Amino-Terminal Fragment of Urokinase-Type Plasminogen Activator Inhibits HIV-1 Replication
| Autor: | Hiroyuki Shirono, Naoko A. Wada, Junichi Koga, Katsumi Taniguchi, Manabu Wada, Hideaki Tsuchie |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
CD4-Positive T-Lymphocytes
HIV Antigens viruses Biophysics Gene Products gag HIV Infections Receptors Cell Surface CD8-Positive T-Lymphocytes Biology Transfection Virus Replication gag Gene Products Human Immunodeficiency Virus Biochemistry Receptors Urokinase Plasminogen Activator Viral Proteins Genes Reporter medicine Humans Secretion Survivors Sarcoma Kaposi Molecular Biology Cells Cultured HIV Long Terminal Repeat Urokinase Reporter gene Dose-Response Relationship Drug Cell growth Cell Biology Urokinase-Type Plasminogen Activator Molecular biology Coculture Techniques Peptide Fragments Clone Cells Urokinase receptor Culture Media Conditioned HIV-1 Plasminogen activator Cell Division CD8 medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 284:346-351 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2001.4965 |
| Popis: | CD8+ T lymphocytes have been shown to produce unidentified soluble factors active in suppressing HIV-1 replication. In this study, we purified an HIV-1 suppressing activity from the culture supernatant of an immortalized CD8+ T cell clone, derived from an HIV-1 infected long-term nonprogressor, and identified this activity as the amino-terminal fragment (ATF) of urokinase-type plasminogen activator (uPA). ATF is catalytically inactive, but suppresses the release of viral particles from the HIV-1 infected cell lines via binding to its receptor CD87. In contrast, cell proliferation and the secretion of an HIV-1 LTR driven reporter gene product were not affected by ATF. These findings suggest that ATF may inhibit the assembly and budding of HIV-1, which provides a novel therapeutic strategy for AIDS. |
| Databáze: | OpenAIRE |
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