ArticleThe Journal of clinical investigation2000
Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme.
Article in The Journal of clinical investigation, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 52 citations in OpenAlex.
- Amniotic Fluid Extracellular Vesicle Properties Evolve With Gestational Age and Reflect Fetal Development.Journal of extracellular biology · 2025Article
- Review
- Genetic Loss of Sucrase-Isomaltase Function: Mechanisms, Implications, and Future Perspectives.The application of clinical genetics · 2023Review
- Interaction between the α-glucosidases, sucrase-isomaltase and maltase-glucoamylase, in human intestinal brush border membranes and its potential impact on disaccharide digestion.Frontiers in molecular biosciences · 2023Article
- The patient journey to diagnosis and treatment of congenital sucrase-isomaltase deficiency.Quality of life research : an international journal of quality of life aspects of treatment, care and rehabilitation · 2021Observational
- Two Novel Mutations in theFrontiers in pediatrics · 2021Article
- Article
- Heterozygotes Are a Potential New Entity among Homozygotes and Compound Heterozygotes in Congenital Sucrase-Isomaltase Deficiency.Nutrients · 2019Article
- Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity.The Journal of biological chemistry · 2017Article
- Congenital Sucrase-isomaltase Deficiency: A Novel Compound Heterozygous Mutation Causing Aberrant Protein Localization.Journal of pediatric gastroenterology and nutrition · 2017Article
- Review
- The Pathobiochemistry of Gastrointestinal Symptoms in a Patient with Niemann-Pick Type C Disease.JIMD reports · 2016Article
- Predicting the impact of diet and enzymopathies on human small intestinal epithelial cells.Human molecular genetics · 2013Article
- Congenital sucrase-isomaltase deficiency: summary of an evaluation in one family.Journal of pediatric gastroenterology and nutrition · 2012Article
- Keratins modulate colonocyte electrolyte transport via protein mistargeting.The Journal of cell biology · 2004Article
- Small bowel review: Normal physiology, part 1.Digestive diseases and sciences · 2003Review
- Congenital sucrase-isomaltase deficiency presenting with failure to thrive, hypercalcemia, and nephrocalcinosis.BMC pediatrics · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Congenital sucrase-isomaltase deficiency (CSID) is an autosomal recessive human intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase, the components of the intestinal integral membrane glycoprotein sucrase-isomaltase (SI). Several known phenotypes of CSID result from an altered posttranslational processing of SI. We describe here a novel CSID phenotype, in which pro-SI undergoes an unusual intracellular cleavage that eliminates its transmembrane domain. Biosynthesis of pro-SI in intestinal explants and in cells transfected with the SI cDNA of this phenotype demonstrated a cleavage occurring within the endoplasmic reticulum due to a point mutation that converts a leucine to proline at residue 340 of isomaltase. Cleaved pro-SI is transported to and processed in the Golgi apparatus and is ultimately secreted into the exterior milieu as an active enzyme. To our knowledge this is the first report of a disorder whose pathogenesis results not from protein malfolding or mistargeting, but from the conversion of an integral membrane glycoprotein into a secreted species that is lost from the cell surface.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.