Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G.

Important note: Information in this article was accurate in 1994. The state of the art may have changed since the publication date.

Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G.

FEBS Lett. 1994 May 23;345(1):81-6. Unique Identifier : AIDSLINE MED/94252410
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.

Abstract: 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.

Keywords: 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

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