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Targeting filamin B induces tumor growth and metastasis via enhanced activity of matrix metalloproteinase-9 and secretion of VEGF-A

Artikel i vetenskaplig tidskrift
Författare Sashidar Bandaru
Xianghua Zhou
Pegah Rouhi
Yan Zhang
Martin Bergö
Cao Yihai
Levent Akyürek
Publicerad i Oncogenesis
Volym 3
Sidor e119
ISSN 2157-9024
Publiceringsår 2014
Publicerad vid Sahlgrenska Cancer Center
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor e119
Språk en
Länkar dx.doi.org/10.1038/oncsis.2014.33
Ämnesord cancer, metastasis growth, mouse, zebrafish
Ämneskategorier Medicinsk cellbiologi, Molekylär medicin (genetik och patologi)

Sammanfattning

Filamins regulate cell locomotion and associate with diverse signaling molecules. We have recently found that targeting filamin A (FLNA) reduces RAS-induced lung adenocarcinomas. In this study, we explored the role of another major filamin isoform, filamin B (FLNB), in tumor development. In contrast to FLNA, we report that targeting FLNB enhances RAS-induced tumor growth and metastasis which is associated with higher matrix metallopeptidase-9 (MMP-9) and extracellular signal-regulated kinase (ERK) activity. Flnb deficiency in mouse embryonic fibroblasts results in increased proteolytic activity of MMP-9 and cell invasion mediated by the RAS/ERK pathway. Similarly, silencing FLNB in multiple human cancer cells increases the proteolytic activity of MMP-9 and tumor cell invasion. Furthermore, we observed that Flnb-deficient RAS-induced tumors display more capillary structures that is correlated with increased vascular endothelial growth factor-A (VEGF-A) secretion. Inhibition of ERK activation blocks phorbol myristate acetate-induced MMP-9 activity and VEGF-A secretion in vitro. In addition, silencing FLNB in human ovarian cancer cells increases secretion of VEGF-A that induces endothelial cells to form more vascular structures in vitro. We conclude that FLNB suppresses tumor growth and metastasis by regulating the activity of MMP-9 and secretion of VEGF-A which is mediated by the RAS/ERK pathway.

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