Hypolactasia as a molecular basis of lactose intolerance.
Indian J Biochem Biophys
;
2006 Oct; 43(5): 267-74
Article
in English
| IMSEAR
| ID: sea-26865
ABSTRACT
Lactase-phlorizin hydrolase (LPH), a membrane-bound glycoprotein present in the luminal surface of enterocytes in the intestine is responsible for lactose intolerance, a phenomenon prevalent in humans worldwide. In the rodent intestine, the post-natal development of the LPH follows a specific pattern, such that the enzyme levels are high in the peri-natal period, but declines considerably upon maturation. The observed maturational decline in the LPH activity is very similar to adult-type hypolactasia observed in humans. Majority of the studies have been carried out using animal models or cell lines and a number of hypotheses have been put forward to explain the maturational decline of lactase activity such as (a) decreased amount of lactase protein, (b) defect in post-translational modification of precursor lactase to the mature enzyme, and (c) synthesis of an inactive, high molecular weight lactase with altered glycosylation, however, the precise underlying mechanism of adult-type hypolactasia remains undefined. The present review describes the recent developments in understanding the regulation of lactase expression and the possible mechanism of adult-type hypolactasia, as a cause of lactose intolerance.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Polymorphism, Genetic
/
Glycosylation
/
Humans
/
Gene Expression Regulation, Enzymologic
/
Lactase-Phlorizin Hydrolase
/
Lactase
/
Lactose
/
Lactose Intolerance
/
Animals
Language:
English
Journal:
Indian J Biochem Biophys
Year:
2006
Type:
Article
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