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C3-induced 3LL cell proliferation is mediated by C kinase
Agostina Longo1, Roberto Gradini, Vincenzo Mattei
1Department of Experimental Medicine and Pathology, La Sapienza University, Viale Regina Elena, 324 00161 Roma, Italy.
Journal of Cellular Biochemistry
|November 18, 2004
Summary
The third component of complement (C3) and its peptides promote cell proliferation. This study reveals that C3 internalization and protein kinase C-dependent phosphorylation are crucial for C3-stimulated proliferation in Lewis lung carcinoma cells.
Area of Science:
- Cell Biology
- Immunology
- Biochemistry
Background:
- The third component of complement (C3) and its peptides are known to enhance both normal and tumor cell proliferation.
- The precise signaling pathways mediating C3-induced cell proliferation remain largely unelucidated.
Purpose of the Study:
- To investigate the mechanisms underlying C3-stimulated cell proliferation.
- To explore the role of C3 peptide trafficking, subcellular localization, and protein phosphorylation in this process.
Main Methods:
- Investigated the influx and efflux of C3 peptides.
- Determined the subcellular localization of internalized C3.
- Assessed the role of protein phosphorylation, specifically protein kinase C, in C3 traffic and Lewis lung carcinoma (3LL) cell proliferation.
Main Results:
- C3 peptide traffic is independent of cytoskeletal integrity.
- C3 traffic necessitates protein kinase C-dependent phosphorylation.
- Proliferation of 3LL cells stimulated by C3 requires both C3 internalization and protein kinase C phosphorylation.
Conclusions:
- Protein kinase C-dependent phosphorylation is a key regulator of C3 peptide trafficking.
- C3-mediated proliferation of Lewis lung carcinoma cells is contingent upon C3 internalization and protein kinase C activity.