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Volume 272, Number 19,
Issue of May 9, 1997
pp. 12591-12600
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Evidence for a Role of the Gut Hormone PYY in the Regulation of
Intestinal Fatty Acid-binding Protein Transcripts in Differentiated
Subpopulations of Intestinal Epithelial Cell Hybrids
(Received for publication, December 17, 1996, and in revised form, February 12, 1997)
Gunnel
Halldén
and
Gregory W.
Aponte
From the Department of Nutritional Sciences, University of
California, Berkeley, California 94720-3104
Peptide tyrosine tyrosine (PYY) is a gut hormone
present in endocrine cells in the lower intestine that can be released
by the presence of luminal free fatty acids (FFAs). The biological action of this peptide includes inhibition of gut motility and gastrointestinal and pancreatic secretions. Intestinal fatty
acid-binding protein (I-FABP) binds FFA and may be involved in their
cytosolic trafficking. Quantitative in situ hybridization
on heterogeneous populations of small intestinal somatic cell hybrids
selected for endogenous I-FABP expression (hBRIE 380i cells)
demonstrated a 5-fold increase in I-FABP transcripts in response to PYY
(within 6 h) that was confined to clusters of differentiated
cells, whereas ribonuclease protection assays performed on
heterogeneous populations of these cells showed no significant
differences. High affinity PYY receptors, with an IC50 of
5-50 pM, were identified in both differentiated and
nondifferentiated cell populations, as determined by competitive
binding assays and autoradiography. In situ hybridization of rat ileal tissue also revealed differing patterns of mRNA
expression for liver fatty acid-binding protein (L-FABP) and I-FABP.
Only I-FABP mRNA was detected in the villus tips. This localization correlated with the expression pattern of I-FABP mRNA in the hBRIE 380i cells where changes in transcripts were observed only in differentiated cells that did not incorporate bromodeoxyuridine. The
sustained expression of I-FABP transcripts in the villar tips suggests
(unlike L-FABP) that older terminally differentiated cell populations
of the mucosa can still be PYY responsive. These studies demonstrate
that physiological concentrations of PYY can regulate I-FABP and place
this peptide in a key position as part of a feedback system that
determines the processing of cytosolic FFA in the enterocyte. In
addition, these studies suggest a mechanism whereby luminal agents can
modulate expression of proteins in terminally differentiated cells in
the gastrointestinal mucosa.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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