Laminin interacts with plasminogen and its tissue‐type activator

Salonen, Eeva‐Marjatta; Zitting, Antti; Vaheri, Antti

doi:10.1016/0014-5793(84)80866-2

Cited by 111 publications

(41 citation statements)

References 20 publications

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“…In developing brain, certain glial-derived inhibitors of plasminogen activators that are not active against thrombin [33] may initially suppress neuroblast migration, thereby allowing glial-derived thrombin inhibitors to induce efficient neuritogenesis, Similar hierarchical effects on the early stages of neuroblastoma differentiation have been described: glial-derived extracellular matrix factors [40] including laminin [35], and inhibition of a pretense with calpain-like specificity [16], potentiate and enhance the outgrowth of the otherwise transient neurites induced by inhibition of the putative thrombinlike proteas¢. In this regard, plasminogen binds with high affinity to both luminia and fibronectin [43], indicating that particular areas rich in extraeeilular matrix components may serve as 'reservoirs' for plasminogen during neuronal migration. Furthermore, neural crest migration on fibronectin requires urokinase-type plas-minogen activator activity [3].…”

Section: Discussionmentioning

confidence: 73%

“…Indeed, suppression of cell motility has been shown to be the major rate-determining event in neuritogenesis in NG 10S-I 5 cells [42]. The physiological role of suri~ace protease inhibition in neurite outgrowth in the developing brain remains uncertain [43]. These studies on cultured neuronal cells demonstrate that plasmin and thrombin~ or a thrombinlike protease [l 6,17,35,40], mediate experimentally separable aspects of neuronal maturation and neuritogenesis.…”

Section: Discussionmentioning

confidence: 99%

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Regulation of neuronal migration and neuritogenesis by distinct surface proteases Relative contribution of plasmin and a thrombin‐like protease

Shea

Beermann

1992

FEBS Letters

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The relative contribution of two neuronal .~urface pretenses, plasmin and a pretense with thrombin-like specificity, on NB2a/dl neutoblastoma migration and neuritogengsis were examined. Exogenoua plasmin induced cell body rounding and increased cell migration, but did not prevent or reverse neurite outgrowth. Inhibition of endogenous plasmin by its specific inhibitor, aprotinin, suppressed migration but did not induce neuritogenesis. Removal or inhibition of the thrombin-like pretense by serum deprivation or hirudin addition, respectively, induced neurite outgrowth, as shown in our previous studie~, but did not suppress migration. By contrast, trypsin induced simultaneous cell rounding and neurite retraction. These findingB indicated that plasmin may regulate cell migration, while the thrombin.like protease may regulate facets of neurite outgrowth. Although unable to induce de nero neurito~enesis, plasmin inhibition potentiated the otherwise transient neurites induced by simultaneou~ inhibition of the thrombin-like pretense. Since cultured neuronal cells migrate primarily in the direction of newly elaborated neurites, this findin~ iz interpreted to indleate that cessation of neuronal migration by plasmin inhibition enhances net neurite outgrowth by inhibition of the putative thrombin-like pretense.

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Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Regulation of neuronal migration and neuritogenesis by distinct surface proteases Relative contribution of plasmin and a thrombin‐like protease

Shea

Beermann

1992

FEBS Letters

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“…The affinity of plasminogen and plasminogen activators for laminin (61), fibronectin (62), and fibrin (45) further suggests the importance of these proteinases in the turnover of matrix components. Clearly, proteolysis taking place at cellular contact sites is of considerable importance for the interaction between the membrane structures and the surrounding matrix components.…”

Section: Abbreviations Used In This Papermentioning

confidence: 99%

Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells

Pöllänen¹,

Saksela²,

Salonen³

et al. 1987

The Journal of Cell Biology

296

127

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Abstract. We studied the immunocytochemical localization of urokinase-type plasminogen activator (u-PA) and the type 1 plasminogen activator inhibitor (PAI-1) in human fibroblasts and sarcoma cells, using both polyclonal and monoclonal antibodies. The u-PA was found to be located at discrete cell-substratum contact sites, and also at areas of cell-cell contacts, whereas PAI-1 was distributed as a homogenous carpet excluding strialike areas on the substrate under the cells. To confirm the extracellular localization of u-PA and PAIl, we stained the cells live at 0°C before fixation. A double-labeling experiment showed different distribution of u-PA and PAI-1 under the cells, and especially their peripheral parts. The staining pattern of u-PA and PAI-1 resisted treatment with 0.2% saponin followed by mechanical removal of cells, a method previously reported to isolate focal contact membranes of fibroblasts. We further demonstrated the deposition of u-PA to the contact areas of cells obtained by saponin treatment by zymography, and that of PAI-1 by metabolic labeling, reverse zymography, immunoblotting, and immunoprecipitation. Fibronectin was also present in the preparations. The deposition of both PAI-1 and fibronectin by the sarcoma cells was enhanced, after treating the cells with 10 -6 M dexamethasone. The confinement of u-PA to discrete contact sites and the more uniform distribution of PAI-1 on the cell substratum may explain how cells producing large amounts of enzyme inhibitors can produce PAmediated focal proteolysis.

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“…Bacterial activators, such as staphylokinase from Staphylococcus aureus and streptokinase, secreted by group A, C, and G streptococci, can also activate plasminogen (9 -11). Plasmin has a relatively broad substrate spectrum, and in addition to fibrin(ogen), plasmin can cleave components of the host ECM, such as laminin (12), fibronectin (13), vitronectin (14,15), and heparan sulfate proteoglycans (16).…”

mentioning

confidence: 99%

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Koenigs

Hammerschmidt

Jutras

et al. 2013

Journal of Biological Chemistry

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Background: Recruitment of plasminogen is important for efficient dissemination of Borrelia burgdorferi. Results: BBA70 of B. burgdorferi binds plasminogen, and following activation, bound plasmin can cleave fibrinogen and inactivate the key complement components C3b and C5. Conclusion: BBA70 is a potent plasminogen-binding protein.Significance: Investigation suggests that binding of plasminogen may aid in pathogen dissemination and inhibit bacteriolytic effects of the host complement system.

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Laminin interacts with plasminogen and its tissue‐type activator

Abstract: Laminin Plasminogen Plasminogen activator Proteolysis

Cited by 111 publications

References 20 publications

Regulation of neuronal migration and neuritogenesis by distinct surface proteases Relative contribution of plasmin and a thrombin‐like protease

Regulation of neuronal migration and neuritogenesis by distinct surface proteases Relative contribution of plasmin and a thrombin‐like protease

Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

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