ArticleMolecular and cellular biochemistry1993
Kinetic study of the cytotoxic effect of alpha-sarcin, a ribosome inactivating protein from Aspergillus giganteus, on tumour cell lines: protein biosynthesis inhibition and cell binding.
Article in Molecular and cellular biochemistry, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 62 citations in OpenAlex.
- Review
- A novel Carcinoembryonic Antigen (CEA)-Targeted Trimeric Immunotoxin shows significantly enhanced Antitumor Activity in Human Colorectal Cancer Xenografts.Scientific reports · 2019Article
- Review
- Anti-tumor activities and apoptotic mechanism of ribosome-inactivating proteins.Chinese journal of cancer · 2015Review
- Hirsutellin A: A Paradigmatic Example of the Insecticidal Function of Fungal Ribotoxins.Insects · 2013Review
- The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins.Nature structural & molecular biology · 2006Article
- Leucine 145 of the ribotoxin alpha-sarcin plays a key role for determining the specificity of the ribosome-inactivating activity of the protein.Protein science : a publication of the Protein Society · 2003Article
- Backbone dynamics of the cytotoxic ribonuclease alpha-sarcin by 15N NMR relaxation methods.Journal of biomolecular NMR · 2002Article
- Involvement of the amino-terminal beta-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activity.Protein science : a publication of the Protein Society · 2001Article
- Antifungal proteins.Applied and environmental microbiology · 2001Review
- Construction, expression and characterization of chimaeric toxins containing the ribonucleolytic toxin restrictocin: intracellular mechanism of action.The Biochemical journal · 1997Article
- Virus-mediated release of endosomal content in vitro: different behavior of adenovirus and rhinovirus serotype 2.The Journal of cell biology · 1995Article
- Membrane interaction of a beta-structure-forming synthetic peptide comprising the 116-139th sequence region of the cytotoxic protein alpha-sarcin.Biophysical journal · 1995Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
alpha-Sarcin is a ribosome inactivating protein produced by the mould Aspergillus giganteus. The effect of this protein on eight different tumour cell lines has been studied in the absence of any agent affecting membrane permeability. The protein is cytotoxic for all the tumour cell lines considered. alpha-Sarcin modifies the cell proliferation pattern by inhibiting the protein biosynthesis of the cultured cells. No membrane damage produced by alpha-sarcin has been observed by measuring lactic dehydrogenase leakage. Alteration on the cell mitochondrial activity has not been detected upon treatment with alpha-sarcin. Differences on the extent of the protein binding to the cells have been observed by flow cytometric measurements. The kinetic analysis of the protein biosynthesis inhibition produced by alpha-sarcin reveals an alpha-sarcin concentration-dependent lag phase followed by a first order decrease of the protein synthesis rate. This parameter is dependent on the external alpha-sarcin concentration. A saturable component for the action of alpha-sarcin is also deduced from these experiments. Results are discussed in terms of the protein passage across the cell membrane as the potential rate-limiting step for the action of alpha-sarcin.
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