scholarly journals Mesoglycan connects Syndecan‐4 and VEGFR2 through Annexin A1 and formyl peptide receptors to promote angiogenesis in vitro

FEBS Journal ◽  
2021 ◽  
Author(s):  
Emanuela Pessolano ◽  
Raffaella Belvedere ◽  
Nunzia Novizio ◽  
Amelia Filippelli ◽  
Mauro Perretti ◽  
...  
Keyword(s):  
Annexin A1 ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide

scholarly journals Annexin A1 Released in Extracellular Vesicles by Pancreatic Cancer Cells Activates Components of the Tumor Microenvironment, through Interaction with the Formyl-Peptide Receptors

Cells ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 2719
Author(s):  
Nunzia Novizio ◽  
Raffaella Belvedere ◽  
Emanuela Pessolano ◽  
Alessandra Tosco ◽  
Amalia Porta ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Tumor Microenvironment ◽  
Extracellular Vesicles ◽  
Soluble Form ◽  
Annexin A1 ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Pancreatic Cancer Cells ◽  
Formyl Peptide

Pancreatic cancer (PC) is one of the most aggressive cancers in the world. Several extracellular factors are involved in its development and metastasis to distant organs. In PC, the protein Annexin A1 (ANXA1) appears to be overexpressed and may be identified as an oncogenic factor, also because it is a component in tumor-deriving extracellular vesicles (EVs). Indeed, these microvesicles are known to nourish the tumor microenvironment. Once we evaluated the autocrine role of ANXA1-containing EVs on PC MIA PaCa-2 cells and their pro-angiogenic action, we investigated the ANXA1 paracrine effect on stromal cells like fibroblasts and endothelial ones. Concerning the analysis of fibroblasts, cell migration/invasion, cytoskeleton remodeling, and the different expression of specific protein markers, all features of the cell switching into myofibroblasts, were assessed after administration of wild type more than ANXA1 Knock-Out EVs. Interestingly, we demonstrated a mechanism by which the ANXA1-EVs complex can stimulate the activation of formyl peptide receptors (FPRs), triggering mesenchymal switches and cell motility on both fibroblasts and endothelial cells. Therefore, we highlighted the importance of ANXA1/EVs-FPR axes in PC progression as a vehicle of intercommunication tumor cells-stroma, suggesting a specific potential prognostic/diagnostic role of ANXA1, whether in soluble form or even if EVs are captured in PC.

scholarly journals Formyl peptide receptors and the regulation of ACTH secretion: targets for annexin A1, lipoxins, and bacterial peptides

2007 ◽  
Vol 21 (4) ◽  
pp. 1037-1046 ◽  
Author(s):  
C. D. John ◽  
V. Sahni ◽  
D. Mehet ◽  
J. F. Morris ◽  
H. C. Christian ◽  
...  
Keyword(s):  
Annexin A1 ◽  
Acth Secretion ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide

Annexin A1 localization and its relevance to cancer

2016 ◽  
Vol 130 (4) ◽  
pp. 205-220 ◽  
Author(s):  
Zied Boudhraa ◽  
Bernadette Bouchon ◽  
Claire Viallard ◽  
Michel D'Incan ◽  
Françoise Degoul
Keyword(s):  
Cancer Progression ◽  
Formyl Peptide Receptor ◽  
Annexin A1 ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Cell Compartments ◽  
Oncogenic Pathways ◽  
Formyl Peptide ◽  
Cell Processes ◽  
Inflammation Resolution

Annexin A1 (ANXA1) is a Ca2+-regulated phospholipid-binding protein involved in various cell processes. ANXA1 was initially widely studied in inflammation resolution, but its overexpression was later reported in a large number of cancers. Further in-depth investigations have revealed that this protein could have many roles in cancer progression and act at different levels (from cancer initiation to metastasis). This is partly due to the location of ANXA1 in different cell compartments. ANXA1 can be nuclear, cytoplasmic and/or membrane associated. This last location allows ANXA1 to be proteolytically cleaved and/or to become accessible to its cognate partners, the formyl-peptide receptors. Indeed, in some cancers, ANXA1 is found at the cell surface, where it stimulates formyl-peptide receptors to trigger oncogenic pathways. In the present review, we look at the different locations of ANXA1 and their association with the deregulated pathways often observed in cancers. We have specifically detailed the non-classic pathways of ANXA1 externalization, the significance of its cleavage and the role of the ANXA1–formyl-peptide receptor complex in cancer progression.

