Altered expression of annexin II in human B-cell lymphoma cell lines

Chiang, Yungping; Davis, Randall G.; Vishwanatha, Jamboor K.

doi:10.1016/0167-4889(96)00103-6

Cited by 35 publications

(24 citation statements)

References 25 publications

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“…Interestingly, annexin I has been reported to be upregulated in human mammary adenocarcinoma cells (Ahn et al, 1997;Pencil and Toth, 1998). Similarly, annexin II has been shown to be upregulated in a variety of tumor cell lines including pancreatic (Vishwanatha et al, 1993), lymphoma (Chiang et al, 1996), and small cell lung (Cole et al, 1992) cancer cell lines. Also, annexin II expression is elevated in glioblastoma (Reeves et al, 1992) and hepatocellular carcinomas (Frohlich et al, 1990).…”

Section: Resultsmentioning

confidence: 99%

Annexin II expression is reduced or lost in prostate cancer cells and its re-expression inhibits prostate cancer cell migration

et al. 2003

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While studying Bim, a BH3-only proapoptotic protein, we identified an B36 kDa protein, which was abundantly expressed in all five strains of primary normal human prostate (NHP) epithelial cells but significantly reduced or lost in seven prostate cancer cell lines. The B36 kDa protein was subsequently identified as annexin II by proteomic approach and confirmed by Western blotting using an annexin II-specific antibody. Conventional and 2D SDS-PAGE, together with Western blotting, also revealed reduced or lost expression of annexin I in prostate cancer cells. Subcellular localization studies revealed that in NHP cells, annexin II was distributed both in the cytosol and underneath the plasma membrane, but not on the cell surface. Prostate cancer cells showed reduced levels as well as altered expression patterns of annexin II. Since annexins play important roles in maintaining Ca 2+ homeostasis and regulating the cytoskeleton and cell motility, we hypothesized that the reduced or lost expression of annexin I/II might promote certain aggressive phenotypes of prostate cancer cells. In subsequent experiments, we indeed observed that restoration of annexin II expression inhibited the migration of the transfected prostate cancer cells without affecting cell proliferation or apoptosis. Hence, our results suggest that annexin II, and, likely, annexin I, may be endogenous suppressors of prostate cancer cell migration and their reduced or lost expression may contribute to prostate cancer development and progression.

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Section: Resultsmentioning

confidence: 99%

Annexin II expression is reduced or lost in prostate cancer cells and its re-expression inhibits prostate cancer cell migration

et al. 2003

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“…Annexin II, a calcium-and phospholipid-binding protein and a substrate for protein-tyrosine kinases, is proposed to be involved in cell proliferation. 40 Expression of annexin II gene is significantly increased in various human cancers, 41,42 and down-regulation of annexin II in some human cells results in the inhibition of cell proliferation. 40 In the present study, TU + LNG treatment suppressed the expression of Annexin II; this might have inhibited cell proliferation in the testes and subsequently hampered spermatogenesis.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Testis Biopsies in Men Treated with Injectable Testosterone Undecanoate Alone or in Combination with Oral Levonorgestrel as Potential Male Contraceptive

Cui

Zhu

et al. 2008

J. Proteome Res.

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Treatment with injectable testosterone undecanoate (TU) alone or in combination with oral levonorgestrel (LNG) resulted in marked decreases in sperm concentrations. In this study, we used proteomic analyses to examine the cellular/molecular events occurring in the human testis after TU or TU + LNG treatment. We conducted a global proteomic analysis of the human testicular biopsies before and at 2 weeks after TU alone or TU + LNG treatment. Proteins showing significant changes in expression were identified and analyzed. As a result, 17 and 46 protein spots were found with significant differential expression after the treatment with TU alone and TU + LNG, respectively. TU treatment changed the expression of heterogeneous nuclear ribonucleoprotein K (hnRNP K), proteasome inhibitor PI31 subunit (PSMF1), and superoxide dismutase [Mn] mitochondrial precursor (SOD2). These proteins inhibit "assembly", induce cell death, and promote compensatory "cell survival" in the testis. After TU + LNG treatment, "proliferation/cell survival" and "apoptosis/death" were the predominant responses in the testis. TU + LNG treatment inhibited the expression of Prolyl 4-hydroxylase beta subunit (P4HB) and Annexin A2 (Annexin II). These proteins are involved in apoptosis and cell proliferation, respectively. TU + LNG treatment also enhanced the expression of SOD2 and Parvalbumin alpha (Pvalb). These two proteins may protect testicular cells against apoptosis/death and promote cell survival. In conclusion, TU and TU + LNG treatments suppress spermatogenesis through different pathways by changing the expression of different proteins. hnRNP K, PSMF1, SOD2, P4HB, Annexin II, and Pvalb, are key proteins that may be early molecular targets responsible for spermatogenesis suppression induced by hormone treatment.

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“…Overexpression of annexins has been reported in various carcinomas, and is thought to be associated with cell proliferation, differentiation and cell-cell adhesion in the pathogenesis of carcinoma [60][61][62][63]. However, the functions of annexins have not been fully elucidated.…”

Section: Proteins Involved In Cell Regulationmentioning

confidence: 99%

Searching for potential biomarkers of cisplatin resistance in human ovarian cancer using a label‐free LC/MS‐based protein quantification method

Fitzpatrick

You²,

Bemis³

et al. 2007

Proteomics Clinical Apps

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Platinum-based chemotherapy, such as cisplatin, is the primary treatment for ovarian cancer. However, drug resistance has become a major impediment to the successful treatment of ovarian cancer. To date, the molecular mechanisms of resistance to platinum-based chemotherapy remain unclear. In this study, we applied an LC/MS-based protein quantification method to examine the global protein expression of two pairs of ovarian cancer cell lines, A2780/A2780-CP (cisplatin-sensitive/cisplatin-resistant) and 2008/2008-C13*5.25 (cisplatin-sensitive/cisplatinresistant). We identified and quantified over 2000 proteins from these cell lines and 760 proteins showed significant expression changes with a false discovery rate of less than 5% between paired groups. Based on the results we obtained, we suggest several potential pathways that may be involved in cisplatin resistance in human ovarian cancer. This study provides not only a new proteomic platform for large-scale quantitative protein analysis, but also important information for discovery of potential biomarkers of cisplatin resistance in ovarian cancer. Furthermore, these results may be clinically relevant for diagnostics, prognostics, and therapeutic improvement for ovarian cancer treatment.

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Altered expression of annexin II in human B-cell lymphoma cell lines

Cited by 35 publications

References 25 publications

Annexin II expression is reduced or lost in prostate cancer cells and its re-expression inhibits prostate cancer cell migration

Annexin II expression is reduced or lost in prostate cancer cells and its re-expression inhibits prostate cancer cell migration

Proteomic Analysis of Testis Biopsies in Men Treated with Injectable Testosterone Undecanoate Alone or in Combination with Oral Levonorgestrel as Potential Male Contraceptive

Searching for potential biomarkers of cisplatin resistance in human ovarian cancer using a label‐free LC/MS‐based protein quantification method

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