Leukotactin-1-induced ERK activation is mediated via G i /G o protein/PLC/PKCδ/Ras cascades in HOS cells
Life Sciences, ISSN: 0024-3205, Vol: 73, Issue: 4, Page: 447-459
2003
- 21Citations
- 5Captures
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Article Description
Recently cloned leukotactin-1 (Lkn-1) that belongs to CC chemokine family has not been characterized. To understand the intracellular events following Lkn-1 binding to CCR1, we investigated the activities of signaling molecules in response to Lkn-1 in human osteogenic sarcoma cells expressing CCR1. Lkn-1-stimulated cells showed elevated phosphorylation of extracellular signal-related kinases (ERK1/2) with a distinct time course. ERK activation was peaked in 30 min and 12 h showing biphasic activation of ERK. Pertussis toxin, an inhibitor of G i /G o protein, and phospholipase C (PLC) inhibitor blocked Lkn-1-induced activation of ERK. Protein kinase Cδ (PKCδ) specific inhibitor rottlerin inhibited ERK activation in Lkn-1-stimulated cells. The activities of PLC and PKCδ were also enhanced by Lkn-1 stimulation. Dominant negative Ras inhibited activation of ERK. Immediate early response genes such as c-fos and c-myc were induced by Lkn-1 stimulation. Lkn-1 affected the cell cycle progression by cyclin D 3 induction. These results suggest that Lkn-1 activates the ERK pathway by transducing the signal through G i /G o protein, PLC, PKCδ and Ras, and it may play a role for cell proliferation, differentiation, and regulation of gene expression for other cellular processes.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0024320503003126; http://dx.doi.org/10.1016/s0024-3205(03)00312-6; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0038636024&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12759139; http://linkinghub.elsevier.com/retrieve/pii/S0024320503003126; http://api.elsevier.com/content/article/PII:S0024320503003126?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0024320503003126?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0024320503003126; http://dx.doi.org/10.1016/s0024-3205%2803%2900312-6; https://dx.doi.org/10.1016/s0024-3205%2803%2900312-6
Elsevier BV
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