Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides
| Autor: | Akira Hattori, Tomohiro Rogi, Masafumi Tsujimoto, Tetsuro Nagasaka, Nobuo Tsuruoka, Shigehiko Mizutani, Hideko Matsumoto |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
medicine.medical_specialty
Forskolin Cystinyl Aminopeptidase digestive oral and skin physiology Cell Neuropeptide Dynorphin A Intracellular vesicle Biology Biochemistry chemistry.chemical_compound medicine.anatomical_structure Nerve growth factor Endocrinology nervous system chemistry Placenta Internal medicine medicine human activities |
| Zdroj: | European Journal of Biochemistry. 268:3259-3266 |
| ISSN: | 0014-2956 |
| DOI: | 10.1046/j.1432-1327.2001.02221.x |
| Popis: | The placental leucine aminopeptidase (P-LAP)/oxytocinase whose serum level increases with gestation is thought to contribute to the maintenance of normal pregnancy. P-LAP mRNAs are expressed in various tissues other than the placenta. In this study, we identified P-LAP protein in the brain. In contrast with the placenta where a significant portion of P-LAP is released, the enzyme was localized in the membrane fraction in brain and PC12 cells and no soluble form of the enzyme was detected. When PC12 cells were differentiated into neuronal cells by nerve growth factor (NGF), a significant increase in the expression level of P-LAP in the cell was observed. As in the case of insulin treatment of 3T3-L1 adipocytes, treatment of PC12 cells with forskolin caused the translocation of the enzyme from intracellular vesicle to the cell surface plasma membrane. In addition, P-LAP was shown to degrade several bioactive neuropeptides such as Met-enkephalin and dynorphin A (1–8). These results suggest that P-LAP plays an important role in the regulation of neuronal cell function in the brain. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|