Lymphocytes and promonocytes attach to the synthetic [Tyr5,12, Lys7]- polyphemusin II peptide
| Autor: | B S, Weeks, M, Nomizu, A, Otaka, C A, Weston, A, Okusu, H, Tamamura, A, Matsumoto, N, Yamamoto, N, Fujii |
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| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
Isoquinolines Virus Replication Monocytes Piperazines Cell Line Kinetics 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine Phorbol Esters Cell Adhesion HIV-1 Tumor Cells Cultured Humans Tetradecanoylphorbol Acetate Amino Acid Sequence Lymphocytes Peptides Antimicrobial Cationic Peptides |
| Zdroj: | Biochemical and biophysical research communications. 202(1) |
| ISSN: | 0006-291X |
| Popis: | The [Tyr5,12,Lys7]-polyphemusin II peptide (T22) has been shown to inhibit HIV-1 replication in lymphocytes. The mechanism of T22 inhibition of HIV-1 replication is not known but may involve T22 competition with HIV-1 for attachment sites on the plasma membrane of targeted cells. Here we find that three human immunocyte cell lines (H9, Jurkat, and U-937) attach to T22. The phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA), has been shown to activate intracellular protein kinase C and to stimulate lymphocyte attachment to various substrates through specific cell surface receptors. Here we find that TPA treatment enhances attachment of the immunocytes to T22 by three- to four-fold. These data demonstrate that T22 binds to immunocyte cell surfaces and support the hypothesis that T22 may inhibit HIV-1 replication by competing with the virus for a common cell surface receptor(s). |
| Databáze: | OpenAIRE |
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