Measurement of the binding of antifibrinolytic amino acids to various plasminogens

Brockway, William J.; Castellino, Francis J.

doi:10.1016/0003-9861(72)90488-2

Cited by 318 publications

(123 citation statements)

References 9 publications

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“…The iPr2P-F-treated sample exhibited no detectable amidolytic activity. Plasminogen and fibrinogen were purified as described (17,18). 1251-labeled fibrinogen was prepared by using the chloramine-T method (11,19 (20).…”

Section: Methodsmentioning

confidence: 99%

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Activated protein C stimulates the fibrinolytic activity of cultured endothelial cells and decreases antiactivator activity.

Sakata¹,

Curriden²,

Lawrence³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

181

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The effects of bovine activated protein C (APC) on the fibrinolytic activity of cultured bovine aortic endothelial cells were investigated. Confluent monolayers were incubated with purified APC under various conditions and changes in total fibrinolytic activity and in the level of plasminogen activator and plasminogen activator inhibitor (antiactivator) were monitored. The addition of APC to the cells in the absence of other blood or plasma components led to a rapid, dose-dependent increase of fibrinolytic activity both in the media and in cellular extracts. For example, 3.4 jtg of APC per ml resulted in a 15-fold increase of fibrinolytic activity in the medium within 1 hour. The enhanced fibrinolytic activity reflected increases in both the urokinase-related and tissue-type plasminogen activators produced by these cells. Interestingly, treatment of-cells with APC also caused a rapid, dose-dependent decrease in antiactivator activity. Diisopropyl fluorophosphate-inactivated APC did not decrease antiactivator or increase plasminogen activator. Although a small but significant direct (i.e., cell-independent) effect of APC on both fibrinolytic activity and antiactivator activity could be demonstrated, the major portion of these changes appeared to be cellmediated. These observations indicate that the fibrinolytic potential of cultured endothelial cells is increased by APC and that the enzyme active site is essential for this change. Moreover, the results suggest that one of the primary mechanisms for this stimulation of endothelial cell fibrinolytic activity involves an APC-mediated decrease in antiactivator.

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Section: Methodsmentioning

confidence: 99%

“…1251-labeled fibrinogen was prepared by using the chloramine-T method (11,19 (20). The cells used for these studies had been passaged [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] …”

Section: Methodsmentioning

confidence: 99%

Activated protein C stimulates the fibrinolytic activity of cultured endothelial cells and decreases antiactivator activity.

Sakata¹,

Curriden²,

Lawrence³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

181

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“…Small Angle X-ray Scattering-For these experiments, hPg was prepared from pooled human plasma on a Lys-Sepharose column as previously described (22). hPg, and the ligands, ⑀-aminocaproic acid (EACA), t-aminomethylcyclohexane-1-carboxylic acid (tranexamic acid; TxA), VEK35, and VEK75…”

Section: Surface Plasmon Resonance (Spr)-mentioning

confidence: 99%

Dimerization Is Not a Determining Factor for Functional High Affinity Human Plasminogen Binding by the Group A Streptococcal Virulence Factor PAM and Is Mediated by Specific Residues within the PAM a1a2 Domain

Bhattacharya

Zhong

Quek

et al. 2014

Journal of Biological Chemistry

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Background: High affinity human plasminogen (hPg) binding to Group A Streptococcus (GAS) is mediated by the coiledcoil M-like protein, PAM. Results: Amino acid residues in the a1a2 domain of PAM direct high affinity PAM/hPg binding regardless of oligomerization status of PAM. Conclusion: The a1a2 domain defines its hPg binding site, regardless of PAM dimerization. Significance: The virulence of GAS is altered by mutations in PAM(a1a2).

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“…Forms 1 and 2 of native Plgs were separated by chromatography on a Lys-Sepharose column (25,26). Form 2 of Plgs was used throughout the experiment.…”

Section: Methodsmentioning

confidence: 99%

Plasminogen Activation by Streptokinase via a Unique Mechanism

Young¹,

Shi²,

Wu³

et al. 1998

Journal of Biological Chemistry

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Measurement of the binding of antifibrinolytic amino acids to various plasminogens

Cited by 318 publications

References 9 publications

Activated protein C stimulates the fibrinolytic activity of cultured endothelial cells and decreases antiactivator activity.

Activated protein C stimulates the fibrinolytic activity of cultured endothelial cells and decreases antiactivator activity.

Dimerization Is Not a Determining Factor for Functional High Affinity Human Plasminogen Binding by the Group A Streptococcal Virulence Factor PAM and Is Mediated by Specific Residues within the PAM a1a2 Domain

Plasminogen Activation by Streptokinase via a Unique Mechanism

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