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C3‐induced 3LL cell proliferation is mediated by C kinase
Author(s) -
Longo Agostina,
Gradini Roberto,
Mattei Vincenzo,
Morgante Emanuela,
Sale Patrizio,
Tafani Marco,
Lipari Marcella,
Pontieri Giuseppe M.,
Russo Matteo A.
Publication year - 2004
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20336
Subject(s) - phosphorylation , microbiology and biotechnology , cell growth , protein kinase c , kinase , protein kinase a , chemistry , cell , signal transduction , biology , biochemistry
It has been demonstrated that the third component of complement (C3) 1 and its peptides increase normal and tumour cell proliferation. However, the signal cascade responsible for this phenomenon is still unknown. In this study, we elucidate some of the mechanisms involved in the signalling of C3 stimulation of cell proliferation. We have first investigated the in and out traffic of C3 peptides, then we have identified the subcellular localisation of internalised C3 and, finally, we have explored the role of protein phosphorylation in C3 traffic and in the proliferation of the Lewis lung carcinoma (3LL) cells. Our results indicate that traffic of C3 is not dependent on cytoskeletal integrity and requires protein kinase C‐dependent phosphorylation. In addition, proliferation of 3LL cells stimulated by C3 depends on both C3 internalisation and protein‐kinase C phosphorylation. © 2004 Wiley‐Liss, Inc.