Last update 01 Nov 2024

ANXA2

Last update 01 Nov 2024

Basic Info

Synonyms

annexin A2, Annexin II, Annexin-2

+ [14]

Introduction

Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640). (Microbial infection) Binds M.pneumoniae CARDS toxin, probably serves as one receptor for this pathogen. When ANXA2 is down-regulated by siRNA, less toxin binds to human cells and less vacuolization (a symptom of M.pneumoniae infection) is seen.

Drugs associated with ANXA2

Lm-ANXA2

Target

ANXA2

Mechanism

ANXA2 inhibitors

Active Org.

Aduro BioTech, Inc.

Originator Org.

Aduro BioTech, Inc.

Active Indication

Pancreatic Cancer

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

PY-60

Target

ANXA2

Mechanism

ANXA2 agonists

Active Org.

The Scripps Research Institute

Originator Org.

The Scripps Research Institute

Active Indication-

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

LS301

Target

ANXA2

Mechanism

ANXA2 inhibitors

Active Org.

Washington University in St. Louis

Originator Org.

Washington University in St. Louis

Active Indication

Solid tumor

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ANXA2

100 Translational Medicine associated with ANXA2

0 Patents (Medical) associated with ANXA2

2,377

Literatures (Medical) associated with ANXA2

01 Dec 2024·Cellular and Molecular Life Sciences

Inhibition of the membrane repair protein annexin-A2 prevents tumor invasion and metastasis

Article

Author: Saltel, F ; Rouyer, L ; Khatib, A M ; Mélane, M ; Bouvet, F ; Iggo, R ; Argoul, F ; Derieppe, M A ; Harté, E ; Prouzet-Mauleon, V ; Tan, S ; d'Agata, L ; Brisson, A R ; Bouton, L ; Souleyreau, W ; Martineau, J ; Siegfried, G ; Bouter, A ; Darbo, E ; Chapeau, D ; Lefeuvre, M ; Gounou, C

AbstractCancer cells are exposed to major compressive and shearing forces during invasion and metastasis, leading to extensive plasma membrane damage. To survive this mechanical stress, they need to repair membrane injury efficiently. Targeting the membrane repair machinery is thus potentially a new way to prevent invasion and metastasis. We show here that annexin-A2 (ANXA2) is required for membrane repair in invasive breast and pancreatic cancer cells. Mechanistically, we show by fluorescence and electron microscopy that cells fail to reseal shear-stress damaged membrane when ANXA2 is silenced or the protein is inhibited with neutralizing antibody. Silencing of ANXA2 has no effect on proliferation in vitro, and may even accelerate migration in wound healing assays, but reduces tumor cell dissemination in both mice and zebrafish. We expect that inhibiting membrane repair will be particularly effective in aggressive, poor prognosis tumors because they rely on the membrane repair machinery to survive membrane damage during tumor invasion and metastasis. This could be achieved either with anti-ANXA2 antibodies, which have been shown to inhibit metastasis of breast and pancreatic cancer cells, or with small molecule drugs.

01 Nov 2024·Drug Development Research

RecQ protein‐like 4 drives cisplatin chemosensitivity of cervical cancer cells by modulating annexin A2

Article

Author: Wang, Ruixue ; Zhang, Yunyan

AbstractCervical cancer is a common malignant tumor in women with high morbidity and mortality. Chemotherapy drugs such as cisplatin (DDP) are easy to cause chemotherapy resistance and affect the therapeutic effect. Hence, it is critical to design new therapies that can reverse chemotherapy resistance and increase sensitivity to chemotherapy drugs. This study investigated the function of RecQ protein‐like 4 (RECQL4) in DDP‐resistant cervical cancer cells and its regulatory mechanism. By constructing DDP‐resistant Hela and CaSki cell lines, it was found that RECQL4 expression was elevated. RECQL4 knockdown is able to promote apoptosis, DNA damage, and increase the DDP sensitivity in cervical cancer cells. In vivo experiments have demonstrated that knockdown of RECQL4 suppresses tumor growth and promotes tumor apoptosis. Next, we investigated the potential regulatory relationship of RECQL4 to Annexin A2 (ANXA2). The results demonstrated that RECQL4 binds to ANXA2. Knockdown of RECQL4 downregulates the ANXA2 expression via promoting ubiquitination. Furthermore, we also found that ANXA2 overexpression partially abolished the role of RECQL4 knockdown in promoting apoptosis and DNA damage of cervical cancer cells, suggesting that RECQL4 plays a role in DDP sensitivity of cervical cancer cells by mediating ANXA2. In conclusion, the present study suggests that knocking down RECQL4 reduces DDP sensitivity in cervical cancer cells by modulating ANXA2. Targeting RECQL4 therapy may be a new strategy to improve chemosensitivity of cervical cancer cells.

01 Nov 2024·Veterinary Microbiology

Host restriction factor Rab11a limits Porcine deltacoronavirus invasion of cells via fusion peptide-mediated membrane fusion

Article

Author: Yan, Wenjun ; Han, Yun ; Wang, Hongning ; Zhang, Anyun ; Song, Cailiang ; Wang, Kailu ; Yang, Xin ; Li, Hao

Porcine deltacoronavirus (PDCoV) poses a serious threat to pork industry and has the potential for cross-species transmission. Yet, the invasion mechanisms and host factors involved are still unknown. In the present work, using siRNA interference and co-immunoprecipitation, we identified Annexin A2 (ANXA2), Prohibitin-2 (PHB2), or Caveolin-2 (CAV2) as host factors positively regulating the internalization of PDCoV. We further found that Rab11a co-localized with PDCoV S and inhibited PDCoV internalization. Subsequently, a pseudoviral infection model (LV-PDCoV S-GFP) was constructed, and ANXA2 or CAV2 promoted PDCoV invasion by downregulating Rab11a. Our results also indicated that ANXA2, CAV2, and Rab11a interact with the S protein via S-FP, thereby regulating virus-host membrane fusion. Through LV-PDCoV S-GFP infection, we found that Rab11a may act as a host restriction factor, and it could regulate the invasion efficiency of PDCoV by adding of exogenous GTP. These findings revealed that Rab11a was an exciting target to restrict fusion of PDCoV with host cell membranes. AVAILABILITY OF DATA AND MATERIAL: Not applicable.

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ANXA2

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