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Publication : Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development.

First Author  Yuan X Year  1998
Journal  Am J Physiol Volume  274
Issue  2 Pt 1 Pages  G342-9
PubMed ID  9486188 Mgi Jnum  J:45786
Mgi Id  MGI:1196116 Doi  10.1152/ajpgi.1998.274.2.G342
Citation  Yuan X, et al. (1998) Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development. Am J Physiol 274(2 Pt 1):G342-9
abstractText  Enterokinase (enteropeptidase) is expressed only in proximal small intestine, where it initiates digestive enzyme activation by converting trypsinogen into trypsin. To investigate this restricted expression pattern, mouse enterokinase cDNA was cloned, and the distribution of enterokinase mRNA and enzymatic activity were determined in adult mice and during gestation. Analysis of enterokinase sequences showed that a mucinlike domain near the NH2 terminus is composed of repeated approximately 15-amino acid Ser/Thr-rich motifs. By Northern blotting and trypsinogen activation assays, enterokinase mRNA and enzymatic activity were undetectable in stomach, abundant in duodenum, and decreased distally until they were undetectable in midjejunum, ileum, and colon. By in situ mRNA hybridization, enterokinase mRNA was localized to the enterocytes throughout the villus. Expression was not observed in goblet cells, Paneth cells, or Brunner's glands. Enterokinase mRNA and enzymatic activity were not detected in the duodenum of fetal mice but were easily detected in the duodenum on postnatal days 2-6. Both enterokinase mRNA and enzymatic activity decreased to very low levels after day 7 but increased after weaning and reached a high level characteristic of adult life by day 60. Therefore, in mice, duodenal enterocytes are the major type of cells expressing enterokinase, which appears to be regulated at the level of mRNA abundance.
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