Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells.
PABA peptide hydrolase (PPH) from human enterocytes is comprised of two subunits, alpha and beta. PPH alpha is over 70% identical to meprin, a protease isolated from mouse and rat kidney. The enzyme shows a modular organization in that it contains an astacin protease domain, an adhesive domain, an EGF-like domain, an a putative C-terminal membrane spanning domain. Expression of a chimeric meprin-PPH alpha cDNA in COS-1 cells led to the synthesis of immature, transport-incompetent homodimers. In addition, complex glycosylated forms were detected in the culture medium, suggesting that the enzyme is secreted after proteolytic removal of the membrane anchor.
Dumermuth
E
E
Institute of Biochemistry and Molecular Biology, University of Berne, Switzerland.
Eldering
J A
JA
Grünberg
J
J
Jiang
W
W
Sterchi
E E
EE
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007421:Intestine, Small / Q000201:enzymology*; D008666:Metalloendopeptidases / Q000096:biosynthesis / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D008625:Tiopronin / Q000378:metabolism
D004247:DNA; D008625:Tiopronin; D008666:Metalloendopeptidases; C053833:meprin A