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
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