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The fungal chimerolectin MOA inhibits protein and DNA synthesis in NIH/3T3 cells and may induce BAX-mediated apoptosis.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2014 May 16; Vol. 447 (4), pp. 586-9. Date of Electronic Publication: 2014 Apr 18. - Publication Year :
- 2014
-
Abstract
- The Marasmius oreades mushroom agglutinin (MOA) is a blood group B-specific lectin carrying an active proteolytic domain. Its enzymatic activity has recently been shown to be critical for toxicity of MOA toward the fungivorous soil nematode Caenorhabditis elegans. Here we present evidence that MOA also induces cytotoxicity in a cellular model system (murine NIH/3T3 cells), by inhibiting protein synthesis, and that cytotoxicity correlates, at least in part, with proteolytic activity. A peptide-array screen identified the apoptosis mediator BAX as a potential proteolytic substrate and further suggests a variety of bacterial and fungal peptides as potential substrates. These findings are in line with the suggestion that MOA and related proteases may play a role for host defense.<br /> (Copyright © 2014 Elsevier Inc. All rights reserved.)
- Subjects :
- Agglutinins metabolism
Agglutinins pharmacology
Agglutinins toxicity
Amino Acid Substitution
Animals
Fungal Proteins metabolism
Fungal Proteins toxicity
Genetic Variation
Lectins metabolism
Lectins pharmacology
Lectins toxicity
Marasmius chemistry
Marasmius genetics
Mice
NIH 3T3 Cells
Nucleic Acid Synthesis Inhibitors pharmacology
Nucleic Acid Synthesis Inhibitors toxicity
Protein Synthesis Inhibitors pharmacology
Protein Synthesis Inhibitors toxicity
Apoptosis drug effects
Apoptosis physiology
Fungal Proteins pharmacology
bcl-2-Associated X Protein metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 447
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 24747075
- Full Text :
- https://doi.org/10.1016/j.bbrc.2014.04.043