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J. Biol. Chem., Vol. 276, Issue 18, 14562-14571, May 4, 2001
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From the Extracellular serine protease neuropsin (NP) is
expressed in the forebrain limbic area of adult brain and is implicated
in synaptic plasticity. We screened for endogenous NP inhibitors with
recombinant NP (r-NP) from extracts of the hippocampus and the cerebral
cortex in adult mouse brain. Two SDS-stable complexes were detected,
and after their purification, peptide sequences were determined by
amino acid sequencing and mass spectrometry, revealing that target
molecules were serine proteinase inhibitor-3 (SPI3) and murinoglobulin
I (MUG I). The addition of the recombinant SPI3 to r-NP resulted in an
SDS-stable complex, and the complex formation followed bimolecular
kinetics with an association rate constant of 3.4 ± 0.22 × 106 M
Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent
Inhibitors of Neuropsin in Adult Mouse Brain*
§,¶,,,¶,,
,,,,,, and
Division of Structural Cell Biology, Nara
Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara,
630-0101 Japan, Biomolecular Characterization Division, RIKEN
(The Institute for Physical and Chemical Research), Wako, Saitama
351-0198, Japan, ** Department of Biochemistry and Molecular Biology,
P.O. Box 13D, Monash University 3800, Australia, the
Faculty of Pharmaceutical Science, Kinki
University, 3-4-1 Kowakae, Higashi-osaka, Osaka 577-8502, Japan, the
§§ Department of Biochemistry, Kinki University
School of Medicine, 377-2 Oonohigashi, Sayama, Osaka 589-8511, Japan,
¶¶ Center for Research and Education, Graduate School of
Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan, and the Department of Pharmaceutical Development,
Medial and Biological Laboratories Co., Ltd., 1063-103 Ohara
Terasawaoka, Ina Nagano 396-0002, Japan
1
s1, showing that SPI3 was a slow, tight
binding inhibitor of NP. In situ hybridization
histochemistry showed that SPI3 mRNA was expressed in pyramidal
neurons in the hippocampal CA1-CA3 subfields, as was NP mRNA.
Alternatively, the addition of purified plasma MUG I to r-NP resulted
in an SDS-stable complex, and MUG I inhibited degradation of
fibronectin by r-NP to 24% at a r-NP/MUG I molar ratio of 1:2.
Immunofluorescence histochemistry showed that MUG I localized in the
hippocampal neurons. These findings indicate that SPI3 and MUG I serve
to inactivate NP and control the level of NP in adult brain, respectively.
*
This work was supported in part by grants from the Ministry
of Education, Science, Culture, and Sports in Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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