Substrate kringle-mediated catalysis by the streptokinase-plasmin activator complex: Critical contribution of kringle-4 revealed by the mutagenesis approaches

Joshi, Kishore Kumar; Nanda, Jagpreet S.; Kumar, Prakash; Sahni, Girish

doi:10.1016/j.bbapap.2011.10.010

Cited by 8 publications

(6 citation statements)

References 67 publications

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“…Notably, this particular domain was shown to be important for the interaction with streptokinase (76). Prediction of the protein's secondary structure revealed that BBA70 consists of seven ␣-helices (designated A-G in Fig.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…Formation of the SK⅐Pg* and SK⅐Pm catalytic complexes is enhanced 12-14-fold in affinity by the COOH-terminal Lys 414 residue of SK binding to a Pg/Pm kringle that has not been definitively identified (13), whereas recent studies suggest that it may be kringle 4 (19). Binding of Pg in the substrate mode is mediated by interaction of Arg 253 , Lys 256 , and Lys 257 of the SK 250-loop in the ␤-domain with kringle 5 of the substrate Pg (20 -22).…”

Section: Streptokinase (Sk)mentioning

confidence: 99%

Full Time Course Kinetics of the Streptokinase-Plasminogen Activation Pathway

Nolan

Bouldin

Bock

2013

Journal of Biological Chemistry

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Background:We previously proposed a mechanism for plasminogen (Pg) activation by streptokinase (SK). Results: We tested the mechanism using new discontinuous assays that resolved the full time courses of all the reaction species. Conclusion: Analysis of the results independently validates the proposed SK-Pg activation pathway. Significance: The assays can be applied to SK-Pg activation in other contexts.

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“…The proteins consisted of the following regions of human plasminogen; K1-K5CD (residues 78-791), K2-K5CD (residues 163-791), K4K5CD (residues 350-791), K5CD (residues 440-791), and CD (residues 543-791). Proteins were expressed in Pichia pastoris and purified according to (15).…”

Section: Plasminogen Domain Mutantsmentioning

confidence: 99%

“…However, it is unclear which of the kringle domains play a role in the interaction of Lys-plasminogen with its binding partners. Recently, Sahni's group developed a series of truncated derivatives of Lys-plasminogen with progressive removal of kringle domains (15). We utilised these mutants to identify which plasminogen kringles interacted with S100A10.…”

Section: The Role Of the Plasminogen Kringle Domains In S100a10-mediamentioning

confidence: 99%

Mechanism of plasmin generation by S100A10

Miller¹,

Madureira²,

Kamaludin³

et al. 2017

Thromb Haemost

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Plasminogen (Pg) is cleaved to form plasmin by the action of specific plasminogen activators such as the tissue plasminogen activator (tPA). Although the interaction of tPA and Pg with the surface of the fibrin clot has been well characterised, their interaction with cell surface Pg receptors is poorly understood. S100A10 is a cell surface Pg receptor that plays a key role in cellular plasmin generation. In the present report, we have utilised domain-switched/deleted variants of tPA, truncated plasminogen variants and S100A10 site-directed mutant proteins to define the regions responsible for S100A10-dependent plasmin generation. In contrast to the established role of the finger domain of tPA in fibrin-stimulated plasmin generation, we show that the kringle-2 domain of tPA plays a key role in S100A10-dependent plasmin generation. The kringle-1 domain of plasminogen, indispensable for fibrin-binding, is also critical for S100A10-dependent plasmin generation. S100A10 retains activity after substitution or deletion of the carboxyl-terminal lysine suggesting that internal lysine residues contribute to its plasmin generating activity. These studies define a new paradigm for plasminogen activation by the plasminogen receptor, S100A10.

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Substrate kringle-mediated catalysis by the streptokinase-plasmin activator complex: Critical contribution of kringle-4 revealed by the mutagenesis approaches

Cited by 8 publications

References 67 publications

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Full Time Course Kinetics of the Streptokinase-Plasminogen Activation Pathway

Mechanism of plasmin generation by S100A10

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