Annexin A5 is involved in migration and invasion of oral carcinoma

Wehder, Liane; Arndt, Stephanie; Murzik, Ulrike; Bosserhoff, Anja‐Katrin; Kob, Robert; Eggeling, Ferdinand von; Melle, Christian

doi:10.4161/cc.8.10.8404

Cited by 34 publications

(27 citation statements)

References 39 publications

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“…In contrast to the evidence of these studies, Annexin A5 was found to be up-regulated in tumors with Aln metastasis in the present study, consistent with report of other cancers (30). Most recently, Annexin A5 has been demonstrated to have possible influence on proliferation and invasion capacity of cancer cells via deregulation of the genes implicated in cell motility (31).…”

Section: Discussionsupporting

confidence: 88%

Differential protein expression in primary breast cancer and matched axillary node metastasis

Thongwatchara

Promwikorn²,

Srisomsap³

et al. 2011

Oncol Rep

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Abstract. Axillary lymph node (Aln) metastasis is a key step of tumor progression in breast cancer and is associated with an unfavorable prognosis. However, the mechanisms of this process are not well understood. proteomic technologies have led to identification of specific protein markers and a better understanding of the cellular processes. to explore this, differential protein expression was analyzed between nodepositive breast carcinoma and node-negative breast carcinoma (11 samples) and between primary breast carcinoma and matched metastatic ALN (five pairs) using a combination of 2D-sDs-pAge and lc-Mc/Ms. of the total 678 protein spots, 19 proteins were up-regulated and 3 proteins were down-regulated in node-positive breast carcinomas compared to node-negative breast carcinomas. Four up-regulated proteins were identified, namely Annexin 5, carbonic anhydrase I, peroxiredoxin 6 and proteasome α2 subunit. For proteins altered in metastatic Aln compared to primary tumors, 6 of 14 up-regulated proteins were identified: heat shock 70 kDa protein 5, protein disulfide isomerase, prolyl 4-hydroxylase β subunit precursor, lactate dehydrogenase B, triosephosphate isomerase 1 and β-tubulin and 5 of 23 down-regulated proteins were identified including 90 kDa heat shock protein, chain A apo-human serum transferrin, chain A α1-antitrypsin, enolase 1 and macrophage migration inhibitory factor. Immunohistochemistry showed stronger immunostaining for β-tubulin in metastatic Aln compared to primary breast tumor. All of the identified proteins function in various processes involved in cell survival and growth. our results suggest that these processes are critical for tumor progression and metastasis and the proteins identified could be candidate markers of clinical usefulness.

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Section: Discussionsupporting

confidence: 88%

Differential protein expression in primary breast cancer and matched axillary node metastasis

Thongwatchara

Promwikorn²,

Srisomsap³

et al. 2011

Oncol Rep

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“…Mostly, they are able to bind the phospholipid of the membranes in a Ca2+ dependent manner, and to perform subsequent activities related to membrane trafficking, signal transduction, and exocytosis [63]. In our proteomics study, we have found an ubiquitous and overexpressed presence of ANX1A (3x) and of two isoform of ANXA5 (3.8x and 1.46 x respectively), which are known to play an anti-apoptotic role and are thought to be involved at different levels in the tumor development, progression and invasivity [64][65][66]. Therefore both of them are regarded as potential tumor markers [67].…”

Section: Regulators Of Apoptosismentioning

confidence: 87%

Retrospective Proteomic Screening of 100 Breast Cancer Tissues

Pucci‐Minafra¹,

Cara²,

Musso³

et al. 2017

Preprint

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Abstract:The present investigation has been conducted on one hundred tissue fragments of breast cancer, collected and immediately cryopreserved following the surgical resection. The fragments were selected from patients with invasive ductal carcinoma of the breast, the most common and potentially aggressive type of mammary cancer, with the objective to increase the knowledge of breast cancer molecular markers, useful for diagnostic and prognostic categorization of patients, in assessing postsurgical therapeutic regimes. The proteomic screening, by 2D-IPG and mass spectrometry, allowed us to identify two main classes of protein clusters: proteins expressed ubiquitously at high levels in all patients, and proteins expressed sporadically among the same patients. Within the group of ubiquitous proteins, glycolytic enzymes and proteins with anti-apoptotic activity were predominant. Among the sporadic ones, proteins involved in cell motility, molecular chaperones and proteins involved in the detoxification appeared prevalent. The data of the present study indicates that the primary tumor growth is generally supported by two concurrent pathways: the inhibition of apoptosis and the stimulation of cellular proliferation. The second phase of the evolution of the tumor can be prematurely scheduled by the occasional presence of proteins involved in cell motility and in the defenses of the oxidative stress. To our knowledge this report on large-scales proteomics of breast cancer is currently a unique approach in the literature that offers the opportunity to evaluate the presence and recurrence of proteins to be used as prognostic indicators and susceptibility to metastasis in patients operated on for invasive ductal carcinoma of the breast.

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“…This protein is a member of a multigene family consisting of 13 members of Ca2+ and phospholipid binding proteins with peripheral membrane location. In our previous proteomics study, we found an ubiquitous and over-expressed presence of ANXA5, which is known to play an anti-apoptotic role, and similarly to other members of the family, it is thought to be involved at different levels in the tumor development, progression and invasivity [17][18][19]. Moreover, Annexin A5 is known to exert an anticoagulant effect, acting as an indirect inhibitor of the thromboplastin-specific complex [20].…”

Section: Common Interactors For Mmp2 and Mmp9mentioning

confidence: 96%

New Insights into the Occurrence of Matrix Metalloproteases -2 and -9 in a Cohort of Breast Cancer Patients and Proteomic Correlations

Cara¹,

Marabeti²,

Musso³

et al. 2018

Preprint

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Matrix metalloproteases (MMPS) are a family of well-known enzymes which operate prevalently in the extracellular domain, where they fulfil the function of remodeling the extracellular matrix. Within the about 26 family members, encoded by 24 genes in humans, MMP-2 and MMP-9, have been regarded as the primary responsibility for the basement membrane and pericellular ECM rearrangement. In cases of infiltrating carcinomas, which arise from the epithelial tissues of a gland or of an internal organ, a marked alteration of the expression and the activity levels of both MMPs is known to occur. Present investigation represents the continuation and upgrading of our previous studies, now focusing on the occurrence and intensity levels of MMP-2 and -9, and their proteomic correlations, in a cohort of 80 breast cancer surgical tissues.

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Annexin A5 is involved in migration and invasion of oral carcinoma

Cited by 34 publications

References 39 publications

Differential protein expression in primary breast cancer and matched axillary node metastasis

Differential protein expression in primary breast cancer and matched axillary node metastasis

Retrospective Proteomic Screening of 100 Breast Cancer Tissues

New Insights into the Occurrence of Matrix Metalloproteases -2 and -9 in a Cohort of Breast Cancer Patients and Proteomic Correlations

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