Annexin I Regulates SKCO-15 Cell Invasion by Signaling through Formyl Peptide Receptors

Babbin, Brian A.; Lee, Winston Y.; Parkos, Charles A.; Winfree, Lilly; Akyildiz, Adil; Perretti, Mauro; Nusrat, Asma

doi:10.1074/jbc.m513025200

Cited by 133 publications

(149 citation statements)

References 92 publications

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“…Small interfering RNA-mediated knockdown of Anx A1 expression resulted in significant reduction of SKCO-15 colorectal adenocarcinoma cell invasion. 7 The tumor-promoting effects of Anx A1 has been attributed to its interaction with FPR members on tumor cells in a paracrine or autocrine fashion. Recently, Anx A1 has been implicated in tumor angiogenesis, as tumors transplanted into Anx A1 null mice grew Sections were prepared from peri-tumor normal tissues and tumors of glioma patients receiving surgical therapy.…”

Section: Discussionmentioning

confidence: 99%

“…Because a reported FPR1 agonist protein Anx A1 has been shown to be produced by malignant tumor cells and may increase the invasiveness of tumor cells, 7 we examined the presence of Anx A1 in NecSup by immunoblotting. Figure 1C shows that after U87 GBM cells were subjected to repeated freezing and thawing to cause necrosis, Anx A1 was released into the supernatant.…”

Section: Anx A1 In Necrotic Tumor Cell Supernatantmentioning

confidence: 99%

“…1,5 Although The content of this publication do not necessarily reflect the views or policies of the Department of Health and Human Services, nor does the mention of trade names, commercial products, or organizations imply endorsement by the U.S. Government. the first agonist identified for FPR1 was bacterial formylated peptide, there are also a number of host-derived agonists including mitochondrial formyl peptides, 6 Annexin 1 (Anx A1) 7 and a neutrophil granule protein cathepsin G. 8 Therefore, FPR1 may be involved in pathophysiological processes in which its pathogen-derived or endogenous agonists are elevated. Studies further revealed that GBM cells undergoing necrosis release chemotactic agonist(s) that activate FPR1 in viable tumor cells.…”

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confidence: 99%

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Annexin 1 Released by Necrotic Human Glioblastoma Cells Stimulates Tumor Cell Growth through the Formyl Peptide Receptor 1

Yang

Liu

Yao

et al. 2011

The American Journal of Pathology

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Highly malignant human gliomas overexpress the Gprotein-coupled chemoattractant receptor formyl peptide receptor (FPR1), which promotes tumor progression when activated. Our previous studies demonstrated that necrotic glioblastoma cells release chemotactic agonist(s) that activate FPR1 on viable tumor cells. In the present study, we identified an FPR1 agonist released by necrotic human glioblastoma cells.

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Section: Discussionmentioning

confidence: 99%

Section: Anx A1 In Necrotic Tumor Cell Supernatantmentioning

confidence: 99%

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confidence: 99%

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Annexin 1 Released by Necrotic Human Glioblastoma Cells Stimulates Tumor Cell Growth through the Formyl Peptide Receptor 1

Yang

Liu

Yao

et al. 2011

The American Journal of Pathology

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“…Furthermore, annexin A1 has been found to be overexpressed in immortalised colorectal cell lines (Guzman-Aranguez et al, 2005). This annexin has also a potential role in tumour invasion and metastasis, as inhibition of annexin A1 using siRNA resulted in a significant reduction of cell invasion using an in vitro assay on an immortalised colorectal cancer cell line (Babbin et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Characterisation and protein expression profiling of annexins in colorectal cancer

