Plasminogen-mediated matrix invasion and degradation by macrophages is dependent on surface expression of annexin II

Falcone, Domenick J.; Borth, Wolfgang; Khan, Korsa; Hajjar, Katherine A.

doi:10.1182/blood.v97.3.777

Cited by 94 publications

(102 citation statements)

References 67 publications

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“…51 Plasminogen and tPA were also up-regulated in the current study. In view of the fact that endotoxin has been shown to induce a hypercoagulable state in alcohol-fed rats, 52 up-regulation of annexin A2 may reflect a cellular defense to limit procoagulant activity in the liver similar to that which occurs in the vascular endothelium.…”

Section: Annexin A2mentioning

confidence: 58%

Gene Expression Profiling of Alcoholic Liver Disease in the Baboon (Papio hamadryas) and Human Liver

Seth¹,

Leo²,

McGuinness³

et al. 2003

The American Journal of Pathology

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The molecular pathogenesis of alcoholic liver disease (ALD) is not well understood. Gene expression profiling has the potential to identify new pathways and altered molecules in ALD. Gene expression profiles of ALD in a baboon model and humans were compared using DNA arrays. Reverse transcriptase-polymerase chain reaction and immunohistochemistry were used for downstream analysis of array results. cDNA array analysis revealed differential expression of several novel genes and pathways in addition to genes known to be involved in ALD pathogenesis. Overall gene expression profiles were similar in both species, with a majority of genes involved with fibrogenesis and xenobiotic metabolism, as well as inflammation, oxidant stress, and cell signaling. Genes associated with stellate cell activation (collagens, matrix metalloproteinases, tissue inhibitors of matrix metalloproteinase) were up-regulated in humans. Decreased expression of several metallothioneins was unexpected.

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Section: Annexin A2mentioning

confidence: 58%

Gene Expression Profiling of Alcoholic Liver Disease in the Baboon (Papio hamadryas) and Human Liver

Seth¹,

Leo²,

McGuinness³

et al. 2003

The American Journal of Pathology

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“…Putative receptors for plasmin on monocyte cell lines and primary monocytes include ␣-enolase, TIP49a, and annexin A2 (25,(43)(44)(45)(46). Recently, the annexin A2 heterotetramer has been identified as a receptor for plasmin-induced signaling in human monocytes (25).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, the annexin A2 heterotetramer has been identified as a receptor for plasmin-induced signaling in human monocytes (25). Moreover, annexin A2 has been linked to plasminogen-dependent matrix invasion by monocytes (46,47). Annexin A2, a member of a family of proteins that bind anionic phospholipids in a Ca 2ϩ -dependent manner, exists in three forms, a monomer (p36), a heterodimer, or a heterotetramer.…”

Section: Discussionmentioning

confidence: 99%

Urokinase-Type Plasminogen Activator Stimulation of Monocyte Matrix Metalloproteinase-1 Production Is Mediated by Plasmin-Dependent Signaling through Annexin A2 and Inhibited by Inactive Plasmin

Zhang¹,

Zhou²,

Bugge

et al. 2007

The Journal of Immunology

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Chronic inflammatory diseases are associated with connective tissue turnover that involves a series of proteases, which include the plasminogen activation system and the family of matrix metalloproteinases (MMPs). Urokinase-type plasminogen activator (uPA) and plasmin, in addition to their role in fibrinolysis and activation of pro-MMPs, have been shown to transduce intracellular signals through specific receptors. The potential for uPA and plasmin to also contribute to connective tissue turnover by directly regulating MMP production was examined in human monocytes. Both catalytically active high m.w. uPA, which binds to the uPAR, and low m.w. uPA, which does not, significantly enhanced MMP-1 synthesis by activated human monocytes. In contrast, the N-terminal fragment of uPA, which binds to uPAR, but lacks the catalytic site, failed to induce MMP-1 production, indicating that uPA-stimulated MMP-1 synthesis was plasmin dependent. Endogenous plasmin generated by the action of uPA or exogenous plasmin increased MMP-1 synthesis by signaling through annexin A2, as demonstrated by inhibition of MMP-1 production with Abs against annexin A2 and S100A10, a dimeric protein associated with annexin A2. Interaction of plasmin with annexin A2 resulted in the stimulation of ERK1/2 and p38 MAPK, cyclooxygenase-2, and PGE2, leading to increased MMP-1 production. Furthermore, binding of inactive plasmin to annexin A2 inhibited plasmin induction of MMP-1, suggesting that inactive plasmin may be useful in suppressing inflammation.

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“…Annexin II is a receptor for fibrinolytic activation localized on the cell surface of endothelial cells, monocytes, and syncytiotrophoblasts (22). Annexin II is directly involved in the pathogenesis of APS.…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis in monocytes of antiphospholipid syndrome patients: Deregulation of proteins related to the development of thrombosis

López‐Pedrera¹,

Cuadrado²,

Herández³

et al. 2008

Arthritis & Rheumatism

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Objective. Antiphospholipid antibodies (aPL) are closely related to the development of thrombosis, but the exact mechanism(s) leading to thrombotic events remains unknown. In this study, using proteomic techniques, we evaluated changes in protein expression of monocytes from patients with antiphospholipid syndrome (APS) related to the pathophysiology of the syndrome.Methods. Fifty-one APS patients were included. They were divided into 2 groups: patients with previous thrombosis, and patients with recurrent spontaneous abortion. As controls, we studied patients with thrombosis but without aPL, and age-and sex-matched healthy subjects.Results. The proteins that were more significantly altered among monocytes from APS patients with thrombosis (annexin I, annexin II, protein disulfide isomerase, Nedd8, RhoA proteins, and Hsp60) were functionally related to the induction of a procoagulant state as well as to autoimmune-related responses. Proteins reported to be connected to recurrent spontaneous abortion (e.g., fibrinogen and hemoglobin) were also determined to be significantly deregulated in APS patients without thrombosis. In vitro treatment with IgG fractions purified from the plasma of APS patients with thrombosis changed the pattern of protein expression of normal monocytes in the same way that was observed in vivo for monocytes from APS patients with thrombosis.

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Plasminogen-mediated matrix invasion and degradation by macrophages is dependent on surface expression of annexin II

Cited by 94 publications

References 67 publications

Gene Expression Profiling of Alcoholic Liver Disease in the Baboon (Papio hamadryas) and Human Liver

Gene Expression Profiling of Alcoholic Liver Disease in the Baboon (Papio hamadryas) and Human Liver

Urokinase-Type Plasminogen Activator Stimulation of Monocyte Matrix Metalloproteinase-1 Production Is Mediated by Plasmin-Dependent Signaling through Annexin A2 and Inhibited by Inactive Plasmin

Proteomic analysis in monocytes of antiphospholipid syndrome patients: Deregulation of proteins related to the development of thrombosis

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