PMID- 10215852
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 261
IP  - 2
DP  - 1999 Apr
TI  - N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase beta (human meprinbeta). A
      13-amino-acid sequence is required for proteolyticprocessing and subsequent
      secretion.
PG  - 421-9
AB  - N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase or human meprin (PPH) is a
      brush-border membrane enzyme of small intestinal epithelial cells. It is a type I
      integral membrane protein composed of two disulphide-bridged subunits (alpha and 
      beta). PPH and its homologous counterparts in rodents belong to the astacin
      family of zinc-metalloendopeptidases. Although the amino-acid sequence of the
      beta subunits is 80-90% identical in these three species, processing is
      different. Expression of PPHbeta in simian virus 40-transformed African green
      monkey kidney cells (COS-1) and Madin Darby canine kidney (MDCK) cells results in
      its cell surface localization and secretion, whereas mouse meprinbeta is only
      found at the plasma membrane. To investigate proteolytic processing of PPHbeta
      and to identify the cleavage site, different C-terminal domains of wild-type
      PPHbeta were exchanged with the homologous domains of mouse meprinbeta. We
      identified a 13-amino-acid sequence (QIQLTPAPSVQDL) necessary for cleavage and
      subsequent secretion of PPHbeta. Using brefeldin A, the site of processing was
      identified as being after passage through the Golgi compartment. Proteolytic
      processing of PPHbeta thus provides a means for secretion of alphabeta
      heterodimers.
FAU - Pischitzis, A
AU  - Pischitzis A
AD  - Institute of Biochemistry and Molecular Biology, University of Berne,
      Switzerland.
FAU - Hahn, D
AU  - Hahn D
FAU - Leuenberger, B
AU  - Leuenberger B
FAU - Sterchi, E E
AU  - Sterchi EE
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Membrane Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 20350-15-6 (Brefeldin A)
RN  - EC 3.2.1.- (Hexosaminidases)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.18 (meprin A)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brefeldin A/pharmacology
MH  - Cell Line
MH  - Gene Expression Regulation, Enzymologic
MH  - Hexosaminidases/metabolism
MH  - Humans
MH  - Intestinal Mucosa/*enzymology
MH  - Membrane Proteins/chemistry/metabolism
MH  - Metalloendopeptidases/genetics/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Processing, Post-Translational/genetics
MH  - Recombinant Proteins/genetics
MH  - Sequence Alignment
MH  - Transfection
EDAT- 1999/04/24 00:00
MHDA- 1999/04/24 00:01
CRDT- 1999/04/24 00:00
PHST- 1999/04/24 00:00 [pubmed]
PHST- 1999/04/24 00:01 [medline]
PHST- 1999/04/24 00:00 [entrez]
AID - 10.1046/j.1432-1327.1999.00268.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1999 Apr;261(2):421-9. doi: 10.1046/j.1432-1327.1999.00268.x.