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Volume 272, Number 49, Issue of December 5, 1997 pp. 31006-31015
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Cloning and Characterization of a Novel Peptidase from Rat and Human Ileum

(Received for publication, May 5, 1997, and in revised form, September 17, 1997)

Benjamin L. Shneider , Sundararajah Thevananther ^¶ , M. Susan Moyer , Holly C. Walters , Piero Rinaldo ^** , Prasad Devarajan ^¶ , An Qiang Sun , Paul A. Dawson and Meenakshisundaram Ananthanarayanan

From the Department of Pediatrics, Divisions of  Pediatric Gastroenterology/Hepatology and ^¶ Pediatric Nephrology, and the ^** Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06520, the  Department of Internal Medicine Gastroenterology, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, North Carolina 27157, and the  Department of Pediatrics, Mount Sinai School of Medicine, New York, New York 10029-6574

A novel 100-kDa ileal brush border membrane protein (I100) has been purified by anionic glycocholate affinity chromatography. Polyclonal antibodies raised against this protein were utilized to clone and characterize I100 in rats. A partial length human I100 cDNA was identified by hybridization screening. In the rat, the I100 protein is a 746-amino acid glycosylated (calculated core molecular mass of 80 kDa) type II integral membrane protein found on the apical surface of ileal villus enterocytes. Its 2.6-kilobase mRNA is expressed in distal small intestine in rats and in humans. The I100 cDNA is homologous to but distinct from human prostate-specific membrane antigen and rat brain N-acetylaspartylglutamate peptidase. It is expressed on both the basolateral and apical surfaces of stably transfected Madin Darby canine kidney cells. Analysis of these stably transfected Madin Darby canine kidney cells and I100 immunoprecipitates of rat ileal brush border membrane vesicles reveals that it has dipeptidyl peptidase IV activity. Future invesitgations will need to determine the exact substrate specificity of this novel peptidase.

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