Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits epithelial cell proliferation, blocks nuclear localization sequence-dependent nuclear protein import

• Published in: The Journal of biological chemistry Vol. 274; no. 8; pp. 4890 - 4899
• Main Authors: Yu, L.G, Fernig, D.G, White, M.R.H, Spillers, D.G, Appleton, P, Evans, R.C, Grierson, I, Smith, J.A, Davies, H, Gerasimenko, O.V, Petersen, O.H
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 19.02.1999
• Subjects: adenocarcinoma; Adult; Agaricus bisporus; Amino Acid Sequence; Biological Transport; bovine serum albumin; Calcium-Calmodulin-Dependent Protein Kinases - metabolism; cell division; Cell Division - drug effects; cell lines; Cell Membrane Permeability - drug effects; colon; cytochemistry; Digitonin - pharmacology; endocytosis; Epithelial Cells - cytology; Epithelial Cells - drug effects; Female; Fluorescein - metabolism; heat shock proteins; HT29 Cells; Humans; inhibition; lectins; Lectins - pharmacology; Microscopy, Confocal; Microscopy, Electron; mitogen activated protein kinase; Molecular Sequence Data; mushrooms; Nuclear Localization Signals - drug effects; Nuclear Proteins - metabolism; nuclei; Nucleic Acid Synthesis Inhibitors - pharmacology; Protein Synthesis Inhibitors - pharmacology; protein transport; protein uptake; signal peptide; synthetic proteins

The Galβ1–3GalNAcα (TF antigen)-binding lectin (ABL) from the common edible mushroom ( Agaricus bisporus ) has a potent anti-proliferative effect without any apparent cytotoxicity. This unusual combination of properties prompted investigation of its mechanism of action. In contrast to soluble le...