Skip to main content

Table 2 Summary of literature of filamin-A in cancer metastasis

From: Complex roles of filamin-A mediated cytoskeleton network in cancer progression

Research system Observations Reference
Literatures reported the role of filamin-A in facilitating metastasis and cell locomotion
Meckel-Gruber syndrome patient Filamin-A interacts with the cytoplasmic domain of meckelin, a transmembrane receptor, which is essential for neuronal migration and Wnt signalling [111]
Hepatocellular carcinoma (HCC) Comparative proteomics revealed that high level of filamin-A expression is associated with increased metastatic potentials of HCC cells. [112]
Cancer tissues By using a newly developed antibody that recognizes secreted variant of filamin-A, gradually increased levels of filamin-A was detected in normal breast tissue, localized and invasive breast cancer, which is associated with cancer progression. [113]
Prostate cancer cell and tissue microarray Filamin-A proteolysis results in nuclear localization of 90 kDa fragment, which is associated with decreased cancer metastasis, while elevated cytoplasmic levels of filamin-A was associated with enhanced metastatic potential [114]
FlnA-knockdown rats Filamin-A deficiency results in the abnormal migration, and then further causes disorganization of radial glia, which is the leading cause of PH pathogenesis. [115]
NIH3T3 and HT1080 cells Interaction of filamin-A with androgen receptor is essential for integrin β1 and FAK activation and cell migration induced by androgen stimulation [79]
M2 and A7 melanoma cells Filamin-A functions to stabilize cortical actin in vivo and is required for efficient cell locomotion [16]
FlnA null mouse platelets The interaction between FlnA and Syk regulates ITAM- and ITAM-like-containing receptor signaling which is essential for platelet spreading [58]
M2 melanoma cells R-Ras regulates migration through an interaction with filamin A in melanoma cells [57]
EK-293 cells Filamin A interacts with vimentin to regulation of cell adhesion to collagen through recycling beta1 integrins to cell membrane [52, 53]
Melanoma and breast cancer cells and breast cancer TMA Filamin-A deficiency in melanoma and breast cancer cells reduces not only cell motility and invasiveness, but also spontaneous and systemic metastasis in nude mouse xenograft. Decreased filamin-A expression levels in cancer cells are associated with better survival of distant metastasis-free in breast cancer patients. [116]
Literatures reported the role of filamin-A inhibiting metastasis
Human fibrosarcoma cells Filamin-A deficiency increases matrix metalloproteinase (MMP) activity and induces MMP2 activation, enhancing the ability of cells to remodel the ECM and increasing their invasive potential [108]
HT1080 and Jurkat cells Filamins play a role in cell migration and spreading through the interactions between filamins and transmembrane or signaling proteins, which is mediated at least in part by repeat 19 to 21. [117]
A7 melanoma cells Migfilin acts as a molecular switch to disconnect filamin from integrin for regulating integrin activation and dynamics of extracellular matrix-actin linkage. [71]
Hematopoietic cell ASB2 may regulate hematopoietic cell differentiation by modulating cell spreading and actin remodeling through targeting of filamins for degradation [48, 118, 119]
Chinese hamster ovary cells Tight filamin binding restricts integrin-dependent cell migration by inhibiting transient membrane protrusion and cell polarization. [105]
A7 and M2 cells Co-expression of CEACAM1-L and filamin A lead to a reduced RalA activation, focal adhesion turnover and cell migration [69]
Primary melanoma cell line Wnt5A activates calpain-1, leading to the cleavage of filamin A, which results in a remodeling of the cytoskeleton and an increase in melanoma cell motility. [120]
ErbB2 overexpressed breast cancer cells and Breast TMA Filamin-A deficiency in ErbB2-breast cancer cells reduces FAK turnover and cell motility. Down-regulation of filamin-A in stromal and base membrane is associated with breast cancer progression and invasive lymph node status [106]