On the Contribution of S100A10 and Annexin A2 to Plasminogen Activation and Oncogenesis: An Enduring Ambiguity

Bydoun, Moamen; Waisman, David M.

doi:10.2217/fon.14.163

Cited by 21 publications

(22 citation statements)

References 52 publications

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“…High levels of AnxA2 correlate with hyperfibrinolysis in acute promyelocytic leukemia (Flood and Hajjar, 2011;Luo and Hajjar, 2013). In addition, data from p11 KO mice support findings that AnxA2/p11-dependent plasmin generation is involved in tumor progression (Bharadwaj et al, 2013;Luo and Hajjar, 2013;Bydoun and Waisman, 2014).…”

Section: Anxa2 Ko Micesupporting

confidence: 63%

“…Different models of AnxA2/p11-mediated plasminogen activation have been proposed. We recommend several reviews that have extensively discussed the formation, structural organization, translocation and mode of action of the extracellular AnxA2/p11 complex (Flood and Hajjar, 2011;Grieve et al, 2012;Hedhli et al, 2012;Bharadwaj et al, 2013;Luo and Hajjar, 2013;Bydoun and Waisman, 2014).…”

Section: Anxa2 Ko Micementioning

confidence: 99%

“…The consequences of high or low plasma levels of AnxA2/p11 in several human diseases linked to vascular homeostasis and angiogenesis have been discussed (Flood and Hajjar, 2011;Hedhli et al, 2012;Bharadwaj et al, 2013;Luo and Hajjar, 2013;Bydoun and Waisman, 2014). For instance, diet-induced hyperhomocysteinemia, which is implicated in thrombotic and atherosclerotic disease, shows fibrin accumulation and defects in neoangiogenesis resembling those observed in the AnxA2 -/-mice ).…”

Section: Anxa2 Ko Micementioning

confidence: 99%

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Annexins – insights from knockout mice

Grewal

Wason

Enrich

et al. 2016

Biological Chemistry

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Annexins are a highly conserved protein family that bind to phospholipids in a calcium (Ca 2+ ) -dependent manner. Studies with purified annexins, as well as overexpression and knockdown approaches identified multiple functions predominantly linked to their dynamic and reversible membrane binding behavior. However, most annexins are found at multiple locations and interact with numerous proteins. Furthermore, similar membrane binding characteristics, overlapping localizations and shared interaction partners have complicated identification of their precise functions. To gain insight into annexin function in vivo, mouse models deficient of annexin A1 (AnxA1), A2, A4, A5, A6 and A7 have been generated. Interestingly, with the exception of one study, all mice strains lacking one or even two annexins are viable and develop normally. This suggested redundancy within annexins, but examining these knockout (KO) strains under stress conditions revealed striking phenotypes, identifying underlying mechanisms specific for individual annexins, often supporting Ca 2+ homeostasis and membrane transport as central for annexin biology. Conversely, mice lacking AnxA1 or A2 show extracellular functions relevant in health and disease that appear independent of membrane trafficking or Ca 2+ signaling. This review will summarize the mechanistic insights gained from studies utilizing mouse models lacking members of the annexin family.

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Section: Anxa2 Ko Micesupporting

confidence: 63%

Section: Anxa2 Ko Micementioning

confidence: 99%

Section: Anxa2 Ko Micementioning

confidence: 99%

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Annexins – insights from knockout mice

Grewal

Wason

Enrich

et al. 2016

Biological Chemistry

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“…Binding sites of the S100A10 proteins and t-PA have been identified in the N-terminal domain of annexin A2 at the amino acids residues 1-14 and 8-13, respectively (Kube et al 1992, Cesarman et al 1994. Recent data suggest that annexin A2 does not bind plasminogen directly but rather acts to transport S100A10 to the cell surface (Madureira et al 2011, Bydoun & Waisman 2014. Our findings suggest that the extracellular form of annexin A2 found in the cancer-associated stroma in the ovarian cancer tissues may represent a cleaved and secreted form of annexin A2, which may assist in ovarian cancer progression and metastasis.…”

Section: :11mentioning

confidence: 69%

WOMEN IN CANCER THEMATIC REVIEW: Ovarian cancer–peritoneal cell interactions promote extracellular matrix processing

Ricciardelli

Lokman

Ween

et al. 2016

Endocrine-Related Cancer

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Ovarian cancer has a distinct tendency for metastasising via shedding of cancerous cells into the peritoneal cavity and implanting onto the peritoneum that lines the pelvic organs. Once ovarian cancer cells adhere to the peritoneal cells, they migrate through the peritoneal layer and invade the local organs. Alterations in the extracellular environment are critical for tumour initiation, progression and intra-peritoneal dissemination. To increase our understanding of the molecular mechanisms involved in ovarian cancer metastasis and to identify novel therapeutic targets, we recently studied the interaction of ovarian cancer and peritoneal cells using a proteomic approach. We identified several extracellular matrix (ECM) proteins including, fibronectin, TGFBI, periostin, annexin A2 and PAI-1 that were processed as a result of the ovarian cancerperitoneal cell interaction. This review focuses on the functional role of these proteins in ovarian cancer metastasis. Our findings together with published literature support the notion that ECM processing via the plasminogen-plasmin pathway promotes the colonisation and attachment of ovarian cancer cells to the peritoneum and actively contributes to the early steps of ovarian cancer metastasis.

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“…The proteolytic cleavage of ECM proteins is regulated by protease receptors. Our research group has previously demonstrated that S100A10 (p11) is a receptor for the pro-protease plasminogen and can drive cancer cell invasion by mediating the conversion of plasminogen into the active protease, plasmin (Choi et al, 2003;Zhang et al, 2004;Phipps et al, 2011;Kwon et al, 2005;O'Connell et al, 2011;Madureira et al, 2012;Bydoun and Waisman, 2014). S100A10 binds to annexin A2 in the cytosol forming a heterotetrameric complex which then translocates to the cell surface (Madureira et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

S100A10, a novel biomarker in pancreatic ductal adenocarcinoma

et al. 2018

Self Cite

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Pancreatic cancer is arguably the deadliest cancer type. The efficacy of current therapies is often hindered by the inability to predict patient outcome. As such, the development of tools for early detection and risk prediction is key for improving outcome and quality of life. Here, we introduce the plasminogen receptor S100A10 as a novel predictive biomarker and a driver of pancreatic tumor growth and invasion. We demonstrated that S100A10 mRNA and protein are overexpressed in human pancreatic tumors compared to normal ducts and nonductal stroma. S100A10 mRNA and methylation status were predictive of overall survival and recurrence‐free survival across multiple patient cohorts. S100A10 expression was driven by promoter methylation and the oncogene KRAS. S100A10 knockdown reduced surface plasminogen activation, invasiveness, and in vivo growth of pancreatic cancer cell lines. These findings delineate the clinical and functional contribution of S100A10 as a biomarker in pancreatic cancer.

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On the Contribution of S100A10 and Annexin A2 to Plasminogen Activation and Oncogenesis: An Enduring Ambiguity

Cited by 21 publications

References 52 publications

Annexins – insights from knockout mice

Annexins – insights from knockout mice

WOMEN IN CANCER THEMATIC REVIEW: Ovarian cancer–peritoneal cell interactions promote extracellular matrix processing

S100A10, a novel biomarker in pancreatic ductal adenocarcinoma

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