PMID- 8939981
OWN - NLM
STAT- MEDLINE
DCOM- 19970113
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 271
IP  - 47
DP  - 1996 Nov 22
TI  - The cleavage of protein kinase A by the kinase-splitting membranal proteinase is 
      reproduced by meprin beta.
PG  - 30272-80
AB  - The Kinase-Splitting Membranal Proteinase (KSMP) is a metallo-endoproteinase that 
      clips off the carboxyl terminus tail of the catalytic (C) subunit of protein 
      kinase A to yield a truncated, catalytically inactive protein (C'). Here we 
      report (a) a new procedure for the purification of KSMP, yielding a major protein 
      band in SDS-polyacrylamide gel electrophoresis that correlates with the 
      characteristic KSMP activity; (b) the sequence of tryptic peptides obtained from 
      this band, suggesting an identity between this protein and meprin beta; (c) the 
      immuno-detection by specific anti-peptide antibodies of both the alpha and the 
      beta subunits of meprin in KSMP preparations; (d) the stable expression of meprin 
      beta in a mammalian cell line (293) to establish a clone that constitutively 
      expresses the full-length precursor of meprin beta; and (e) the optimalization of 
      the proteolytic activation of this precursor to obtain an enzyme exhibiting the 
      specific KSMP cleavage, suggesting that KSMP is either derived from, or identical 
      with, the meprin beta gene product. It is hoped that these results will shed 
      light on the possible physiological role of KSMP and the way it may affect 
      protein kinase A-mediated processes.
FAU - Chestukhin, A
AU  - Chestukhin A
AD  - Department of Biological Regulation, The Weizmann Institute of Science, Rehovot 
      76100, Israel. lishalt@weizmann.weizmann.ac.il
FAU - Muradov, K
AU  - Muradov K
FAU - Litovchick, L
AU  - Litovchick L
FAU - Shaltiel, S
AU  - Shaltiel S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Enzyme Precursors)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.21.4 (Trypsin)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.63 (meprin B)
RN  - EC 3.4.99.- (kinase-splitting membranal proteinase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cloning, Molecular
MH  - Cyclic AMP-Dependent Protein Kinases/*metabolism
MH  - Endopeptidases/isolation & purification/*metabolism
MH  - Enzyme Activation
MH  - Enzyme Precursors/metabolism
MH  - Hydrolysis
MH  - Metalloendopeptidases/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Protein Biosynthesis
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Trypsin/metabolism
EDAT- 1996/11/22 00:00
MHDA- 1996/11/22 00:01
CRDT- 1996/11/22 00:00
PHST- 1996/11/22 00:00 [pubmed]
PHST- 1996/11/22 00:01 [medline]
PHST- 1996/11/22 00:00 [entrez]
AID - S0021-9258(19)79275-8 [pii]
AID - 10.1074/jbc.271.47.30272 [doi]
PST - ppublish
SO  - J Biol Chem. 1996 Nov 22;271(47):30272-80. doi: 10.1074/jbc.271.47.30272.