Annexin II overexpression is correlated with poor prognosis in human gastric carcinoma.
Koji EmotoH SawadaYukishige YamadaH. FujimotoYasushi TakahamaMasatou UenoTomoyoshi TakayamaHideki UchidaKiyoshi KamadaAkihiko NaitoShuya HiraoYoshiyuki Nakajima
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Abstract:
Annexins belong to a family of the calcium-dependent phospholipid binding proteins. They are also substrates of receptor tyrosine kinases. Overexpression of Annexin II, which has been reported in various carcinomas, is thought to be associated with cell proliferation, differentiation and cell-cell adhesion in the pathogenesis of carcinoma, but the functions of Annexins have not been fully elucidated. In this study, we investigated the role of Annexin II (p36) and its relationship with c-erbB-2 overexpression in gastric carcinoma. We studied Annexin II expression using Western blot analysis in 8 human gastric carcinoma cell lines and expression of Annexin II and c-erbB-2 using, immunohistochemistry in 153 primary gastric carcinomas. Western blot revealed that Annexin II was expressed in 8 human gastric carcinoma cell lines. It was more strongly expressed in the cell membrane than in the cytoplasm of tumor cells in primary gastric carcinoma tissues. Thirty-three percent of all cases were immunopositive for Annexin II, overexpression of which was more frequent in differentiated type (p = 0.0009), lymph node, metastasis (p = 0.0147) and venous invasion (p = 0.0092). Annexin II and c-erbB-2 overexpression were significantly correlated p = 0.0002) and patients with Annexin II had poorer prognoses (p = 0.0066). Multivariate analysis showed that immunopositivity of both Annexin II and c-erbB-2 was an independent and poor prognostic factor (p = 0.0037). In conclusion, Annexin II was overexpressed in advanced gastric carcinomas and it could contribute to the progression of gastric carcinoma.Keywords:
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Previously, we established an in vitro cellular carcinogenesis model of oral squamous cell carcinoma (OSCC), including the human immortalized oral epithelia cells (HIOECs) and its derived cancerous HB96 cells. In this study, comparative proteomic analysis identified that Annexin A1 was one of the significantly down‐regulated genes in the cancerous HB96 cells. To investigate Annexin A1 down‐regulation and its potential usefulness as a molecular marker in OSCC, we further screened Annexin A1 expressions with a panel of OSCC lines, and clinical samples of cancerous and the paired adjacent normal tissues from primary OSCC patients. By Western blot analysis and real‐time PCR, we showed that both Annexin A1 mRNA and protein expressions decreased in OSCC cell lines except in two cell lines for the mRNA levels. Immunohistochemistry and real‐time PCR also showed that both Annexin A1 mRNA and protein expressions decreased in the cancerous tissues from OSCC patients compared with those in the paired adjacent non‐malignant epithelia. More importantly, both Annexin A1 mRNA and protein expressions negatively correlated with the pathologic differentiation grades of cancerous tissues. The lower Annexin A1 mRNA or protein expressions correlated with the poorer pathologic differentiation grades. These results suggest that decreased expression of Annexin A1 contributes to the cancerous progression of OSCC, and Annexin A1 may be a potential biomarker for pathologic differentiation grade of OSCC.
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1alpha,25-Dihydroxyvitamin D(3) has been shown to exert its effects by both genomic (minutes to hours) and rapid (seconds to minutes) mechanisms. The genomic effects are mediated by interaction with the nuclear vitamin D receptor. We show that the vitamin D analog, [(14)C]-1alpha,25-dihydroxyvitamin D(3) bromoacetate, is specifically bound to a protein (molecular weight 36 kDa) in the plasma membrane of rat osteoblastlike cells (ROS 24/1). The plasma membrane protein labeled with the bromoacetate analog was identified as annexin II by sequence determination and Western blot. Partially purified plasma membrane proteins (PI 6.9-7.4) and purified annexin II exhibited specific and saturable binding for [(3)H]-1alpha, 25-dihydroxyvitamin D(3). Antibodies to annexin II inhibited [(14)C]-1alpha,25-dihydroxyvitamin D(3) bromoacetate binding to ROS 24/1 plasma membranes, immunoprecipitated the ligand-protein complex, and inhibited 1alpha,25-dihydroxyvitamin D(3)-induced increases in intracellular calcium in ROS 24/1 cells. The results indicate that annexin II may serve as a receptor for rapid actions of 1alpha, 25-dihydroxyvitamin D(3).
