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Sucrase-isomaltase deficiency in humans : different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme

Naim, H. Y. and Roth, J. and Sterchi, E. E. and Lentze, M. and Milla, P. and Schmitz, J. and Hauri, H. P.. (1988) Sucrase-isomaltase deficiency in humans : different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme. Journal of Clinical Investigation, Vol. 82, H. 2. S. 667-679.

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Official URL: http://edoc.unibas.ch/dok/A5257824

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Abstract

Eight cases of congenital sucrase-isomaltase deficiency were studied at the subcellular and protein level with monoclonal antibodies against sucrase-isomaltase. At least three phenotypes were revealed: one in which sucrase-isomaltase protein accumulated intracellularly probably in the endoplasmic reticulum, as a membrane-associated high-mannose precursor, one in which the intracellular transport of the enzyme was apparently blocked in the Golgi apparatus, and one in which catalytically altered enzyme was transported to the cell surface. All patients expressed electrophoretically normal or near normal high-mannose sucrase-isomaltase. The results suggest that different, probably small, mutations in the sucrase-isomaltase gene lead to the synthesis of transport-incompetent or functionally altered enzyme which results in congenital sucrose intolerance.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Pharmacology/Neurobiology (Hauri)
UniBasel Contributors:Hauri, Hans-Peter
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:American Society for Clinical Investigation
ISSN:0021-9738
e-ISSN:1558-8238
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:13 Oct 2017 08:17
Deposited On:22 Mar 2012 13:19

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