AI Article Synopsis
- The study investigates how intestinal alkaline phosphatase (IAP) is secreted into blood using fetal and differentiated intestinal cell lines.
- In IRD-98 cells, tissue-unspecific alkaline phosphatase (AP) activity increased significantly with certain additives, but no AP was secreted into the medium.
- In contrast, Caco-2 cells demonstrated time-dependent secretion of newly synthesized IAP into the medium, with some AP remaining attached to membranes and released by serum addition.
Article Abstract
A fraction of intestinal alkaline phosphatase (IAP) is secreted into blood. To study this process, enzyme secretion was examined in a fetal (IRD-98) and a differentiated (Caco-2) intestinal cell line. Tissue-unspecific alkaline phosphatase (AP) activity in the IRD-98 cells increased 20-fold after addition of 1.5 mM sodium butyrate and 40 mM NaCl, but no AP activity was secreted into the medium. In contrast, newly synthesized IAP in Caco-2 cells was secreted into the medium. AP secretion increased with time and was inhibited by monensin. Medium AP was still partially bound to membranes as assessed by Triton X-114 phase separation and could be released by the addition of serum. Analysis by sodium dodecyl sulfate polyacrylamide gels and by isoelectric focussing showed that secreted AP gave a pattern similar to that of the AP released from membranes by phospholipase D treatment. When Caco-2 cells were grown on filters, AP activity was found in both basolateral (75%) and luminal (25%) media. These data demonstrate that the secretion of a particulate AP with extracellular release from the membrane can account for the appearance of the intestinal isozyme in both the serum and the lumen.
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| http://dx.doi.org/10.1152/ajpgi.1989.257.1.G14 | DOI Listing |
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