(2008) S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway. Journal of Leukocyte Biology. pp. 1484-1492. ISSN 0741-5400
Full text not available from this repository.
Abstract
The complex formed by two members of the S100 calcium-binding protein family, S100A8/A9, exerts apoptosis-inducing activity against various cells, especially tumor cells. Here, we present evidence that S100A8/A9 also has cell growth-promoting activity at low concentrations. Receptor of advanced glycation end product (RAGE) gene silencing and cotreatment with a RAGE-specific blocking antibody revealed that this activity was mediated via RAGE ligation. To investigate the signaling pathways, MAPK phosphorylation and NF-kappa B activation were characterized in S100A8/A9-treated cells. S100A8/A9 caused a significant increase in p38 MAPK and p44/42 kinase phosphorylation, and the status of stress-activated protein kinase/JNK phosphorylation remained unchanged. Treatment of cells with S100A8/ A9 also enhanced NF-kappa B activation. RAGE small interfering RNA pretreatment abrogated the S100A8/ A9-induced NF-kappa B activation. Our data indicate that S100A8/A9-promoted cell growth occurs through RAGE signaling and activation of NF-kappa B.
Item Type: | Article |
---|---|
Keywords: | NF-kappa B proliferation MRP8 MRP14 endokines S100/calgranulins cytotoxic peptides glycation end-products calcium-binding proteins apoptosis-inducing activity endothelial-cells neurite outgrowth arachidonic-acid s100 proteins exudate cells metal-ions expression Cell Biology Hematology Immunology |
Page Range: | pp. 1484-1492 |
Journal or Publication Title: | Journal of Leukocyte Biology |
Journal Index: | ISI |
Volume: | 83 |
Number: | 6 |
Identification Number: | https://doi.org/10.1189/jlb.0607397 |
ISSN: | 0741-5400 |
Depositing User: | خانم مهدیه رضائی پور |
URI: | http://eprints.zaums.ac.ir/id/eprint/2852 |
Actions (login required)
![]() |
View Item |