Maltase-Glucoamylase and Residual Isomaltase in Sucrose Intolerant Patients

Skovbjerg, Hanne; Krasilnikoff, P. A.

doi:10.1097/00005176-198605000-00005

Cited by 24 publications

(12 citation statements)

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“…The disaccharidase activities in the duodenum are reduced by almost 40% as compared with the proximal jejunum (25,26). In some SI-deficient patients, the activity of maltase-glucoamylase is reduced, as is the isomaltase activity (27). The activities of other brush border disaccharidases such as lactase-phlorizin hydrolase and maltase-glucoamylase and peptidases such as aminopeptidase N, dipeptidyl peptidase IV, and meprin are usually within the normal range.…”

Section: Pathophysiology Clinical Features and Diagnosis Of Csidmentioning

confidence: 99%

Congenital Sucrase‐Isomaltase Deficiency

Naim

Heisenberg

Zimmer

2012

J. pediatr. gastroenterol. nutr.

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Section: Pathophysiology Clinical Features and Diagnosis Of Csidmentioning

confidence: 99%

Congenital Sucrase‐Isomaltase Deficiency

Naim

Heisenberg

Zimmer

2012

J. pediatr. gastroenterol. nutr.

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“…Duodenal mucosal histology is always normal. CSID patients have different phenotypes of enzymatic activities associated with SI, ranging from reductions of sucrase activity to total absence, as well as variable absence, of isomaltase activity (7)(8)(9)(10). Low sucrase activity leads to malabsorption of sucrose, resulting in dyspeptic-like symptoms such as dietrelated chronic osmotic diarrhea and abdominal pain.…”

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confidence: 99%

¹³C‐Breath Tests for Sucrose Digestion in Congenital Sucrase Isomaltase–deficient and Sacrosidase‐supplemented Patients

Robayo–Torres

Opekun

Quezada‐Calvillo

et al. 2009

J. pediatr. gastroenterol. nutr.

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Congenital sucrase-isomaltase deficiency (CSID) is characterized by absence or deficiency of the mucosal sucrase-isomaltase enzyme. Specific diagnosis requires upper gastrointestinal biopsy with evidence of low to absent sucrase enzyme activity and normal histology. The hydrogen breath test (BT) is useful but is not specific for confirmation of CSID. We investigated a more specific 13C-sucrose labeled BT. Objectives were to determine if CSID can be detected with the 13C-sucrose BT without duodenal biopsy sucrase assay and if the 13C-sucrose BT can document restoration of sucrose digestion by CSID patients after oral supplementation with sacrosidase (Sucraid®). Methods Ten CSID patients were diagnosed by low biopsy sucrase activity. Ten controls were children who underwent endoscopy and biopsy because of dyspepsia or chronic diarrhea with normal mucosal enzymes activity and histology. Uniformly-labeled 13C-glucose and 13C-sucrose loads were orally administered. 13CO2 breath enrichments were assayed using an infrared spectrophotometer. In CSID patients the 13C-sucrose load was repeated adding Sucraid®. Sucrose digestion and oxidation were calculated as a mean % coefficient of glucose oxidation (% CGO) averaged between 30 and 90 minutes. Results Classification of patients by 13C-sucrose BT % CGO agreed with biopsy sucrase activity. The breath test also documented the return to normal of sucrose digestion and oxidation after supplementation of CSID patients with Sucraid®. Conclusion 13C-sucrose BT is an accurate and specific non-invasive confirmatory test for CSID and for enzyme replacement management.

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“…Recently, single amino acid substitution was identified in sucrase subunit in a patient with CSID (34). On the other hand, human cases with isolated sucrase deficiency are also reported, however, the precise molecular basis of this abnormality has not been elucidated (35,36). The present report is the first to investigate the molecular basis of isolated sucrase deficiency in the mammalian species.…”

Section: Discussionmentioning

confidence: 74%

Molecular Cloning of Sucrase-Isomaltase cDNA in the House Musk Shrew Suncus murinusand Identification of a Mutation Responsible for Isolated Sucrase Deficiency

