Expression of functional formyl peptide receptors by human astrocytoma cell lines

Le, Yingying; Hu, Jinyue; Gong, Wanghua; Shen, Weiping; Li, Baoqun; Dunlop, Nancy M.; Halverson, David; Blair, Donald G.; Wang, Ji Ming

doi:10.1016/s0165-5728(00)00373-8

Cited by 81 publications

(71 citation statements)

References 29 publications

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“…Thus, by activating FPR family members, annexin A1 can serve as an important regulator of leukocyte migration and as an endogenous anti-inflammatory protein. Moreover, since FPR is not restricted to leukocytes, the annexin-A1-FPR interaction might also regulate the migratory behavior of other cells expressing FPR/FPRLs, such as dendritic cells, hepatocytes, astrocytes and alveolar type II cells (McCoy et al, 1995;Sozzani et al, 1998;Le et al, 2000;Rescher et al, 2002).…”

Section: The Ultimate Puzzle: Extracellular Annexin Activitiesmentioning

confidence: 99%

Annexins – unique membrane binding proteins with diverse functions

Rescher

Gerke

2004

Journal of Cell Science

540

435

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IntroductionThe annexins are a family of Ca 2+ /lipid-binding proteins that differ from most other Ca 2+ -binding proteins in their Ca 2+ -binding sites. These have a unique architecture that allows them to dock onto membranes in a peripheral and reversible manner. The conserved Ca 2+ -and membrane-binding module is the annexin core domain, which consists of four so-called annexin repeats, each of which is 70 residues in length. It is highly α-helical and forms a compact, slightly curved disc that has a convex surface harboring the Ca 2+ -and membranebinding sites and a concave side that points away from the membrane and is thereby available for other types of interaction/regulation (Fig. 1). The N-terminal region precedes the core domain and is diverse in sequence and length. It mediates regulatory interactions with protein ligands and regulates the annexin-membrane association (reviewed by Gerke and Moss, 2002;Raynal and Pollard, 1994). Although the N-terminal domain has long been considered a separately folded entity, recent crystal structures reveal that, at least in annexin A1, part of it can integrate into the folded core. Ca 2+ (and probably membrane) binding can then trigger exposure of the N-terminal region, making it available for additional interactions/activities ( Fig. 1) (Rosengarth and Luecke, 2003). The activity of the exposed N-terminal region could thus be tightly controlled through Ca 2+ /membrane binding.The annexin family comprises >500 different gene products expressed in most phyla and species (reviewed by Morgan and Fernandez, 1997). In vertebrates, 12 annexin subfamilies (A1-A11 and A13), which have different splice variants, have been identified. These have different N-terminal domains and differently positioned Ca 2+ /membrane-binding sites within the core domain. Analyses of the biochemical properties and subcellular localizations of annexins, and later studies of the effects of anti-annexin antibodies and annexin mutants, mainly in permeabilized cell systems, have allowed several potential physiological functions to be assigned to different annexins. Most of these take into account their regulated binding to membranes and a scaffold role at certain membrane domains is a common theme.Proposed to act as membrane-membrane or membranecytoskeleton linkers, annexins have been implicated in Ca 2+ -regulated exocytotic events, certain aspects of endocytosis and stabilization of specific domains of organelle membranes and the plasma membrane. However, other potential functions have been put forward -for example, those taking into account the RNA-binding capacity of some annexins (Filipenko et al., 2004;Vedeler and Hollas, 2000), their regulated nuclear localization (Eberhard et al., 2001;Mizutani et al., 1992;Tomas and Moss, 2003) or specific nucleotide-binding activities (Banderowicz-Pikula et al., 2001; Caohuy et al., 1996). Because some annexins occur extracellularly, they might also function outside the cell, although their (direct or indirect) secretion is not well understood. Detailed ...

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Section: The Ultimate Puzzle: Extracellular Annexin Activitiesmentioning

confidence: 99%

Annexins – unique membrane binding proteins with diverse functions

Rescher

Gerke

2004

Journal of Cell Science

540

435

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“…Assays for tumour cell chemotaxis (Le et al, 2000;Zhou et al, 2005), Ca 2 þ mobilisation and immunoblotting were performed according to the described procedures (Le et al, 2000;Zhou et al, 2005).…”

Section: Chemotaxis Ca 2 þ Flux and Immunoblottingmentioning

confidence: 99%

The G-protein-coupled formylpeptide receptor FPR confers a more invasive phenotype on human glioblastoma cells

