期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 343, 期 2, 页码 617-622出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2006.02.190
关键词
alpha-antitrypsin; antithrombin III; proteinase inhibitor 9; LDL-receptor-related protein; CD91; CD36; U937 cells; interferon alpha 2
Serpin A1 (alpha 1-proteinase inhibitor) inhibits human immunodeficiency virus 1 (HIV-1) production by mechanisms which remain to be elucidated. The complex formation of serpin A1 with proteinases eliminates the proteolytic activity and generates a fragment corresponding to the serpin C-terminal 36-residue peptide. Here, we show that the C-terminal 26-residue peptide of serpin A1 (A1-C26) inhibits HIV-Iong terminal repeat (LTR)-driven transcription in epithelial cells transfected with HIV-1 LTR promoter-driven genes. A1-C26 increased STAT1 phosphorylation and strongly reduced viral expression in a monocytic cell line infected with HIV-1 NL4-3. This reduction of expression was also observed in HIV-1 infected, PHA-activated peripheral blood mononuclear cells. In HIV-1 infected cells, the inhibitory activity of HIV-1 caused by B9-C23 and C1-C26, the A1-C26 homologues corresponding to the C-terminal sections of serpin B9 and serpin C1, was much lower than that obtained with Al-C26. These serpin peptides represent a novel class of antiviral agents. (c) 2006 Elsevier Inc. All rights reserved.
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