Carpenter²,

et al. 2007

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The annexins are family of calcium-regulated phospholipid-binding proteins with diverse roles in cell biology. Individual annexins have been implicated in tumour development and progression, and in this investigation a range of annexins have been studied in colorectal cancer. Annexins A1, A2, A4 and A11 were identified by comparative proteomic analysis to be overexpressed in colorectal cancer. Annexins A1, A2, A4 and A11 were further studied by immunohistochemistry with a colorectal cancer tissue microarray containing primary and metastatic colorectal cancer and also normal colon. There was significant increase in expression in annexins A1 (P ¼ 0.01), A2 (Po0.001), A4 (Po0.001) and A11 (Po0.001) in primary tumours compared with normal colon. There was increasing expression of annexins A2 (P ¼ 0.001), A4 (P ¼ 0.03) and A11 (P ¼ 0.006) with increasing tumour stage. An annexin expression profile was identified by k-means cluster analysis, and the annexin profile was associated with tumour stage (P ¼ 0.01) and also patient survival. Patients in annexin cluster group 1 (low annexin expression) had a better survival (log rank ¼ 5.33, P ¼ 0.02) than patients in cluster group 2 (high annexins A4 and A11 expression). In conclusion, this study has shown that individual annexins are present in colorectal cancer, specific annexins are overexpressed in colorectal cancer and the annexin expression profile is associated with survival.

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“…9 Therefore, we evaluated if ANXA1 could have a proinvasive role in LNCaP, DU145 and PC3 cell lines thanks to its ability to activate FPRs, as previously reported in pancreas and colon carcinomas. 18,33 We performed a matrigel invasion assay by stimulating or not LNCaP, DU145 and PC3 cells by administration of Ac2-26 peptide, the N-terminus mimetic peptide of ANXA1, of the natural FPR agonist N-FormylmethionyL-leucyL-phenylalanine (fMLP) peptide 30 and of 2 FPR antagonists, in normoxia and hypoxia conditions.…”

Section: Secretion Of Anxa1 Protein Has a Crucial Role During Hypoxiamentioning

confidence: 99%

Hypoxia regulates ANXA1 expression to support prostate cancer cell invasion and aggressiveness

Bizzarro

Belvedere

Migliaro

et al. 2016

Cell Adhesion & Migration

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Annexin A1 (ANXA1) is a Ca 2C -binding protein overexpressed in the invasive stages of prostate cancer (PCa) development; however, its role in this tumor metastatization is largely unknown. Moreover, hypoxic conditions in solid tumors have been related to poor prognosis in PCa patients. We have previously demonstrated that ANXA1 is implicated in the acquisition of chemo-resistant features in DU145 PCa cells conferring them a mesenchymal/metastatic phenotype. In this study, we have investigated the mechanisms by which ANXA1 regulates metastatic behavior in LNCaP, DU145 and PC3 cells exposed to hypoxia. ANXA1 was differentially expressed by PCa cell lines in normoxia whereas hypoxic stimuli resulted in a significant increase of protein expression. Additionally, in low oxygen conditions ANXA1 was extensively secreted out-side the cells where its binding to formyl peptide receptors (FPRs) induced cell invasion. Loss and gain of function experiments performed by using the RNA interfering siANXA1 and an ANXA1 over-expressing plasmid (MF-ANXA1), also confirmed the leading role of the protein in modulating LNCaP, DU145 and PC3 cell invasiveness. Finally, ANXA1 played a crucial role in the regulation of cytoskeletal dynamics underlying metastatization process, such as the loss of adhesion molecules and the occurrence of the epithelial to mesenchymal transition (EMT). ANXA1 expression increased inversely to epithelial markers such as E-cadherin and cytokeratins 8 and 18 (CKs) and proportionally to mesenchymal ones such as vimentin, ezrin and moesin. Our results indicated that ANXA1 may be a key mediator of hypoxia-related metastasis-associated processes in PCa.

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Annexin I Regulates SKCO-15 Cell Invasion by Signaling through Formyl Peptide Receptors

Cited by 133 publications

References 92 publications

Annexin 1 Released by Necrotic Human Glioblastoma Cells Stimulates Tumor Cell Growth through the Formyl Peptide Receptor 1

Annexin 1 Released by Necrotic Human Glioblastoma Cells Stimulates Tumor Cell Growth through the Formyl Peptide Receptor 1

Characterisation and protein expression profiling of annexins in colorectal cancer

Hypoxia regulates ANXA1 expression to support prostate cancer cell invasion and aggressiveness

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