The cell biology of the plasminogen system

Plow, Edward F.; Herren, Thomas; Redlitz, Alexander; Miles, Lindsey A.; Hoover‐Plow, Jane

doi:10.1096/fasebj.9.10.7615163

Cited by 405 publications

(343 citation statements)

References 52 publications

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“…[26][27][28][29][30][31][32][33] Independent studies also have implicated externalized α-enolase and GAPDH on mammalian and pathogen surfaces as sites for plasminogen binding and subsequent activation by host or pathogen activities, [26][27][28]30,31,[34][35][36] and we have demonstrated that externalized glycolytic enzymes on the apoptotic cell surface, including α-enolase, also are sites for plasminogen binding. 12 Although enhanced virulence has been attributed to the presumptive augmentation in mobility through matrix or fibrin clots associated with localized plasminogen activation following binding on the pathogen surface, 37,38 no compelling physiological rationale exists for plasminogen binding on non-invasive bacteria and apoptotic cells.…”

Section: Box 1 the Repertoire Of Innate Apoptotic Immunity Early Transupporting

confidence: 58%

Exploiting death: apoptotic immunity in microbial pathogenesis

Ucker

2016

Cell Death Differ

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Innate immunity typically is responsible for initial host responses against infections. Independently, nucleated cells that die normally as part of the physiological process of homeostasis in mammals (including humans) suppress immunity. Specifically, the physiological process of cell death (apoptosis) generates cells that are recognized specifically by viable cells of all types and elicit a profound transient suppression of host immunity (termed 'innate apoptotic immunity' (IAI)). IAI appears to be important normally for the maintenance of self-tolerance and for the resolution of inflammation. In addition, pathogens are able to take advantage of IAI through a variety of distinct mechanisms, to enable their proliferation within the host and enhance pathogenicity. For example, the protist pathogen Leishmania amazonensis, at its infective stage, mimics apoptotic cells by expressing apoptotic-like protein determinants on the cell surface, triggering immunosuppression directly. In contrast, the pathogenic bacterium Listeria monocytogenes triggers cell death in host lymphocytes, relying on those apoptotic cells to suppress host immune control and facilitate bacterial expansion. Finally, although the inhibition of apoptotic cell death is a common attribute of many viruses which facilitates their extended replication, it is clear that adenoviruses also reprogram the non-apoptotic dead cells that arise subsequently to manifest apoptotic-like immunosuppressive properties. These three instances represent diverse strategies used by microbial pathogens to exploit IAI, focusing attention on the potency of this facet of host immune control. Further examination of these cases will be revealing both of varied mechanisms of pathogenesis and the processes involved in IAI control.

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Section: Box 1 the Repertoire Of Innate Apoptotic Immunity Early Transupporting

confidence: 58%

Exploiting death: apoptotic immunity in microbial pathogenesis

Ucker

2016

Cell Death Differ

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“…Plasminogen is a proenzyme found in plasma and extracellular fluids, which is converted to the broad spectrum serine protease plasmin upon activation (46). Active plasmin is capable of degrading fibronectin, fibrin, vitronectin, and laminin, with considerable evidence for the ability of plasmin to facilitate extracellular matrix degradation and invasion (34).…”

Section: Discussionmentioning

confidence: 99%

A Processed Multidomain Mycoplasma hyopneumoniae Adhesin Binds Fibronectin, Plasminogen, and Swine Respiratory Cilia

Seymour¹,

Deutscher

Jenkins

et al. 2010

Journal of Biological Chemistry

134

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Porcine enzootic pneumonia is a chronic respiratory disease that affects swine. The etiological agent of the disease, Mycoplasma hyopneumoniae, is a bacterium that adheres to cilia of the swine respiratory tract, resulting in loss of cilia and epithelial cell damage. A M. hyopneumoniae protein P116, encoded by mhp108, was investigated as a potential adhesin. Examination of P116 expression using proteomic analyses observed P116 as a full-length protein and also as fragments, ranging from 17 to 70 kDa in size. A variety of pathogenic bacterial species have been shown to bind the extracellular matrix component fibronectin as an adherence mechanism. M. hyopneumoniae cells were found to bind fibronectin in a dose-dependent and saturable manner. Surface plasmon resonance was used to show that a recombinant C-terminal domain of P116 bound fibronectin at physiologically relevant concentrations (K D 24 ؎ 6 nM). Plasmin(ogen)-binding proteins are also expressed by many bacterial pathogens, facilitating extracellular matrix degradation. M. hyopneumoniae cells were found to also bind plasminogen in a dose-dependent and saturable manner; the C-terminal domain of P116 binds to plasminogen (K D 44 ؎ 5 nM). Plasminogen binding was abolished when the C-terminal lysine of P116 was deleted, implicating this residue as part of the plasminogen binding site. P116 fragments adhere to the PK15 porcine kidney epithelial-like cell line and swine respiratory cilia. Collectively these data suggest that P116 is an important adhesin and virulence factor of M. hyopneumoniae.

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“…However, ligated plasmin can still be inactivated by aprotinin, which competes with fibrin for the plasmin active site. There is a growing list of ubiquitous plasminogen receptors, including alpha-enolase, cytokeratin 8, and annexin 11 [36]. Plasmin displays a broad spectrum activity, and is able to degrade many glycoproteins (laminin, fibronectin) and proteoglycans of the ECM, as well as fibrin, and to activate other proteinases such as pro-metalloproteinases (MMP-1, MMP-3 and MMP-9).…”

Section: The Plasminogen Systemmentioning

confidence: 99%

Role of plasminogen activator-plasmin system in tumor angiogenesis

Rakic¹,

Maillard²,

Jost³

et al. 2003

Cellular and Molecular Life Sciences (CMLS)

119

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New blood formation or angiogenesis has become a key target in therapeutic strategies aimed at inhibiting tumor growth and other diseases associated with neovascularization. Angiogenesis is associated with important extracellular remodeling involving different proteolytic systems among which the plasminogen system plays an essential role. It belongs to the large serine proteinase family and can act directly or indirectly by activating matrix metalloproteinases or by liberating growth factors and cytokines sequestered within the extracellular matrix. Migration of endothelial cells is associated with significant upregulation of proteolysis and conversely, immunoneutralization or chemical inhibition of the system reduces angiogenesis in vitro. On the other hand genetically altered mice developed normally without overt vascular anomalies indicating the possibility of compensation by other proteases in vivo. Nevertheless, they have in some experimental settings revealed unanticipated roles for previously characterized proteinases or their inhibitors. In this review, the complex mechanisms of action of the serine proteases in pathological angiogenesis are summarized alongside possible therapeutic applications.

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The cell biology of the plasminogen system

Cited by 405 publications

References 52 publications

Exploiting death: apoptotic immunity in microbial pathogenesis

Exploiting death: apoptotic immunity in microbial pathogenesis

A Processed Multidomain Mycoplasma hyopneumoniae Adhesin Binds Fibronectin, Plasminogen, and Swine Respiratory Cilia

Role of plasminogen activator-plasmin system in tumor angiogenesis

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