Serum amyloid A stimulates matrix-metalloproteinase-9 upregulation via formyl peptide receptor like-1-mediated signaling in human monocytic cells

Lee, Ha Young; Kim, Mi-Kyoung; Park, Kyoung Sun; Bae, Yun Hee; Yun, Jeanho; Park, Joo-In; Kwak, Jong‐Young; Bae, Yoe‐Sik

doi:10.1016/j.bbrc.2005.03.069

Cited by 124 publications

(110 citation statements)

References 39 publications

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“…Furthermore, SAA may modulate adhesion of tumor cells to platelets and enhance plasminogen activation, both of which are involved in ECM degradation and tissue remodeling processes. Indeed, another important approach to SAA influencing ECM, has been verified by an increasing number of studies, is that it can stimulate the production of MMPs (Stix et al, 2001;Lee et al, 2005). This partially explains the value of SAA level as a monitor of metastatic dissemination in several solid tumor and the relationship with prognosis.…”

Section: Discussionmentioning

confidence: 92%

Serum Amyloid A is a Novel Prognostic Biomarker in Hepatocellular Carcinoma

Ni¹,

Ye²,

Fu³

et al. 2015

Asian Pacific Journal of Cancer Prevention

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Purpose: To investigate the prognostic value of serum amyloid A (SAA) in patients with hepatocellular carcinoma (HCC) undergoing surgery. Materials and Methods: Preoperative serum samples of 328 patients with HCC who underwent curative resection and of 47 patients with benign liver lesion were assayed. Serum levels of SAA were measured by enzyme-linked immunosorbent assay and its correlations with clinicopathological characteristics and survival were explored. Results: Levels of SAA were significantly higher in patients with HCC than those with benign liver lesion. There were strong correlations between preoperative serum SAA level and tumor size and more advanced BCLC stage. On univariate analysis, elevated SAA was associated with reduced disease-free survival and overall survival (p=0.001 and 0.03, respectively). Multivariate analyses showed that serum SAA level was an independent prognostic factor for overall survival (hazard ratio 2.80, p=0.01). Conclusions: High SAA serum level is a novel biomarker for the prognosis of HCC patients.

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Section: Discussionmentioning

confidence: 92%

Serum Amyloid A is a Novel Prognostic Biomarker in Hepatocellular Carcinoma

Ni¹,

Ye²,

Fu³

et al. 2015

Asian Pacific Journal of Cancer Prevention

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“…Previous studies have shown that many SAA-induced signals are inhibited by PTX, suggesting that PTX-sensitive G i -proteins are involved with SAA-induced signaling (Badolato et al, 1995;Lee et al, 2005;Zhao et al, 2007;Bjorkman et al, 2008). SAA has been reported to stimulate chemotactic migration of some leukocytic cells in a PTX-sensitive manner (Lee et al, 2005;Zhao et al, 2007;Bjorkman et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated CCL2 production

et al. 2010

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“…The capacity to mediate MMP production may be a common feature for chemoattractant GPCRs. For instance, an FPR variant receptor, FPRL1, in monocytic cells (Lee et al, 2005) and a chemokine GPCR CXCR3 in colon cancer cells have also been shown to up-regulate MMP9 (Zipin-Roitman et al, 2007). Thus, GPCRs have an important function in increasing the proteolytic processes favouring leucocyte infiltration of tissues and tumour dissemination.…”

Section: Discussionmentioning

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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Serum amyloid A stimulates matrix-metalloproteinase-9 upregulation via formyl peptide receptor like-1-mediated signaling in human monocytic cells

Cited by 124 publications

References 39 publications

Serum Amyloid A is a Novel Prognostic Biomarker in Hepatocellular Carcinoma

Serum Amyloid A is a Novel Prognostic Biomarker in Hepatocellular Carcinoma

A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated CCL2 production

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

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