Publication: Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase
Authors
Naim, H.Y.
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Publisher
Murcia : F. Hernández
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Description
Abstract
Carbohydrates are hydrolyzed in the
intestinal lumen by specific enzymes to monosaccharides
before transport across the brush border
membrane of epithelial cells into the cell interior. The
enzymes implicated in the digestion of carbohydrates in
the intestinal lumen are membrane-bound glycoproteins
that are expressed at the apical domain of the
enterocytes. Absent or reduced activity of one of these
enzymes is the cause of disaccharide intolerance and
malabsorption, the symptoms of which are abdominal
pain, cramps or distention, flatulence, nausea and
osmotic diarrhea. Lactose intolerance is the most
common intestinal disorder that is associated with an
absence or drastically reduced levels of an intestinal
enzyme, in this case lactase-phlorizin hydrolase (LPH).
The pattern of reduction of activity has been temed late
onset of lactase deficiency or adult type hypolactasia. It
was thought that the regulation of LPH was posttranslational
and was associated with altered structural
features of the enzyme. Recent studies, however, suggest
that the major mechanism of regulation of LPH is
transcriptional. Other forms of lactose intolerance
include the rare congenital lactase deficiency and
secondary forms, such as those caused by mucosa1
injury, due to infectious gastroenteritis, celiac disease,
parasitic infection, drug-induced enteritis and Crohn's disease. This review will shed light on important
strucural and biosynthetic aspects of LPH, the role
played by particular regions of the LPH protein in its
transport, polarized sorting, and function, as well as on
the gene expession and regulation of the activity of the
enzyme.
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