Characterization of recombinant and brain neuropsin, a plasticity-related serine protease
| Autor: | Keiko Kato, Shigetaka Yoshida, Yoshiharu Momota, Takahiko Shiosaka, Akiko Kawabe, Chigusa Shimizu, Ryosuke Midorikawa, Sadao Shiosaka, Tomohiro Kamachi, Kazumasa Matsumoto, Masao Shibata |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
medicine.medical_treatment
Molecular Sequence Data Biology Biochemistry Hippocampus law.invention Substrate Specificity Mice law Gene expression medicine Animals Humans Amino Acid Sequence Enzyme Inhibitors Rats Wistar Molecular Biology Peptide sequence chemistry.chemical_classification Serine protease Enzyme Precursors Protease Neuronal Plasticity Hydrolysis Serine Endopeptidases Cell Biology Recombinant Proteins Fibronectins Rats Fibronectin Enzyme Activation Enzyme chemistry biology.protein Recombinant DNA Kallikreins KALLIKREIN 8 Subcellular Fractions |
| Zdroj: | The Journal of biological chemistry. 273(18) |
| ISSN: | 0021-9258 |
| Popis: | Activity-dependent changes in neuropsin gene expression in the hippocampus implies an involvement of neuropsin in neural plasticity. Since the deduced amino acid sequence of the gene contained the complete triplet (His-Asp-Ser) of the serine protease domain, the protein was postulated to have proteolytic activity. Recombinant full-length neuropsin produced in the baculovirus/insect cell system was enzymatically inactive but was readily converted to active enzyme by endoprotease processing. The activational processing of prototype neuropsin involved the specific cleavage of the Lys32-Ile33 bond near its N terminus. Native neuropsin that was purified with a purity of 1,100-fold from mouse brain had enzymatic characteristics identical to those of active-type recombinant neuropsin. Both brain and recombinant neuropsin had amidolytic activities cleaving Arg-X and Lys-X bonds in the synthetic chromogenic substrates, and the highest specific activity was found against Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide. The active-type recombinant neuropsin effectively cleaved fibronectin, an extracellular matrix protein. Taken together, these results indicate that this protease, which is enzymatically novel, has significant limbic effects by changing the extracellular matrix environment. |
| Databáze: | OpenAIRE |
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