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1996-02-27
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Document 0679
DOCN M9630679
TI Calcium requirement and inhibitor spectrum for intracellular HIV type 1
gp160 processing in cultured HeLa cells and CD4+ lymphocytes: similarity
to those of viral envelope glycoprotein maturase.
DT 9603
AU Kamoshita K; Shiota M; Sasaki M; Koga Y; Okumura Y; Kido H; Division of
Enzyme Chemistry, University of Tokushima.
SO J Biochem (Tokyo). 1995 Jun;117(6):1244-53. Unique Identifier : AIDSLINE
MED/96104996
AB We recently purified the calcium-independent processing protease named
viral envelope glycoprotein maturase (VEM), that converts human
immunodeficiency virus type 1 (HIV-1) envelope glycoprotein precursor
gp160 to gp120 and gp41, from the human CD4+ T cell line, Molt-4 clone 8
[Kido, H., Kamoshita, K., Fukutomi, A., and Katunuma, N. (1993) J. Biol.
Chem. 268, 13406-13413]. In this report, we deal with the inhibitor
specificity and calcium requirement for intracellular gp160 processing
in cultured HeLa cells and human CD4+ lymphocytes. Processing of gp160
in these cells infected with recombinant vaccinia virus encoding the
gp160 gene was not affected by intracellular calcium depletion induced
by the calcium ionophore A23187 and EGTA or by intracellular calcium
administration. Processing of gp160 by the purified VEM in vitro was not
inhibited by EDTA, EGTA, or the metallo-protease inhibitor
phosphoramidon, but was specifically inhibited by a substrate analog,
decanoyl-RVKR-chloromethylketone, and the trypsin-type protease
inhibitors aprotinin, HI-30, and diisopropyl fluorophosphate (DFP). It
was also inhibited by E-64 and thiol reagents. But intracellular gp160
processing was inhibited only by permeable, low molecular mass
inhibitors of VEM, such as DFP, E-64, and thiol reagents. Syncytium
formation induced by cell surface gp120 was also inhibited by permeable
inhibitors of VEM. Taken together, our results indicate that calcium
ions may not be essential for intracellular gp160 processing and so
HIV-1 gp160 induced by recombinant vaccinia virus may be processed
mainly by a protease(s) that does not require calcium ions, such as VEM
in these cells.
DE Amino Acid Sequence Aniline Compounds Calcimycin/PHARMACOLOGY
Calcium/*METABOLISM/PHARMACOLOGY CD4-Positive T-Lymphocytes/*METABOLISM
Egtazic Acid/PHARMACOLOGY Fluorescent Dyes Gene Products,
env/GENETICS/*METABOLISM Giant Cells/METABOLISM Glycoside
Hydrolases/METABOLISM Hela Cells Human *HIV-1/GENETICS Kinetics
Microscopy, Phase-Contrast Molecular Sequence Data Peptide
Peptidohydrolases/*METABOLISM Protease
Inhibitors/CHEMISTRY/PHARMACOLOGY Protein
Precursors/GENETICS/*METABOLISM *Protein Processing, Post-Translational
Recombinant Proteins/METABOLISM Sulfhydryl Reagents/PHARMACOLOGY
Support, Non-U.S. Gov't Vaccinia Virus Xanthenes JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).