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Objective: To construct pIRES2-eGFP-Annexin A2 eukaryotic expression vector carrying human Annexin A2 gene and express Annexin A2 protein in 293T cell.Methods: Annexin A2 gene digested from pCMV5-Annexin A2 was ligated into eukaryotic expression vector pIRES2-eGFP.After restriction analysis and sequencing,the recombinant plasmid pIRES2-eGFP-Annexin A2 was transfected into 293T cells in the mediation of liposome.The expression of Annexin A2 was analyzed by western blot and real-time PCR. Results: The expression of Annexin A2 at both mRNA and protein levels were significantly increased when transfected with pIRES2-eGFP-Annexin A2 in 293T cells. Conclusion: The eukaryotic expression vector pIRES2-eGFP-Annexin A2 was correctly constructed and the Annexin A2 protein was successfully expressed in 293T cells.This will facilitate the following study on Annexin A2.
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To study the expression of Annexin A7 in the mouse testis, especially in different types of spermatogonia.We prepared Annexin A7 recombinant protein using prokaryotic expression, adsorbed the Annexin A7 antibody with it after identified by mass spectrometry, and detected the expression of Annexin A7 by Western-blot and immunohistochemistry.Annexin A7 was expressed in a development-dependent manner in the spermatogonia of the prepubertal mice and in the type-A single (As) and type-A paired (Apr) spermatogonia of adult mice. These results were confirmed by the co-localization of Annexin A7 and Stra8, a known determinant of differentiated spermatogonial stem cells (SSCs).Annexin A7 is the internal factor of As and Apr spermatogonia, which might be involved in the biological functions of SSCs.
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Annexin A2 has been involved in cancer cell adhesion, invasion and metastasis. However, the exact function and mechanism of Annexin A2 in tumor progression of NSCLCs have not been elucidated. In this study, we showed that Annexin A2 was evidently overexpressed in human NSCLCs cell lines and NSCLCs tissues. Clinicopathologic analysis showed that Annexin A2 expression was significantly correlated with clinical stage, and lymph node metastasis. Kaplan-Meier analysis revealed that patients with high Annexin A2 expression had poorer overall survival rates than those with low Annexin A2 expression. Moreover, we found that knockdown of Annexin A2 significantly suppressed cell proliferation and invasion of NSCLCs cells. Mechanistically, our studies showed that knockdown of Annexin A2 increased the expression of p53, which in turn, induced cell cycle G2 arrest and inhibited epithelial-to-mesenchymal transition (EMT). Taken together, these data suggest that Annexin A2 plays an important role in NSCLCs progression, which could serve as a potential prognosis marker and a novel therapeutic target for NSCLCs.
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Abstract This study investigates the expression of annexin 1 in urothelial carcinoma (UC) and its relation with clinicopathologic factors, and evaluates its potential clinical significance. Annexin 1 expression was analyzed by immunohistochemical staining with manual tissue microarrays and Western blot in UC. Immunohistochemical analysis of UC in tissue microarrays showed that annexin 1 protein was 76.5% (150/196) positive, which was markedly increased compared with that in the normal urothelium 20.8% (5/24) ( p < 0.01). In addition, the positive expression rate of annexin 1 was higher in the high‐grade UC (81.7%; 143/175) than in the low‐grade UC (33.3%; 7/21). Western blot revealed that the expression of annexin 1 was low in low‐grade UC, and markedly increased in high‐grade UC. In conclusion, annexin 1 overexpression is observed in UC, which suggests it may be associated with tumorigenesis and its expression correlates with the differentiation of UC.
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Annexin 1 (named p35, lipocortin I or calpactin II), initially described as a glucocorticoid induced protein, belongs to a new characterized family of intracellular proteins. In the skin, the role of annexins has still not been elucidated. In a previous study, we reported the localization of annexin 1 in both freshly isolated human epidermal cells and in cultured keratinocytes using immunofluorescence, FACS analysis and immunoblotting techniques. The protein was characterized by Western blot and immunoprecipitation as a 35 kDa protein. Results from in vivo studies confirmed the presence of annexin 1 in basal and suprabasal layers of normal human skin with modified reactivity patterns in hyperproliferative lesions. In the present study, the role of glucocorticoids in annexin 1 regulation was investigated in epidermal cells by Western blot and immunoprecipation assays. In contrast to other studies, we found that glucocorticoid treatment of epidermal cells led to a decrease in annexin 1 content in the cytoplasm and the membranes of cells. As annexin 1 was not detected in the nucleus of cells, we conclude that there was a down regulation of annexin 1 after glucocorticoid treatments rather than a translocation of the protein to the nucleus. Despite the absence of the signal peptide sequence necessary for protein secretion, annexin 1 was released in the keratinocyte culture medium. We found that the protein was secreted only in low Ca2+ medium (0.15 mM), this process required an active metabolism.
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