Cloning and characterization of BAI2 and BAI3, novel genes homologous to brain-specific angiogenesis inhibitor 1 (BAI1)

Shiratsuchi, Takayuki; Nishimori, Hiroyuki; Ichise, Hirotake; Nakamura, Yusuke; Tokino, T.

doi:10.1159/000134693

Cited by 90 publications

(73 citation statements)

References 6 publications

(8 reference statements)

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“…The high affinity of this binding (K D = 1-20 nM), along with the nature of C1ql proteins as small secreted proteins and of BAI3 as a membrane-bound GPCR, suggest that BAI3 is a genuine receptor for C1ql proteins in the brain. Both C1ql and BAI3 proteins are expressed in adult animals almost exclusively in the brain and appear to be enriched in neurons (11,12,31). Strikingly, the addition of the recombinant gC1q domains of C1ql proteins to the medium of cultured hippocampal neurons caused significant decreases in synapse density without affecting other measured morphological parameters (Figs.…”

Section: Discussionmentioning

confidence: 93%

“…The extracellular sequences of BAI proteins are composed of an N-terminal CUB domain, five (BAI1) or four (BAI2 and BAI3) thrombospondin type 1 repeats, a hormonebinding domain, and the GPS (10,11). RNA quantification and in situ hybridization have indicated that in adult mice, BAI proteins are expressed primarily in the brain, with low-level expression in other tissues (12)(13)(14)(15).…”

mentioning

confidence: 99%

“…The antiangiogenic activity of BAI1 is thought to be mediated by a fragment of its N-terminal extracellular sequence, a fragment known as vasculostatin (17,23,24). BAI2 and BAI3 expression are not p53-inducible, but both proteins also act as inhibitors of angiogenesis (11,14,15,25). Moreover, BAI1 functions as a surface receptor for phosphatidylserine that is exposed on the surface of apoptotic cells, suggesting that BAI1 is an engulfment receptor that can initiate phagocytosis (26).…”

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confidence: 99%

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The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

Bolliger¹,

Martinelli²,

Südhof

2011

Proc. Natl. Acad. Sci. U.S.A.

155

168

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C1q-like genes (C1ql1-C1ql4) encode small, secreted proteins that are expressed in differential patterns in the brain but whose receptors and functions remain unknown. BAI3 protein, in contrast, is a member of the cell-adhesion class of G protein-coupled receptors that are expressed at high levels in the brain but whose ligands have thus far escaped identification. Using a biochemical approach, we show that all four C1ql proteins bind to the extracellular thrombospondin-repeat domain of BAI3 with high affinity, and that this binding is mediated by the globular C1q domains of the C1ql proteins. Moreover, we demonstrate that addition of submicromolar concentrations of C1ql proteins to cultured neurons causes a significant decrease in synapse density, and that this decrease was prevented by simultaneous addition of the thrombospondin-repeat fragment of BAI3, which binds to C1ql proteins. Our data suggest that C1ql proteins are secreted signaling molecules that bind to BAI3 and act, at least in part, to regulate synapse formation and/or maintenance.

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Section: Discussionmentioning

confidence: 93%

mentioning

confidence: 99%

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confidence: 99%

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The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

Bolliger¹,

Martinelli²,

Südhof

2011

Proc. Natl. Acad. Sci. U.S.A.

155

168

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“…The recently discovered brain-specific angiogenesis inhibitor family was implicated in tumor angiogenesis regulation; brain-specific angiogenesis inhibitor-1 expression is regulated by p53 (16,17). Finally, in the COOH terminus of p120 immediately adjacent to the putative site of CIRL proteolysis a novel structural motif is found that is characteristic for about a dozen large orphan GPCRs of the secretin receptor family (GenBank numbers U39848, U76764, P48960, Q61549, Q14246, AC004262, D87469, AB011529, AB011528, AB011536, AB005297, X81892, AB005298, AF006014, AB011122).…”

Section: Domainmentioning

confidence: 99%

Structural Requirements for α-Latrotoxin Binding and α-Latrotoxin-stimulated Secretion

