Document Detail

Expression of the alpha subunit of PABA peptide hydrolase (EC in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer.
MedLine Citation:
PMID:  8262186     Owner:  NLM     Status:  MEDLINE    
In this paper, we report the expression of PPH alpha in the polarized cell line MDCK (Madin Darby canine kidney). In these cells, the enzyme was synthesized in an inactive proform, 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 PPH alpha was detectable on the surface of intact cells by immunofluorescence. 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 PPH alpha.
J Grünberg; E Dumermuth; J A Eldering; E E Sterchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  335     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1993 Dec 
Date Detail:
Created Date:  1994-01-26     Completed Date:  1994-01-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  376-9     Citation Subset:  IM    
Institute of Biochemistry and Molecular Biology, University of Berne, Switzerland.
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MeSH Terms
Amino Acid Sequence
Cell Line
Culture Media
Endoplasmic Reticulum / enzymology
Enzyme Activation
Enzyme Precursors / metabolism
Fluorescent Antibody Technique
Metalloendopeptidases / genetics*,  metabolism,  secretion
Molecular Sequence Data
Protein Processing, Post-Translational
Reg. No./Substance:
0/Culture Media; 0/Enzyme Precursors; EC; EC 3.4.24.-/Metalloendopeptidases; EC A

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