AJP - GI AJP: Renal Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Gastrointest Liver Physiol 274: G342-G349, 1998;
0193-1857/98 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yuan, X.
Right arrow Articles by Sadler, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yuan, X.
Right arrow Articles by Sadler, J. E.
Vol. 274, Issue 2, G342-G349, February 1998

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

Xin Yuan, Xinglong Zheng, Deshun Lu, Deborah C. Rubin, Christopher Y. M. Pung, and J. Evan Sadler

Howard Hughes Medical Institute, Departments of Medicine and Biochemistry and Molecular Biophysics, Barnes-Jewish Hospital, Washington University School of Medicine, St. Louis, Missouri 63110

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 ~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.

duodenum; trypsinogen activation; serine protease; pancreatic enzymes


This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
T. Imamura and Y. Kitamoto
Expression of enteropeptidase in differentiated enterocytes, goblet cells, and the tumor cells in human duodenum
Am J Physiol Gastrointest Liver Physiol, December 1, 2003; 285(6): G1235 - G1241.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
X. Zheng and J. E. Sadler
Mucin-like Domain of Enteropeptidase Directs Apical Targeting in Madin-Darby Canine Kidney Cells
J. Biol. Chem., February 22, 2002; 277(9): 6858 - 6863.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. D. Hooper, J. A. Clements, J. P. Quigley, and T. M. Antalis
Type II Transmembrane Serine Proteases. INSIGHTS INTO AN EMERGING CLASS OF CELL SURFACE PROTEOLYTIC ENZYMES*
J. Biol. Chem., January 5, 2001; 276(2): 857 - 860.
[Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online