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M9470123.TXT
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1994-07-02
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Document 0123
DOCN M9470123
TI Identification of the U-937 membrane-associated proteinase interacting
with the V3 loop of HIV-1 gp120 as cathepsin G.
DT 9409
AU Avril LE; Di Martino-Ferrer M; Pignede G; Seman M; Gauthier F;
Laboratoire d'Enzymologie, Centre National de la Recherche; Scientifique
URA 1334, University Francois Rabelais, Faculty of; Medicine, Tours,
France.
SO FEBS Lett. 1994 May 23;345(1):81-6. Unique Identifier : AIDSLINE
MED/94252410
AB We have purified a serine proteinase from the membrane of U-937 cells
that was inhibited in a tight-binding manner by recombinant gp120 and by
peptides mimicking the V3 loop of gp120 [(1993) FEBS Lett. 317,
167-172]. This proteinase has now been characterized, both structurally
and functionally. It has a dual trypsin- and chymotrypsin-like
specificity, and N-terminal sequence analysis of the first 32 residues
indicates complete identity with leukocyte cathepsin G. Cathepsin G-like
material was located at the surface of U-937 cells using a monoclonal
antibody directed against leukocyte cathepsin G, and polyclonal
anti-cathepsin G antibodies precipitated the purified proteinase.
However, the U-937 enzyme differs slightly from commercial leukocyte
cathepsin G in its apparent M(r) because of different glycosylation. No
other protein structurally related to cathepsin G was found upon
screening a U-937 cDNA library using several oligonucleotide probes
constructed from the membrane proteinase N-terminal amino acid sequence.
The possible interaction of a cathepsin G-like proteinase at the surface
of U-937 cells with the V3 loop of HIV-1 gp120 is discussed.
DE Amino Acid Sequence Base Sequence Cathepsins/IMMUNOLOGY/*ISOLATION &
PURIF/*METABOLISM Cell Membrane/*ENZYMOLOGY Cross Reactions DNA,
Complementary/GENETICS Human HIV Envelope Protein gp120/*METABOLISM
Immunoblotting Leukocytes/ENZYMOLOGY Molecular Sequence Data
Oligonucleotide Probes Peptide Fragments/*METABOLISM Sequence Analysis
Substrate Specificity Support, Non-U.S. Gov't Tumor Cells, Cultured
JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).