Huang

Chen

et al. 2010

Br J Cancer

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BACKGROUND: The G-protein-coupled formylpeptide receptor (FPR) that mediates chemotaxis of phagocytic leucocytes induced by bacterial and host-derived chemotactic peptides is selectively expressed by highly malignant human gliomas and contributes to tumour growth and angiogenesis. As invasion of surrounding normal tissues is one of the important features of tumour malignancy, we investigated the function of FPR in the invasive behaviour of human glioblastoma cells. METHODS: Cells (FPR þ and FPR À ) were isolated by single-cell cloning from a human glioblastoma cell line U-87MG. The FPR expression was assayed by flow cytometry and reverse transcription PCR. The function of FPR was investigated by chemotaxis and calcium flux induced by FPR agonist fMLF. Tumour cell motility was assayed by a wound-healing model in vitro. The growth and invasive phenotype were observed with subcutaneous implantation of tumour cells in nude mice. Over-expression of FPR in FPR À cells was performed by transfection of a plasmid vector-containing human FPR gene. RESULTS: One of the glioma clones F9 that expressed high level of FPR showed a more 'motile' phenotype in vitro as compared with a clone G3 without FPR expression. Although F9 and G3 clones both formed subcutaneous tumours in nude mice, only F9 tumours invaded surrounding mouse connective tissues. Over-expression of FPR in G3 clone (G3F) increased the cell motility in vitro and the capacity of the cells to form more rapidly growing and invasive tumours in nude mice. We further found that, in addition to supernatant of necrotic tumour cells, foetal calf serum and human serum used in culture media contained FPR agonist activity and increased the motility of FPR-expressing glioblastoma cells. CONCLUSION: The expression of FPR is responsible for increased motility of human glioblastoma cells and their formation of highly invasive tumours.

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“…FPRL1 is one of the classic chemoattractant receptors encompassing G protein-coupled seven transmembrane domains. Previous reports have pointed to a role for FPRL1 in the regulation of a variety of cellular responses in several cell types, including astrocytoma cell lines (24), neutrophils, monocytes, and T cells (25), as well as HUVECs (26). Recently, O'Hara et al (27) showed that overexpressed SAA and FPRL1 in inflamed synovial tissue can be associated with the production of matrix metalloproteinase.…”

Section: R Heumatoid Arthritis (Ra)mentioning

confidence: 99%

Serum Amyloid A Binding to Formyl Peptide Receptor-Like 1 Induces Synovial Hyperplasia and Angiogenesis

Lee

Yoo

Cho

et al. 2006

The Journal of Immunology

123

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Serum amyloid A (SAA) is a major acute-phase reactant, and has been demonstrated to mediate proinflammatory cellular responses. Although SAA has been used as an indicator for a variety of inflammatory diseases, the role of SAA in synovial hyperplasia and proliferation of endothelial cells, a pathological hallmark of rheumatoid arthritis (RA), has yet to be elucidated. In this study, we have demonstrated that SAA promotes the proliferation of human fibroblast-like synoviocytes (FLS). In addition, SAA protects RA FLS against the apoptotic death induced by serum starvation, anti-Fas IgM, and sodium nitroprusside. The activity of SAA appears to be mediated by the formyl peptide receptor-like 1 (FPRL1) receptor, as it was mimicked by the WKYMVm peptide, a specific ligand for FPRL1, but completely abrogated by down-regulating the FPRL1 transcripts with short interfering RNA. The effect of SAA on FLS hyperplasia was shown to be caused by an increase in the levels of intracellular calcium, as well as the activation of ERK and Akt, which resulted in an elevation in the expression of cyclin D1 and Bcl-2. Moreover, SAA stimulated the proliferation, migration, and tube formation of endothelial cells in vitro, and enhanced the sprouting activity of endothelial cells ex vivo and neovascularization in vivo. These observations indicate that the binding of SAA to FPRL1 may contribute to the destruction of bone and cartilage via the promotion of synoviocyte hyperplasia and angiogenesis, thus providing a potential target for the control of RA.

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Expression of functional formyl peptide receptors by human astrocytoma cell lines

Cited by 81 publications

References 29 publications

Annexins – unique membrane binding proteins with diverse functions

Annexins – unique membrane binding proteins with diverse functions

The G-protein-coupled formylpeptide receptor FPR confers a more invasive phenotype on human glioblastoma cells

Serum Amyloid A Binding to Formyl Peptide Receptor-Like 1 Induces Synovial Hyperplasia and Angiogenesis

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