Krasnoperov¹,

Bittner²,

Holz³

et al. 1999

Journal of Biological Chemistry

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Stimulation of neurotransmitter release by ␣-latrotoxin requires its binding to the calcium-independent receptor of ␣-latrotoxin (CIRL), an orphan neuronal G protein-coupled receptor. CIRL consists of two noncovalently bound subunits, p85, a heptahelical integral membrane protein, and p120, a large extracellular polypeptide with domains homologous to lectin, olfactomedin, mucin, the secretin receptor family, and a novel structural motif common for large orphan G proteincoupled receptors. The analysis of CIRL deletion mutants indicates that the high affinity ␣-latrotoxin-binding site is located within residues 467-891, which comprise the first transmembrane segment of p85 and the C-terminal half of p120. The N-terminal lectin, olfactomedin, and mucin domains of p120 are not required for the interaction with ␣-latrotoxin. Soluble p120 and all its fragments, which include the 467-770 residues, bind ␣-latrotoxin with low affinity suggesting the importance of membrane-embedded p85 for the stabilization of the complex of the toxin with p120. Two COOH-terminal deletion mutants of CIRL, one with the truncated cytoplasmic domain and the other with only one transmembrane segment left of seven, supported both ␣-latrotoxin-induced calcium uptake in HEK293 cells and ␣-latrotoxin-stimulated secretion when expressed in chromaffin cells, although with a different dose dependence than wild-type CIRL and its N-terminal deletion mutant. Thus the signaling domains of CIRL are not critically important for the stimulation of exocytosis in intact chromaffin cells by ␣-latrotoxin.

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“…BAI1 has been isolated and characterized by Nishimori and co-workers as a gene that is transactivated by p53. It has been proposed to be a member of a novel family of seven-span transmembrane receptors that also includes BAI2 and BAI3, cloned and described by Shiratsuchi et al (1997). The extracellular region of BAI1 uniquely encompasses five thrombospondin type I repeats and also one RGD (Arg-Gly-Asp) motif, which can be recognized by integrins.…”

mentioning

confidence: 99%

Overexpression of the p53-inducible brain-specific angiogenesis inhibitor 1 suppresses efficiently tumour angiogenesis

et al. 2002

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The brain-specific angiogenesis inhibitor 1 gene has been isolated in an attempt to find fragments with p53 functional binding sites. As reported herein and by others, brain-specific angiogenesis inhibitor 1 expression is present in some normal tissues, but is reduced or lost in tumour tissues. Such data and its particular structure prompted the hypothesis that brain-specific angiogenesis inhibitor 1 may act as a mediator in the local angiogenesis balance. We herein demonstrate that brain-specific angiogenesis inhibitor 1 over-expression suppresses tumour angiogenesis, delaying significantly the human tumour growth in immunodeficient mice. The inhibitory effect of brain-specific angiogenesis inhibitor 1 was documented using our intravital microscopy system, strongly implicating brain-specific angiogenesis inhibitor 1 as a mediator in the control of tumour angiogenesis. In contrast, in vitro tumour cell proliferation was not inhibited by brain-specific angiogenesis inhibitor 1 transfection, whereas some level of cytotoxicity was assessed for endothelial cells. Immunohistochemical analysis of tumour samples confirmed a reduction in the microvessel density index in brain-specific angiogenesis inhibitor 1-overexpressing tumours. At messenger level, moderate changes could be detected, involving the down-regulation of vascular endothelial growth factor and collagenase-1 expression. Furthermore, brain-specific angiogenesis inhibitor 1 expression that was lost in a selection of human cancer cell lines could be restored by wild-type p53 adenoviral transfection. Brain-specific angiogenesis inhibitor 1 should be considered for gene therapy and development of efficient drugs based on endogenous antiangiogenic molecules.

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Cloning and characterization of BAI2 and BAI3, novel genes homologous to brain-specific angiogenesis inhibitor 1 (BAI1)

Cited by 90 publications

References 6 publications

The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins

Structural Requirements for α-Latrotoxin Binding and α-Latrotoxin-stimulated Secretion

Overexpression of the p53-inducible brain-specific angiogenesis inhibitor 1 suppresses efficiently tumour angiogenesis

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