D-penicillamine inhibits transactivation of human immunodeficiency virus type-1 (HIV-1) LTR by transactivator protein. NLM AIDSLINE Important note: Information in this article was accurate in 1988. The state of the art may have changed since the publication date.

Click here to return to AIDSLINE main menu
DonateNow
Print this Article


D-penicillamine inhibits transactivation of human immunodeficiency virus type-1 (HIV-1) LTR by transactivator protein.

FEBS Lett. 1988 Aug 29;236(2):282-6. Unique Identifier : AIDSLINE MED/88312982
Chandra A; Demirhan I; Arya SK; Chandra P; Abteilung fur Molekularbiologie (ZBC), Klinikum der Universitat; Frankfurt, FRG.


Abstract: D-Penicillamine, an amino acid analogue of cysteine, has been shown to inhibit the transactivation of HIV-1 LTR by the transactivator protein, tat protein. The transactivation was studied in Jurkat cells co-transfected with plasmids containing HIV-LTR sequences fused to the bacterial chloramphenicol acetyltransferase (CAT) gene and HIV tat gene. The expression of CAT activity was a measure of transactivation of LTR by the tat protein. Incubation of transfected Jurkat cells with D-penicillamine led to inhibition of CAT activity. This inhibition was found to be concentration-dependent; more than 90% inhibition of chloramphenicol acetylation was seen in extracts prepared from cultures incubated with 40 micrograms/ml of D-penicillamine. Earlier experiments have shown that D-penicillamine at 40 micrograms/ml can completely inhibit HIV-1 (HTLV-III B) replication in H9 cells [(1986) Drug Res. 36, 184-186]. These results suggest that inhibition of transactivation may be the molecular mechanism involved in the inhibition of HIV-1 replication by D-penicillamine.
Keywords: Cell Line DNA-Binding Proteins/*ANTAGONISTS & INHIB Gene Expression Regulation/DRUG EFFECTS HIV/*GENETICS Penicillamine/*PHARMACOLOGY Regulatory Sequences, Nucleic Acid Retroviridae Proteins/*ANTAGONISTS & INHIB Support, Non-U.S. Gov't Transcription, Genetic/DRUG EFFECTS JOURNAL ARTICLE

KWDcelllinedna-bindingproteins/KWDantagonists&inhibgeneexpressionregulation/drugeffectshiv/KWDgeneticspenicillamine/KWDpharmacologyregulatorysequences,nucleicacidretroviridaeproteins/KWDantagonists&inhibsupport,non-uKWDsKWDgov'ttranscription,genetic/drugeffectsjournalarticle
881230
M88C0573


Copyright © 1988 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

AEGiS is a 501(c)3, not-for-profit, tax-exempt, educational corporation. AEGiS is made possible through unrestricted funding from Boehringer Ingelheim, Bridgestone/Firestone Charitable Trust, Bristol-Myers Squibb Company, Elton John AIDS Foundation, Gill Foundation, the National Library of Medicine, Quest Diagnostics, Roche and Trimeris, and donations from users like you. Always watch for outdated information. This article first appeared in 1988. This material is designed to support, not replace, the relationship that exists between you and your doctor.

AEGiS presents published material, reprinted with permission and neither endorses nor opposes any material. All information contained on this website, including information relating to health conditions, products, and treatments, is for informational purposes only. It is often presented in summary or aggregate form. It is not meant to be a substitute for the advice provided by your own physician or other medical professionals. Always discuss treatment options with a doctor who specializes in treating HIV.

Copyright ©1980, 1988. AEGiS. All materials appearing on AEGiS are protected by copyright as a collective work or compilation under U.S. copyright and other laws and are the property of AEGiS, or the party credited as the provider of the content. .