonspecific symptoms diagnosis is usually delayed. Prevalence of CSID may also be underrecognized due to overlapping presentation with other gastrointestinal (GI) conditions such as irritable bowel syndrome (IBS) and celiac disease, so the condition may be of greater clinical significance than previously suspected [3].

[13] Congenital sucrase-isomaltase deficiency: an under-diagnosed disease in Chinese children

  • Authors: L. Geng, Ding-You Li, Wen-ji Ou, Qunying Yang, Tiefu Fang et al.
  • Year: 2014
  • Venue: BMC Pediatrics
  • URL: https://www.semanticscholar.org/paper/cf422f5ac242252a3153f89b7d7d8fe587283ad4
  • DOI: 10.1186/1471-2431-14-11
  • PMID: 24433566
  • PMCID: 3927221
  • Citations: 10
  • Influential citations: 1
  • Summary: This is the first case series of CSID in Chinese children and the diagnosis can be made based on clinical suspicion and sucrose tolerance test and no children developed watery stools up to 4 hours after feeding glucose test solution.
  • Evidence snippets:
  • Snippet 1 (score: 0.419) > Congenital sucrase-isomaltase deficiency: an under-diagnosed disease in Chinese children

[14] Histopathology of intestinal villi in neonatal and paediatric age: main features with clinical correlation - Part I

  • Authors: Chiara Rossi, Gloria Simoncelli, Giovanni Arpa, A. Stracuzzi, P. Parente et al.
  • Year: 2021
  • Venue: Pathologica
  • URL: https://www.semanticscholar.org/paper/05ec008cc8fb5e3aa285fa656fe0bd632eb90ea6
  • DOI: 10.32074/1591-951X-337
  • PMID: 34856604
  • PMCID: 9040547
  • Citations: 4
  • Summary: This review aims to provide a comprehensive histopathological summary of paediatric small bowel alteration and their differential diagnoses with a reference to the main clinical aspects required for appropriate interpretation.
  • Evidence snippets:
  • Snippet 1 (score: 0.410) > Several congenital disorders of substrate digestion, absorption and transport have been described. The main subgroups included in this family are: i) disaccharidase deficiencies, ii) lipid trafficking disorders, and iii) ion and nutrient transport deficiencies. Apart from fat processing disorders, which may show rela-tively specific histopathologic features, small bowel histology of these enteropathies is generally normal or near normal and genetic analysis is required for their definitive diagnosis. Congenital disaccharidase deficiencies are rare, genetically determined entities, that comprise: i) congenital lactase deficiency, ii) sucrase-isomaltase deficiency, iii) maltase-glucoamylase deficiency, and iv) trehalase deficiency. Lactase-phlorizin hydrolase, sucrase-isomaltase, maltase-glucoamylase and trehalase are enzymes responsible for degradation of milk lactose, sucrose, starch, and mushroom trehalose, respectively. These enzymes are expressed on the brush border of villous absorptive cells in a time-dependent pattern (e.g. lactase is mainly expressed in neonates). Disaccharidase deficiencies cause a severe, osmotic-type diarrhoea in children. Importantly, small bowel mucosa looks histologically normal. Congenital disaccharidase disorders should be distinguished from secondary disaccharidase defects due to mucosal damage occurring in various enteropathies of different aetiology (e.g. coeliac or Crohn's disease) and from other disorder leading to carbohydrate malabsorption such as congenital fructose malabsorption, due to mutation in GLUT5 gene, which encodes for a hexose transporter at enterocyte basolateral membrane. Congenital lipid trafficking disorders are characterized by primary defects in lipid transport within absorptive cells, resulting in fat malabsorption, steatorrhoea, failure to thrive and various neurologic symptoms in neonates. They include i) abetalipoproteinaemia, ii) hypolipoproteinaemia, and iii) Anderson disease. They

[15] Genetic and acquired sucrase-isomaltase deficiency: A clinical review.

  • Authors: T. Danialifar, B. Chumpitazi, Devendra I Mehta, C. Di Lorenzo
  • Year: 2024
  • Venue: Journal of pediatric gastroenterology and nutrition
  • URL: https://www.semanticscholar.org/paper/7180bb4ab8b870683b89c2aebf30234b9a600ba8
  • DOI: 10.1002/jpn3.12151
  • PMID: 38327254
  • Citations: 26
  • Influential citations: 3
  • Summary: Management of GSID is based on sucrose and potentially starch restriction tailored to the individual patients' tolerance and symptoms, and additional treatment with commercially available sacrosidase is available, however, some patients may require continued starch restriction.
  • Evidence snippets:
  • Snippet 1 (score: 0.406) > Genetic and acquired sucrase-isomaltase deficiency: A clinical review.

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