title: Ubiquitin-proteasome system is involved in induction of LFA-1/ICAM-1-dependent adhesion of HL-60 cells.
abstract: Membrane-permeable proteasome inhibitors, lactacystin (LC) and N-acetyl-Leu-Leu-norleucinal (ALLN), but not calpain inhibitor Z-Leu-leucinal (ZLL), prevented LFA-1/ICAM-1-dependent cellular adhesion of TPA-stimulated HL-60 cells. These proteasome inhibitors affected neither the induction of monocytic differentiation nor the accompanying protein-tyrosine phosphorylation. They suppressed the increase in the avidity of LFA-1 to ICAM-1 without changing the expression of these molecules. Immunoblotting using monoclonal antibody FK-1, which reacts specifically with polyubiquitinated proteins, demonstrated that the proteasome inhibitors caused the drastic accumulation of the polyubiquitinated proteins in the membrane fraction of TPA-treated HL-60 cells. This indicates that accompanying activation of LFA-1, TPA induces the polyubiquitination of the membrane proteins, which are rapidly degraded by proteasomes. These data taken together show that proteolysis mediated by the ubiquitin-proteasome system is a prerequisite for the induction of LFA-1-dependent adhesion of HL-60 cells.
authors.affiliation: Institute of Biomatrix, Nippi Inc., Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Katagiri
authors.forename: H
authors.initials: H
authors.lastname: Yokosawa
authors.forename: T
authors.initials: T
authors.lastname: Kinashi
authors.forename: S
authors.initials: S
authors.lastname: Kawashima
authors.forename: S
authors.initials: S
authors.lastname: Irie
authors.forename: K
authors.initials: K
authors.lastname: Tanaka
authors.forename: T
authors.initials: T
authors.lastname: Katagiri
mesh_terms: D000111:Acetylcysteine / Q000031:analogs & derivatives / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D000915:Antibody Affinity / Q000187:drug effects; D002448:Cell Adhesion / Q000187:drug effects; D002454:Cell Differentiation / Q000187:drug effects; D003546:Cysteine Endopeptidases / Q000502:physiology*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D018922:HL-60 Cells / Q000737:chemistry / Q000166:cytology* / Q000187:drug effects; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000494:pharmacology*; D007976:Leupeptins / Q000494:pharmacology; D016169:Lymphocyte Function-Associated Antigen-1 / Q000276:immunology / Q000494:pharmacology*; D009000:Monocytes / Q000166:cytology; D009097:Multienzyme Complexes / Q000502:physiology*; D046988:Proteasome Endopeptidase Complex; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014212:Tretinoin / Q000494:pharmacology; D014452:Ubiquitins / Q000502:physiology*
chemical_list: D015853:Cysteine Proteinase Inhibitors; D007976:Leupeptins; D016169:Lymphocyte Function-Associated Antigen-1; D009097:Multienzyme Complexes; D014452:Ubiquitins; C063261:acetylleucyl-leucyl-norleucinal; D018799:Intercellular Adhesion Molecule-1; C067713:lactacystin; D014212:Tretinoin; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases; D013755:Tetradecanoylphorbol Acetate; D000111:Acetylcysteine