Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS‐1 cells
- 13 December 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 335 (3) , 367-375
- https://doi.org/10.1016/0014-5793(93)80421-p
Abstract
PABA peptide hydrolase (PPH) from human enterocytes is comprised of two submits, alpha and beta. PPHα 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, and a putative C-terminal membrane spanning domain. Expression of a chimeric meprin-PPHα 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.Keywords
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