作者: Laura Simone , Francesco Pisani , Maria G. Mola , Manuela De Bellis , Giuseppe Merla
DOI: 10.1158/0008-5472.CAN-18-2015
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摘要: The glial water channel protein aquaporin-4 (AQP4) forms heterotetramers in the plasma membrane made of M23-AQP4 and M1-AQP4 isoforms. isoform ratio controls AQP4 aggregation into supramolecular structures called orthogonal arrays particles (AQP4-OAP). role OAP malignant gliomas is still unclear. In this study, we demonstrate that aggregation/disaggregation influences biology glioma cells. Selective expression OAP-forming (AQP4-OAP) triggered cell shape changes cells associated with alterations to F-actin cytoskeleton affected apoptosis. By contrast, (AQP4-tetramers), which unable aggregate OAP, ameliorated invasiveness, improved migration, increased methalloproteinase-9 activity. Two prolines (254 296) at C-terminus tail were shown be important mediating relationship between actin AQP4-OAP AQP4-tetramers. conclusion, study demonstrates state might an determinant orienting persist or perish. disaggregation may potentiate invasiveness potential, whereas activate apoptotic path. This shows a new perspective on brain tumors not necessarily edema formation but dynamics their link cytoskeleton. SIGNIFICANCE: how alter proliferation, potential