Annexin A2 Coordinates STAT3 to Regulate the Invasion and Migration of Colorectal Cancer Cells<i>In Vitro</i>

Xiu, Dianhui; Liu, Lin; Qiao, Fengli; Yang, Huajun; Lu, Cuihua

doi:10.1155/2016/3521453

Cited by 20 publications

(15 citation statements)

References 33 publications

(43 reference statements)

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“…Furthermore, ANXA2 depletion significantly reduced cell invasion and metastatic potential of breast cancer model in vivo. Similar findings of EGF enhanced ANXA2 expression and EMT promotion were observed in cervical cancer, pancreatic cancer and colon cancer cell lines (19,27,28).…”

Section: Discussionsupporting

confidence: 79%

Relationship Between Circulating Tumor Cells and Annexin A2 in Early Breast Cancer Patients

Bystrický

Čierna

Sieberova

et al. 2017

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Section: Discussionsupporting

confidence: 79%

Relationship Between Circulating Tumor Cells and Annexin A2 in Early Breast Cancer Patients

Bystrický

Čierna

Sieberova

et al. 2017

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“…We have reported that pY23-Anxa2 binds to and enhances STAT3 activation and promotes invasion and metastasis of breast cancer cells [56]. Consistently, Anxa2 associates with STAT3 and confers the aggressive behavior in colorectal cancer [46,66]. Interestingly, Rack1 is also involved in the activation of STAT3 in several cancer cells [36,67].…”

Section: Discussionmentioning

confidence: 73%

Rack1 mediates tyrosine phosphorylation of Anxa2 by Src and promotes invasion and metastasis in drug-resistant breast cancer cells

Fan

et al. 2019

Breast Cancer Res

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Background: Acquirement of resistance is always associated with a highly aggressive phenotype of tumor cells. Recent studies have revealed that Annexin A2 (Anxa2) is a key protein that links drug resistance and cancer metastasis. A high level of Anxa2 in cancer tissues is correlated to a highly aggressive phenotype. Increased Anxa2 expression appears to be specific in many drug-resistant cancer cells. The functional activity of Anxa2 is regulated by tyrosine phosphorylation at the Tyr23 site. Nevertheless, the accurate molecular mechanisms underlying the regulation of Anxa2 tyrosine phosphorylation and whether phosphorylation is necessary for the enhanced invasive phenotype of drug-resistant cells remain unknown. Methods: Small interfering RNAs, small molecule inhibitors, overexpression, loss of function or gain of function, rescue experiments, Western blot, wound healing assays, transwell assays, and in vivo metastasis mice models were used to investigate the functional effects of Rack1 and Src on the tyrosine phosphorylation of Anxa2 and the invasion and metastatic potential of drug-resistant breast cancer cells. The interaction among Rack1, Src, and Anxa2 in drug-resistant cells was verified by co-immunoprecipitation assay. Results: We demonstrated that Anxa2 Tyr23 phosphorylation is necessary for multidrug-resistant breast cancer invasion and metastasis. Rack1 is required for the invasive and metastatic potential of drug-resistant breast cancer cells through modulating Anxa2 phosphorylation. We provided evidence that Rack1 acts as a signal hub and mediates the interaction between Src and Anxa2, thereby facilitating Anxa2 phosphorylation by Src kinase. Conclusions: Our findings suggest a convergence point role of Rack1/Src/Anxa2 complex in the crosstalk between drug resistance and cancer aggressiveness. The interaction between Anxa2 and Rack1/Src is responsible for the association between drug resistance and invasive/metastatic potential in breast cancer cells. Thus, our findings provide novel insights on the mechanism underlying the functional linkage between drug resistance and cancer aggressiveness.

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“…Bcl2 and Bcl-xL expression can be regulated by STAT3, an important factor that relays signals from cytokines and growth factors to regulate gene expression in biological processes, including apoptosis induced by the JAK/STAT pathway (42,43). The relationship among GroEL, annexin A2, cell apoptosis, and the JAK/STAT pathway remains unknown and requires further studies.…”

Section: Discussionmentioning

confidence: 99%

GroEL Protein (Heat Shock Protein 60) of Mycoplasma gallisepticum Induces Apoptosis in Host Cells by Interacting with Annexin A2

Zhang

Chen

et al. 2019

Infect Immun

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Mycoplasma gallisepticum is an avian respiratory and reproductive tract pathogen that has a significant economic impact on the poultry industry worldwide. Although membrane proteins of Mycoplasma spp. are thought to play crucial roles in host interactions, very few have had their biochemical function defined. In this study, we found that the GroEL protein (heat shock protein 60) of Mycoplasma gallisepticum could induce apoptosis in peripheral blood mononuclear cells, and the underlying molecular mechanism was further determined. The GroEL gene from Mycoplasma gallisepticum was cloned and expressed in Escherichia coli to facilitate the functional analysis of recombinant protein. The purified GroEL protein was shown to adhere to peripheral blood mononuclear cells (PBMCs) and DF-1 cells and cause apoptosis in PBMCs. A protein pulldown assay coupled with mass spectrometry identified that annexin A2 possibly interacted with GroEL protein. Coimmunoprecipitation assays confirmed that GroEL proteins could bind to annexin A2, and confocal analysis further demonstrated that GroEL colocolized with annexin A2 in HEK293T cells and PBMCs. Moreover, annexin A2 expression was significantly induced by a recombinant GroEL protein in PBMCs, and knocking down annexin A2 expression resulted in significantly reduced apoptosis. Taken together, these data suggest that GroEL induces apoptosis in host cells by interacting with annexin A2, a novel virulence mechanism in Mycoplasma gallisepticum. Our findings lead to a better understanding of molecular pathogenesis in Mycoplasma gallisepticum.

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Annexin A2 Coordinates STAT3 to Regulate the Invasion and Migration of Colorectal Cancer CellsIn Vitro

Cited by 20 publications

References 33 publications

Relationship Between Circulating Tumor Cells and Annexin A2 in Early Breast Cancer Patients

Relationship Between Circulating Tumor Cells and Annexin A2 in Early Breast Cancer Patients

Rack1 mediates tyrosine phosphorylation of Anxa2 by Src and promotes invasion and metastasis in drug-resistant breast cancer cells

GroEL Protein (Heat Shock Protein 60) of Mycoplasma gallisepticum Induces Apoptosis in Host Cells by Interacting with Annexin A2

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