ArticleJapanese journal of cancer research : Gann2001
PI3-kinase p85alpha is a target molecule of proline-rich antimicrobial peptide to suppress proliferation of ras-transformed cells.
Article in Japanese journal of cancer research : Gann, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 45 citations in OpenAlex.
- Anti-Cancer Peptides: Status and Future Prospects.Molecules (Basel, Switzerland) · 2023Review
- NADPH oxidases: Current aspects and tools.Redox biology · 2020Review
- Combination of cecropinXJ and LY294002 induces synergistic cytotoxicity, and apoptosis in human gastric cancer cells via inhibition of the PI3K/Akt signaling pathway.Oncology letters · 2017Article
- Antimicrobial Peptides from Fruits and Their Potential Use as Biotechnological Tools-A Review and Outlook.Frontiers in microbiology · 2016Review
- Nox Inhibitors & Therapies: Rational Design of Peptidic and Small Molecule Inhibitors.Current pharmaceutical design · 2015Review
- Redox control of leukemia: from molecular mechanisms to therapeutic opportunities.Antioxidants & redox signaling · 2013Review
- Article
- Antimicrobial peptides: versatile biological properties.International journal of peptides · 2013Article
- Novel p65 binding glucocorticoid-induced leucine zipper peptide suppresses experimental autoimmune encephalomyelitis.The Journal of biological chemistry · 2011Article
- Membrane-active host defense peptides--challenges and perspectives for the development of novel anticancer drugs.Chemistry and physics of lipids · 2011Review
- Studies on anticancer activities of antimicrobial peptides.Biochimica et biophysica acta · 2008Review
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PR-39, which is an endogenous antimicrobial peptide, can bind to Src homology 3 domains of the NADPH complex protein p47(phox) and the signaling adapter protein p130(Cas). Recently, we have reported that PR-39 gene transduction altered invasive activity and actin structure of human hepatocellular carcinoma cells, suggesting that this peptide affects cellular signaling due to its proline-rich motif. In order to clarify the mechanism of the PR-39 functions, we transfected the PR-39 gene into mouse NIH3T3 cells which had already been transformed with human activated k-ras gene. The PR-39 gene transfectant showed a reorganization of actin structure and suppression of cell proliferation both in vitro and in vivo. Decreases of MAP (mitogen-activated protein) kinase activity, cyclin D1 expression and JNK activity were observed in the PR-39 gene transfectant. Co-immunoprecipitation analysis revealed that PR-39 binds to PI3-kinase p85alpha, which is a regulatory subunit of PI3-kinase and one of the effectors by which ras induces cytoskeletal changes and stimulates mitogenesis. The PI3-kinase activity of the PR-39 gene transfectant was decreased compared with that of the ras transformant. These results suggest that PR-39 alters actin structure and cell proliferation rate by binding to PI3-kinase p85alpha and suppressing the PI3-kinase activity.
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