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Data suggest agonist-induced signal transduction via either BAI1/ADGRB1 or GPR56 (show GPR56 Proteins)/ADGRG1 does not require conserved membrane-proximal stalk region; thus, it appears GAIN domain cleavage via autoproteolysis is not necessary for receptor activation.
BAI1 may be involved in the negative regulation of bladder transitional cell carcinoma microvascular proliferation, and its expression may be associated with a reduction in p53 (show TP53 Proteins) mutations.
Results show that lower BAI1 expression correlates with poorer patient survival, and high Nestin (show NES Proteins) expression is associated with an increased probability of metastases in breast cancer patients.
recognition of apoptotic cells by BAI1 contributes to their clearance in the human gastric mucosa and this is associated with anti-inflammatory effects
findings demonstrate that BAI1 is a synaptic receptor that can activate both the Rho and ERK (show EPHB2 Proteins) pathways, with the N-terminal and C-terminal regions of the receptor playing key roles in the regulation of BAI1 signaling activity
The results of this study indicated that BAI1 plays an important role in synaptogenesis that is mechanistically distinct from its role in phagocytosis.
Proprotein convertases, primarily furin (show FURIN Proteins), activate latent matrix metalloproteinase-14 (show MMP14 Proteins), which then directly cleaves BAI1 to release the bioactive fragment.
MBD2 (show DPEP2 Proteins) overexpression during gliomagenesis may drive tumor growth by suppressing the antiangiogenic activity of a key tumor BAI1.
brain-specific angiogenesis inhibitor 1 over-expression suppresses tumour angiogenesis
BAI1 was expressed in cerebral neurons but not astrocytes. It was localized in the cytoplasm and cell membrane. BAI1 protein may play an important role in synapse formation and signal transduction
these findings suggest that BAI1 mediates the clearance of Gram-negative bacteria by stimulating both phagocytosis and NADPH oxidase (show NOX1 Proteins) activation, thereby coupling bacterial detection to the cellular microbicidal machinery.
transgenic mice overexpressing BAI1 had fewer apoptotic cells, reduced inflammation, and attenuated disease. Boosting BAI1-mediated uptake by intestinal epithelial cells was important in attenuating inflammation.
BAI1(-) mice have deficits in hippocampus-dependent spatial learning and memory, enhanced long-term potentiation, impaired long-term depression, and postsynaptic density thinning. BAI1 stops PSD-95 (show DLG4 Proteins) polyubiquitination/degradation via interaction with MDM2 (show MDM2 Proteins).
data identify apoptotic cells as a new type of cue that induces signalling via the phosphatidylserine receptor (show JMJD6 Proteins) BAI1 to promote fusion of healthy myoblasts, with important implications for muscle development and repair
expression pattern in brain regions and role as anti-angiogenic factor (show VEGFA Proteins) in mature neuropil
findings identify BAI1 as a pattern recognition receptor that mediates nonopsonic phagocytosis of Gram-negative bacteria by macrophages and directly affects the host response to infection
BAI1 is a phosphatidylserine recognition receptor that can directly recruit a Rac (show AKT1 Proteins)-GEF (show ARHGEF2 Proteins) complex to mediate the uptake of apoptotic cells.
Angiogenesis is controlled by a local balance between stimulators and inhibitors of new vessel growth and is suppressed under normal physiologic conditions. Angiogenesis has been shown to be essential for growth and metastasis of solid tumors. In order to obtain blood supply for their growth, tumor cells are potently angiogenic and attract new vessels as results of increased secretion of inducers and decreased production of endogenous negative regulators. BAI1 contains at least one 'functional' p53-binding site within an intron, and its expression has been shown to be induced by wildtype p53. There are two other brain-specific angiogenesis inhibitor genes, designated BAI2 and BAI3 which along with BAI1 have similar tissue specificities and structures, however only BAI1 is transcriptionally regulated by p53. BAI1 is postulated to be a member of the secretin receptor family, an inhibitor of angiogenesis and a growth suppressor of glioblastomas
brain-specific angiogenesis inhibitor 1
, brain-specific angiogenesis inhibitor 1-like