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Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells
Author(s) -
Grünberg Jürgen,
Dumermuth Eric,
Eldering Joyce A.,
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)80422-q
Subject(s) - protein subunit , peptide , alpha (finance) , chemistry , hydrolase , g alpha subunit , enzyme , microbiology and biotechnology , protein expression , biochemistry , biology , medicine , gene , construct validity , nursing , patient satisfaction
In this paper, we report the expression of PPHα in the polarized cell line MDCK (Madin Darby canine kidney). In these cells, the enzyme was synthesized m an inactive profonn, which upon treatment with trypsin was activated. The enzyme isolated from cell extracts was core‐glycosylated and appeared to be retained in the ER as a homodimer. No PPHα was detectable on the surface of intact cells by immunofluoreseence. However, a complex glycosylated soluble but inactive form was present in the culture medium, suggesting that proteolytic removal of the C‐terminal membrane anchoring peptide leads to the secretion of PPHα.