Annexin II a plasminogen-plasminogen activator co-receptor

Hajjar, Katherine A.

doi:10.2741/a779

Cited by 7 publications

(1 citation statement)

References 29 publications

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“…Age-related alterations in hemostatic cascades may also impair the subsequent induction of growth-factormediated angiogenesis. Proteases of the coagulation and fibrinolytic pathways have a significant role in the cleavage and activation of angiogenic growth factors (30). The same cascades have direct actions on the activation of matrix metalloproteases that are critical in the latter maturation stages of angiogenesis (31)(32).…”

Section: Hemostatic Proteolytic Cascades: Pre-angiogenic Vascular Sel...mentioning

confidence: 99%

Aging and angiogenesis

Edelberg

Reed

2003

Front Biosci

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Angiogenesis is impaired in aged tissues. It is probable that this deficit contributes to the increased severity of vascular diseases observed in older persons. The changes in angiogenesis that occur with aging have been noted at the molecular, cellular, and physiologic levels of regulation. Components of the neovascular process that are influenced by age include endothelial cells, the hemostatic cascade, neuro-chemical mediators, and growth factors and their cognate receptors. The structural and regulatory components of the matrix scaffold that surround newly formed vessels is also altered in aged tissues. These myriad changes result in delayed and impaired neovascularization. The clinical consequences of the decreased potential of aged tissues to form new vessels is detrimental during the revascularization of the ischemic heart and during the repair of injured tissues, but may be of benefit in slowing the growth of tumors. In this context, clinical strategies to improve the function of the aging vasculature in general, and the angiogenic response in particular, must be targeted to specific disease states in order to maximize the potential benefit to older individuals.

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Section: Hemostatic Proteolytic Cascades: Pre-angiogenic Vascular Sel...mentioning

confidence: 99%

Aging and angiogenesis

Edelberg

Reed

2003

Front Biosci

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Laser capture microdissection-based in vivo genomic profiling of wound keratinocytes identifies similarities and differences to squamous cell carcinoma

et al. 2003

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Identification of the annexin A2 heterotetramer as a receptor for the plasmin-induced signaling in human peripheral monocytes

Laumonnier

Syrovets

Burýšek

et al. 2006

Blood

106

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We have previously demonstrated that plasmin acts as a potent proinflammatory activator of human peripheral monocytes. Here we identify the annexin A2 heterotetramer, composed of annexin A2 and S100A10, as a receptor for the plasmin-induced signaling in human monocytes. Monocytes express the annexin A2 heterotetramer on the cell surface as shown by flow cytometry, fluorescence microscopy, and coimmunoprecipitation of biotinylated cell surface proteins. Binding of plasmin to annexin A2 and S100A10 on monocytes was verified by biotin transfer from plasmin labeled with a trifunctional cross-linker. Antibodies directed against annexin A2 or S100A10 inhibited the chemotaxis elicited by plasmin, but not that induced by fMLP. Further, downregulation of annexin A2 or S100A10 in monocytes by antisense oligodeoxynucleotides impaired the chemotactic response to plasmin, but not that to fMLP. Antisense oligodeoxynucleotides similarly decreased the TNF-␣ release by plasmin- IntroductionMost cells are able to bind plasmin(ogen) with low affinity. [1][2][3] Generally, the membrane binding of plasmin(ogen) has been mainly regarded in terms of membrane-associated activation of fibrinolytic or proteolytic activity. [4][5][6][7] However, plasmin may elicit profound functional changes in various cells implying receptormediated signaling. Plasmin induces neutrophil aggregation, biosynthesis of platelet-activating factor in endothelial cells, and Ca 2ϩ signaling in platelets and endothelial cells as well as proliferation of hepatocytes. 1,2 In monocytes plasmin triggers release of proinflammatory lipid mediators, 8 chemotaxis, 9 and expression of different proinflammatory genes such as tumor necrosis factor ␣ (TNF-␣), interleukin-1, monocyte chemoattractant protein-1, CD40, and tissue factor through activation of nuclear factor B (NF-B), 10 JAK/STAT, and p38 MAPK signaling cascades. 11 All these effects are critically dependent on the proteolytic activity and cannot be mimicked by either plasminogen or catalytically inactivated plasmin. [8][9][10] Several proteins, such as ␣-enolase, 12,13 annexin A2, and TIP49a on monocytic cell lines, [14][15][16] annexin A2 on endothelial cells, macrophages, and monocytes, [16][17][18] S100A10 in colorectal cancer and fibrosarcoma cells, 19,20 gp330 on kidney epithelial cells, 21 and several others 1 have been identified as plasmin(ogen) binding sites. Occasionally these binding sites have been termed receptors, yet mostly in terms of membrane-associated proteolytic activity without signal transduction function. Protease-activated receptor 1 (PAR1) and PAR4 have been proposed to mediate plasmin signaling in fibroblasts, platelets, 22,23 and transfected CHO cells. 24 Others proposed that PARs are not activated but rather truncated and inactivated by plasmin. 25 Available evidence indicates that on human monocytes the signaling plasmin receptor is distinct from PARs, 26 yet its identity remains obscure.Annexin A2 belongs to the family of calcium-binding proteins; it is found in the cytoplasm and co...

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Annexin II a plasminogen-plasminogen activator co-receptor

Cited by 7 publications

References 29 publications

Aging and angiogenesis

Aging and angiogenesis

Laser capture microdissection-based in vivo genomic profiling of wound keratinocytes identifies similarities and differences to squamous cell carcinoma

Identification of the annexin A2 heterotetramer as a receptor for the plasmin-induced signaling in human peripheral monocytes

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