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J Biol Chem, Vol. 273, Issue 32, 20417-20424, August 7, 1998

Folylpoly--glutamate Carboxypeptidase from Pig Jejunum
MOLECULAR CHARACTERIZATION AND RELATION TO GLUTAMATE CARBOXYPEPTIDASE II

Charles H. Halsted, Erh-hsin Ling, Ruth Luthi-Carter^¶, Jesus A. Villanueva, John M. Gardner, and Joseph T. Coyle^¶

From the  Department of Internal Medicine, School of Medicine and  Center for Engineering of Plants for Resistance against Pathogens, University of California, Davis, California 95616 and the ^¶ Department of Psychiatry, Harvard Medical School, Boston, Massachusetts 02115

Jejunal folylpoly--glutamate carboxypeptidase hydrolyzes dietary folates prior to their intestinal absorption. The complete folylpoly--glutamate carboxypeptidase cDNA was isolated from a pig jejunal cDNA library using an amplified homologous probe incorporating primer sequences from prostate-specific membrane antigen, a protein capable of folate hydrolysis. The cDNA encodes a 751-amino acid polypeptide homologous to prostate-specific membrane antigen and rat brain N-acetylated -linked acidic dipeptidase. PC3 transfectant membranes exhibited activities of folylpoly--carboxypeptidase and N-acetylated -linked acidic dipeptidase, while immunoblots using monoclonal antibody to native folylpoly--glutamate carboxypeptidase identified a glycoprotein at 120 kDa and a polypeptide at 84 kDa. The kinetics of native folylpoly--carboxypeptidase were expressed in membranes of PC3 cells transfected with either pig folylpoly--carboxypeptidase or human prostate-specific membrane antigen. Folylpoly--carboxypeptidase transcripts were identified at 2.8 kilobase pairs in human and pig jejunum, human and rat brain, and human prostate cancer LNCaP cells. Thus, pig folylpoly--carboxypeptidase, rat N-acetylated -linked acidic dipeptidase, and human prostate-specific membrane antigen appear to represent varied expressions of the same gene in different species and tissues. The discovery of the jejunal folylpoly--carboxypeptidase gene provides a framework for future studies on relationships among these proteins and on the molecular regulation of intestinal folate absorption.

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