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Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS‐1 cells
Author(s) -
Dumermuth Eric,
Eldering Joyce A.,
Grünberg Jürgen,
Jiang Weiping,
Sterchi Erwin E.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80421-p
Subject(s) - protease , hydrolase , protein subunit , enzyme , cloning (programming) , microbiology and biotechnology , peptide , metalloproteinase , chemistry , biochemistry , complementary dna , expression cloning , fusion protein , peptide sequence , biology , recombinant dna , gene , computer science , programming language
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.