| Sucrase-isomaltase genotype and response to a starch-reduced and sucrose-reduced diet in IBS-D patients. | Sucrase-isomaltase genotype and response to a starch-reduced and sucrose-reduced diet in IBS-D patients.
Zamfir-Taranu A, Löscher BS, Husein DM, Hoter A, Garcia-Etxebarria K, Etxeberria U, Gayoso L, Mayr G, Nilholm C, Gustafsson RJ, Ozaydin O, Zheng T, Esteban-Blanco C, Bozzarelli I, Bonfiglio F, Rizk S, Franke A, Bujanda L, Naim HY, Ohlsson B, D'Amato M., Free PMC Article | 03/28/2024 |
| Prevalence of congenital sucrase-isomaltase deficiency in Turkey may be much higher than the estimates. | Prevalence of congenital sucrase-isomaltase deficiency in Turkey may be much higher than the estimates.
Taskin DG, Civan HA, Sari EE, Altuntaş C, Ersoy M, Tuncel T, Onay H, Selimoğlu A. | 06/28/2023 |
| Rare Hypomorphic Sucrase Isomaltase Variants in Relation to Irritable Bowel Syndrome Risk in UK Biobank. | Rare Hypomorphic Sucrase Isomaltase Variants in Relation to Irritable Bowel Syndrome Risk in UK Biobank.
Zheng T, Camargo-Tavares L, Bonfiglio F, Marques FZ, Naim HY, D'Amato M. | 03/19/2022 |
| The glucose-regulated protein GRP94 interacts avidly in the endoplasmic reticulum with sucrase-isomaltase isoforms that are associated with congenital sucrase-isomaltase deficiency. | The glucose-regulated protein GRP94 interacts avidly in the endoplasmic reticulum with sucrase-isomaltase isoforms that are associated with congenital sucrase-isomaltase deficiency.
Hoter A, Naim HY. | 01/1/2022 |
| Through a 2-step computational and experimental strategy, the present study found increased prevalence new dysfunctional SI variants associated with irritable bowel syndrome. | Increased Prevalence of Rare Sucrase-isomaltase Pathogenic Variants in Irritable Bowel Syndrome Patients.
Garcia-Etxebarria K, Zheng T, Bonfiglio F, Bujanda L, Dlugosz A, Lindberg G, Schmidt PT, Karling P, Ohlsson B, Simren M, Walter S, Nardone G, Cuomo R, Usai-Satta P, Galeazzi F, Neri M, Portincasa P, Bellini M, Barbara G, Jonkers D, Eswaran S, Chey WD, Kashyap P, Chang L, Mayer EA, Wouters MM, Boeckxstaens G, Camilleri M, Franke A, D'Amato M., Free PMC Article | 11/16/2019 |
| Three biosynthetic phenotypes for the novel SI mutations were identified. The first biosynthetic phenotype was defined by mutants that are intracellularly transported in a fashion similar to wild type SI and with normal, but varying, levels of enzymatic activity. The second biosynthetic phenotype was defined by mutants with delayed maturation and trafficking kinetics and reduced activity. The third is inactive. | Molecular pathogenicity of novel sucrase-isomaltase mutations found in congenital sucrase-isomaltase deficiency patients.
Gericke B, Amiri M, Scott CR, Naim HY. | 12/1/2018 |
| Novel compound heterozygote V577G/C1531W SI mutations, which lead to lack of SI expression in the duodenal brush border, were found in a family with congenital sucrase-isomaltase deficiency. | Congenital Sucrase-isomaltase Deficiency: A Novel Compound Heterozygous Mutation Causing Aberrant Protein Localization.
Haberman Y, Di Segni A, Loberman-Nachum N, Barel O, Kunik V, Eyal E, Kol N, Hout-Siloni G, Kochavi B, Avivi C, Schvimer M, Rechavi G, Anikster Y, Barshack I, Weiss B., Free PMC Article | 02/24/2018 |
| A common mutation was found in the sucrase-isomaltase gene, c.273_274delAG, to be responsible for the high prevalence of congenital sucrase-isomaltase deficiency among Inuit people. | Congenital sucrase-isomaltase deficiency: identification of a common Inuit founder mutation.
Marcadier JL, Boland M, Scott CR, Issa K, Wu Z, McIntyre AD, Hegele RA, Geraghty MT, Lines MA., Free PMC Article | 06/20/2015 |
| SI mutations result in loss of enzyme function by preventing the biosynthesis of catalytically competent SI at the cell surface in lymphocytic leukemia | Functional analysis of sucrase-isomaltase mutations from chronic lymphocytic leukemia patients.
