Abstract
Rat intestinal alkaline phosphatase exists in two separate forms, differing markedly in the carboxy-terminal coding region, as well as in the 3' untranslated regions. It is secreted bound to a phospholipid-rich particle (surfactant-like particle) which appears to have unique properties. Evidence is presented to suggest that intestinal alkaline phosphatase is secreted bound to this particle, and it in turn stimulates production of this particle. The particle appears to be associated with the process of fat absorption, as its secretion from the enterocyte is impaired when triacylglycerol secretion is decreased by the detergent Pluronic L-81. These data are consistent with a role of alkaline phosphatase in the post-prandial absorption of fat, and could explain the rise of alkaline phosphatase after fat feeding.
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