Ito

Hayashi

Ohmori

et al. 1998

Journal of Biological Chemistry

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Isolated sucrase deficiency has been demonstrated in a line of house musk shrew, Suncus murinus (laboratory name: suncus). This animal belongs to the order Insectivore and is phylogenetically different from ordinarily used laboratory animals. They are believed to have evolved with mainly animal food without sucrose. To study the molecular basis of the sucrase deficiency in suncus, we cloned 6.0-kilobase (kb) sucrase-isomaltase (SI, EC 3.2.1.48 -10) cDNA from suncus intestinal cDNA library. The cDNA clone contained a 5442-base pair (bp)-long open reading frame preceded by an in frame termination codon. The deduced 1813-amino acid sequence showed 68.6, 71.2, and 74.7% similarity with those of rat, rabbit, and human, respectively. A cleavage site between isomaltase and sucrase as well as the region surrounding the catalytic sites for sucrase and isomaltase were conserved among the species. Out of 18 potential N-linked glycosylation sites, 5 were common among all 4 species. In the connecting segment which was enriched with O-linked glycosylation sites in the other species, only two sites were present in suncus. Northern blot analysis revealed that the 6.0-kb SI mRNA was expressed in the KAT line with intact sucrase-isomaltase activity. In contrast, 3.0-kb SI mRNA was expressed in suncus of the MI line with isolated sucrase deficiency. The 3.0-kb mRNA cosegregated with sucrase deficiency phenotype as an autosomal recessive trait. Sequence analysis revealed a 2-nucleotide deletion at position 2767-2768, which results in a frameshift and an immature termination codon. The cDNA of the MI line diverged from that of the KAT line at position 2865, having an 18-bp unique sequence followed by a poly(A) tail. The mutant cDNA encodes 922 amino acid residues which preserves the region for isomaltase but lacks that for whole sucrase. While the cells transfected with the plasmids expressing SI in the KAT line showed both sucrase and isomaltase activity, the plasmids expressing MI line cDNA showed only isomaltase activity. Thus it was concluded that the mutation in the SI gene was responsible for isolated sucrase deficiency in the MI line.Mammals of the order Insectivore have received attention as possible laboratory animals which are phylogenetically different from ordinarily used laboratory animals, such as the mouse, rat, hamster, and rabbit (1, 2). Both primates and rodents apparently originated from Insectivore and then evolved separately (3). In 1976, Oda and Kondo succeeded in rearing and breeding the house musk shrew, Suncus murinus, mammal belonging to the family Soricidae of Insectivore (4). Thereafter, several laboratory lines of suncus which originated from different wild populations in Asian regions have been developed in Nagoya, Japan, and a number of studies have been carried out on the morphology, endocrinology, and physiology of this animal (1). As a result, several lines of suncus were established as a model of sucrase deficiency. It was further established that hereditary sucrase deficiency in suncus was transmi...

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Maltase-Glucoamylase and Residual Isomaltase in Sucrose Intolerant Patients

Cited by 24 publications

References 0 publications

Congenital Sucrase‐Isomaltase Deficiency

Congenital Sucrase‐Isomaltase Deficiency

¹³C‐Breath Tests for Sucrose Digestion in Congenital Sucrase Isomaltase–deficient and Sacrosidase‐supplemented Patients

Molecular Cloning of Sucrase-Isomaltase cDNA in the House Musk Shrew Suncus murinusand Identification of a Mutation Responsible for Isolated Sucrase Deficiency

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Maltase-Glucoamylase and Residual Isomaltase in Sucrose Intolerant Patients

Cited by 24 publications

References 0 publications

Congenital Sucrase‐Isomaltase Deficiency

Congenital Sucrase‐Isomaltase Deficiency

13C‐Breath Tests for Sucrose Digestion in Congenital Sucrase Isomaltase–deficient and Sacrosidase‐supplemented Patients

Molecular Cloning of Sucrase-Isomaltase cDNA in the House Musk Shrew Suncus murinusand Identification of a Mutation Responsible for Isolated Sucrase Deficiency

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¹³C‐Breath Tests for Sucrose Digestion in Congenital Sucrase Isomaltase–deficient and Sacrosidase‐supplemented Patients