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Annexin A2-dependent extracellular vesicle proteome modulates pre-metastatic stromal fibroblast behavior in triple-negative breast cancer

ABSTRACT: Proteomic profiling of AnxA2-enriched extracellular vesicles from MDA-MB-4175 triple-negative breast cancer cells

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Andrew Lemoff

LAB HEAD: Jamboor Vishwanatha

PROVIDER: PXD067600 | Pride | 2026-03-02

REPOSITORIES: pride

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			Action	DRS
	ECL1_1253144.mgf	Mgf
	ECL1_1253144_F.msf	Msf
	ECL1_1253144_F1.raw	Raw
	ECL1_1253144_F2.raw	Raw
	ECL1_1253144_F3.raw	Raw

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1 - 5 of 11

Publications

Annexin A2-dependent extracellular vesicle proteome modulates pre-metastatic stromal fibroblast behavior in triple-negative breast cancer.

Trivedi Rucha R Ranade Payal P Vishwanatha Jamboor K JK

Cell communication and signaling : CCS 20260131

<h4>Background</h4>Triple-negative breast cancer (TNBC) is an aggressive subclass of breast cancer with limited treatment options and a strong tendency to metastasize to the lung. Tumor-derived extracellular vesicles (EVs) are key mediators of stromal reprogramming in the pre-metastatic niche. Annexin A2 (AnxA2) is overexpressed in TNBC and linked to signal transduction, cytoskeletal remodeling, and poor prognosis, but its role in shaping EV cargo composition and consequent stromal behavior rema ...[more]

PMID: 41620716

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Role of annexin A2 in muscle repair

Project description:Repair of injured muscle involves repair of injured myofibers through the involvement of dysferlin and its interacting partners, including annexin. Studies with mice and patients have established that dysferlin deficit leads to chronic inflammation and adipogenic replacement of the diseased muscle. However, longitudinal analysis of annexin deficit on muscle pathology and function is lacking. Here we show that unlike annexin A1, but similar to dysferlin, lack of annexin A2 (AnxA2) causes poor myofiber repair and progressive weakening with age. However, unlike dysferlin-deficient muscle, AnxA2-deficient muscles do not exhibit chronic inflammation or adipogenic replacement. Deletion of AnxA2 in dysferlin deficient mice reduces inflammation, adipogenic replacement, and loss in muscle function caused by dysferlin deficit. These results show that: a) AnxA2 facilitates myofiber repair, b) chronic inflammation and adipogenic replacement of dysferlinopathic muscle requires AnxA2, and c) inhibiting AnxA2-mediated inflammation is a novel therapeutic avenue for dysferlinopathy.

2016-10-04 | GSE87557 | GEO

Characterization of Primary Patient B-cells under Various Stimulation Conditions

Project description:The goal of this project was to compare the effects of differential stimulation of primary patient B-cells with CD40L, CpG, anti-IgM, and IL4 individually and in combination. Additionally, we observed a phenomenon where anti-IgM+CpG treatment resulted in a lymphoma-like phenotype and sought to compare this treatment regimen to the lymphoma cell line HBL-1.

2025-08-21 | PXD016961 | Pride

Genotoxic agents promote the nuclear accumulation of annexin A2: role of annexin A2 in mitigating DNA damage.

Project description:Annexin A2 is an abundant cellular protein that is mainly localized in the cytoplasm and plasma membrane, however a small population has been found in the nucleus, suggesting a nuclear function for the protein. Annexin A2 possesses a nuclear export sequence (NES) and inhibition of the NES is sufficient to cause nuclear accumulation. Here we show that annexin A2 accumulates in the nucleus in response to genotoxic agents including gamma-radiation, UV radiation, etoposide and chromium VI and that this event is mediated by the nuclear export sequence of annexin A2. Nuclear accumulation of annexin A2 is blocked by the antioxidant agent N-acetyl cysteine (NAC) and stimulated by hydrogen peroxide (H₂O₂), suggesting that this is a reactive oxygen species dependent event. In response to genotoxic agents, cells depleted of annexin A2 show enhanced phospho-histone H2AX and p53 levels, increased numbers of p53-binding protein 1 nuclear foci and increased levels of nuclear 8-oxo-2'-deoxyguanine, suggesting that annexin A2 plays a role in protecting DNA from damage. This is the first report showing the nuclear translocation of annexin A2 in response to genotoxic agents and its role in mitigating DNA damage.

| S-EPMC3511559 | biostudies-literature

Membrane Binding Promotes Annexin A2 Oligomerization.

Project description:Annexin A2 (AnxA2) is a cytosolic Ca2+ regulated membrane binding protein that can induce lipid domain formation and plays a role in exocytosis and endocytosis. To better understand the mode of annexin-membrane interaction, we analyzed membrane-bound AnxA2 assemblies by employing a novel 3-armed chemical crosslinker and specific AnxA2 mutant proteins. Our data show that AnxA2 forms crosslinkable oligomers upon binding to membranes containing negatively charged phospholipids. AnxA2 mutants with amino acid substitutions in residues predicted to be involved in lateral protein-protein interaction show compromised oligomer formation, albeit still being capable of binding to negatively charged membranes in the presence of Ca2+. These results suggest that lateral protein-protein interactions are involved in the formation of AnxA2 clusters on a biological membrane.

| S-EPMC7291239 | biostudies-literature

Bridging of membrane surfaces by annexin A2.