Rodríguez D, Ramsay AJ, Quesada V, Garabaya C, Campo E, Freije JM, López-Otín C. | 03/8/2014 |
| study found four common mutations in the SI gene (3 of the 4 are in the sucrase domain, with 1 in the isomaltase domain) account for 59 percent of clinical symptoms of congenital sucrase-isomaltase deficiency (CSID); the remaining 41 percent were rare events | Four mutations in the SI gene are responsible for the majority of clinical symptoms of CSID.
Uhrich S, Wu Z, Huang JY, Scott CR. | 06/8/2013 |
| investigation of EIS (enzyme-inhibitor-substrate) complex of sucrase: kinetic studies of complex formation/stability; role of complex in prevention of hyperglycemia by L-arabinose | Determination of the transient period of the EIS complex and investigation of the suppression of blood glucose levels by L-arabinose in healthy adults.
Shibanuma K, Degawa Y, Houda K. | 12/24/2011 |
| Core2 O-glycan structure is essential for expression of SI and DDP-IV during intestinal cell differentiation. | Core2 O-glycan structure is essential for the cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV during intestinal cell differentiation.
Lee SH, Yu SY, Nakayama J, Khoo KH, Stone EL, Fukuda MN, Marth JD, Fukuda M., Free PMC Article | 01/1/2011 |
| The effects of mutations in the sucrase domain of SIC1229Y and SIF1745C indicate the importance of a direct interaction between isomaltase and sucrose and the role of sucrose as an intermolecular chaperone in the intracellular transport of SI | Compound heterozygous mutations affect protein folding and function in patients with congenital sucrase-isomaltase deficiency.
Alfalah M, Keiser M, Leeb T, Zimmer KP, Naim HY. | 01/21/2010 |
| phenylalanine cluster is required for shielding a folding determinant in the extracellular domain of SI; substitution of a Q by a P at residue 1098 of sucrase disrupts this determinant and elicits retention of SI(Q1098P) in ER and cis-Golgi | A phenylalanine-based folding determinant in intestinal sucrase-isomaltase that functions in the context of a quality control mechanism beyond the endoplasmic reticulum.
Pröpsting MJ, Kanapin H, Jacob R, Naim HY. | 01/21/2010 |
| glucose regulation of sucrase-isomaltase gene expression was attenuated in HNF-1alphaT539fsdelC cells, but was well maintained in empty vector & HNF-1betaR177X cells.Results suggest that HNF-1alpha participates in glucose regulation of SI gene expression. | HNF-1alpha participates in glucose regulation of sucrase-isomaltase gene expression in epithelial intestinal cells.
Gu N, Adachi T, Matsunaga T, Tsujimoto G, Ishihara A, Yasuda K, Tsuda K. | 01/21/2010 |
| These results suggest that sucrase-isomaltase transcription might be unchanged or lower in maturity-onset diabetes of the young (MODY) type 3, but greater in MODY5. | Effect of mutations in HNF-1alpha and HNF-1beta on the transcriptional regulation of human sucrase-isomaltase in Caco-2 cells.
Gu N, Suzuki N, Takeda J, Adachi T, Tsujimoto G, Aoki N, Ishihara A, Tsuda K, Yasuda K. | 01/21/2010 |
| The sucrase-isomaltase (SI) gene from 11 patients of Hungarian origin with congenital sucrase-isomaltase deficiency was analysed.In six out of the 11 patients the phenotype of CSID could be explained by compound heterozygosity. | Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption.
Sander P, Alfalah M, Keiser M, Korponay-Szabo I, Kovács JB, Leeb T, Naim HY. | 01/21/2010 |
| analysis of a mutation which affects an epitope responsible for the apical targeting fidelity of sucrase-isomaltase in congenital sucrase-isomaltase deficiency | Altered folding, turnover, and polarized sorting act in concert to define a novel pathomechanism of congenital sucrase-isomaltase deficiency.
Keiser M, Alfalah M, Pröpsting MJ, Castelletti D, Naim HY. | 01/21/2010 |
| hepatocyte nuclear factor (HNF)-1alpha and HNF-1beta would contribute to constitutive expression of the SI gene in the differentiated state in Caco-2 cells | Sucrase-isomaltase gene expression is inhibited by mutant hepatocyte nuclear factor (HNF)-1alpha and mutant HNF-1beta in Caco-2 cells.
Gu N, Adachi T, Takeda J, Aoki N, Tsujimoto G, Ishihara A, Tsuda K, Yasuda K. | 01/21/2010 |