scholarly journals Annexin A1 Induces Skeletal Muscle Cell Migration Acting through Formyl Peptide Receptors

PLoS ONE ◽  
2012 ◽  
Vol 7 (10) ◽  
pp. e48246 ◽  
Author(s):  
Valentina Bizzarro ◽  
Raffaella Belvedere ◽  
Fabrizio Dal Piaz ◽  
Luca Parente ◽  
Antonello Petrella
Keyword(s):  
Skeletal Muscle ◽  
Cell Migration ◽  
Muscle Cell ◽  
Skeletal Muscle Cell ◽  
Annexin A1 ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide

scholarly journals Formyl Peptide Receptors and Annexin A1: Complementary Mechanisms to Infliximab in Murine Experimental Colitis and Crohn’s Disease

2021 ◽  
Vol 12 ◽  
Author(s):  
Marina de Paula-Silva ◽  
Gustavo Henrique Oliveira da Rocha ◽  
Milena Fronza Broering ◽  
Maria Luíza Queiroz ◽  
Silvana Sandri ◽  
...  
Keyword(s):  
Inflammatory Bowel Disease ◽  
Crohn’S Disease ◽  
Crohn's Disease ◽  
Bowel Disease ◽  
Formyl Peptide Receptor ◽  
Annexin A1 ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide ◽  
Inflammatory Bowel

Non-responsiveness to anti-TNF-α therapies presents relevant rates in inflammatory bowel disease patients, presenting the need to find biomarkers involved in therapeutic efficacy. Herein, we demonstrate that higher levels of colonic formyl peptide receptor 1 and annexin A1 correlate with histological recovery in Crohn’s disease patients under remission. Using the dextran sulfate sodium colitis model in mice, we suggest that infliximab induces annexin A1 expression and secretion in activated intestinal leukocytes. Conversely, this mechanism might stimulate epithelial formyl peptide receptors, inducing wound healing and consequent histological remission. Our data indicate that assessing intestinal expressions of formyl peptide receptors and annexin A1 might provide precious information on the disease activity and responsiveness to infliximab in inflammatory bowel disease patients.

scholarly journals Caulerpin Mitigates Helicobacter pylori-Induced Inflammation via Formyl Peptide Receptors

2021 ◽  
Vol 22 (23) ◽  
pp. 13154
Author(s):  
Paola Cuomo ◽  
Chiara Medaglia ◽  
Ivana Allocca ◽  
Angela Michela Immacolata Montone ◽  
Fabrizia Guerra ◽  
...  
Keyword(s):  
Immune Response ◽  
Helicobacter Pylori ◽  
Indole Alkaloid ◽  
G Protein Coupled Receptors ◽  
Innate Immune ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide ◽  
G Protein Coupled

The identification of novel strategies to control Helicobacter pylori (Hp)-associated chronic inflammation is, at present, a considerable challenge. Here, we attempt to combat this issue by modulating the innate immune response, targeting formyl peptide receptors (FPRs), G-protein coupled receptors that play key roles in both the regulation and the resolution of the innate inflammatory response. Specifically, we investigated, in vitro, whether Caulerpin—a bis-indole alkaloid isolated from algae of the genus Caulerpa—could act as a molecular antagonist scaffold of FPRs. We showed that Caulerpin significantly reduces the immune response against Hp culture filtrate, by reverting the FPR2-related signaling cascade and thus counteracting the inflammatory reaction triggered by Hp peptide Hp(2–20). Our study suggests Caulerpin to be a promising therapeutic or adjuvant agent for the attenuation of inflammation triggered by Hp infection, as well as its related adverse clinical outcomes.

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