Project description:The protein-mediated formation of membrane contacts is a crucial event in many cellular processes ranging from the establishment of organelle contacts to the docking of vesicles to a target membrane. Annexins are Ca2+ regulated membrane-binding proteins implicated in providing such membrane contacts; however, the molecular basis of membrane bridging by annexins is not fully understood. We addressed this central question using annexin A2 (AnxA2) that functions in secretory vesicle exocytosis possibly by providing membrane bridges. By quantitatively analyzing membrane contact formation using a novel assay based on quartz crystal microbalance recordings, we show that monomeric AnxA2 can bridge membrane surfaces Ca2+ dependently. However, this activity depends on an oxidative crosslink involving a cysteine residue in the N-terminal domain and thus formation of disulfide-linked dimers. Alkylated AnxA2 in which this cysteine residue has been modified and AnxA2 mutants lacking the N-terminal domain are not capable of bridging membrane surfaces. In contrast, a heterotetrameric complex comprising two membrane binding AnxA2 subunits linked by a S100A10 dimer can provide membrane contacts irrespective of oxidation status. Thus, monomeric AnxA2 only contains one lipid binding site and AnxA2-mediated linking of membrane surfaces under non-oxidative intracellular conditions most likely requires AnxA2-S100 complex formation.

| S-EPMC6168566 | biostudies-literature

HEK293T cell degradome (pulse chase) time course (5h, 10, 15h) analysis upon Torin1 treatment. Related to Supplementary Table 3 from An et al (2020)

Project description:HEK293T Azidohomoalanine (AHA) Pulse Chase (degradome) time course experiment, were cells from various genetic background (WT, ATG7-/-, RB1CC1-/-) are treated or not with Torin1 for 5h, 10h or 15h. Samples are Biotin-click, and streptavidin enriched, digested and labeled with TMTpro 16plex.

2020-04-30 | PXD018158 | Pride

Role of the long non‑coding RNA‑Annexin A2 pseudogene 3/Annexin A2 signaling pathway in biliary atresia‑associated hepatic injury.

Project description:Biliary atresia (BA) is the most common cause of chronic cholestasis in children. The long non‑coding RNA (lncRNA) Annexin A2 pseudogene 3 (ANXA2P3) and Annexin A2 (ANXA2) have been suggested to serve pivotal roles in BA; however, the clinical significance and biological roles of ANXA2P3 and ANXA2 in BA remain to be elucidated. The present study aimed to elucidate the function of ANAX2P3 and ANXA2 in BA‑induced liver injury using a human liver cell line and liver tissues from patients with BA. Reverse transcription‑quantitative polymerase chain reaction, western blotting and immunohistochemistry were conducted to determine the expression levels of ANXA2 and ANXA2P3 in liver tissues from patients with BA. Classification of fibrosis was analyzed by Masson staining. The functional roles of ANXA2 and ANXA2P3 in liver cells were determined by Cell Counting kit‑8 assay, and flow cytometric and cell cycle analyses. Activation of the ANXA2/ANXA2P3 signaling pathway in liver cells was evaluated by western blot analysis. According to the present results, the expression levels of ANXA2 and ANXA2P3 were significantly increased in liver tissues from patients with BA. In addition, knocking down the expression of ANXA2P3 and ANXA2 may result in reduced liver cell proliferation, cell cycle arrest in G1 phase and increased apoptosis of liver cells in vitro. Furthermore, in cells in which ANXA2 and ANXA2P3 were overexpressed, cell apoptosis was reduced and cell cycle arrest in G2 phase. Taken together, these results indicated that ANXA2P3 and ANXA2 may have protective effects against liver injury progression and may be considered biomarkers in patients with BA.

| S-EPMC6317672 | biostudies-literature

Annexin A2 facilitates endocytic trafficking of antisense oligonucleotides.

Project description:Chemically modified antisense oligonucleotides (ASOs) designed to mediate site-specific cleavage of RNA by RNase H1 are used as research tools and as therapeutics. ASOs modified with phosphorothioate (PS) linkages enter cells via endocytotic pathways. The mechanisms by which PS-ASOs are released from membrane-enclosed endocytotic organelles to reach target RNAs remain largely unknown. We recently found that annexin A2 (ANXA2) co-localizes with PS-ASOs in late endosomes (LEs) and enhances ASO activity. Here, we show that co-localization of ANXA2 with PS-ASO is not dependent on their direct interactions or mediated by ANXA2 partner protein S100A10. Instead, ANXA2 accompanies the transport of PS-ASOs to LEs, as ANXA2/PS-ASO co-localization was observed inside LEs. Although ANXA2 appears not to affect levels of PS-ASO internalization, ANXA2 reduction caused significant accumulation of ASOs in early endosomes (EEs) and reduced localization in LEs and decreased PS-ASO activity. Importantly, the kinetics of PS-ASO activity upon free uptake show that target mRNA reduction occurs at least 4 hrs after PS-ASOs exit from EEs and is coincident with release from LEs. Taken together, our results indicate that ANXA2 facilitates PS-ASO trafficking from early to late endosomes where it may also contribute to PS-ASO release.

| S-EPMC5009748 | biostudies-literature

Annexin A2 antibodies in post-treatment Lyme disease

Project description: Not available

| S-EPMC10981857 | biostudies-literature

HEK293T cell proteome remodeling upon Torin1 treatment or amino acid withdraw in WT and RPS3-Halo knock-in cells with or without NUFIP1 deletion. Related to Supplementary Table 5 from An et al (2020)

Project description:HEK293T proteome (single shot) with knock-in or not for RPS3-Halo and Knock out or not for NUFIP1. Cells were treated or not with Torin1 or deprived of amino acids.

2020-04-30 | PXD017851 | Pride

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