Evidence for high-molecular weight active peptides originating from porcine plasmin autolysis

Grimard, M.

doi:10.1016/s0300-9084(77)80026-6

Cited by 4 publications

(2 citation statements)

References 14 publications

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“…Several laboratories have suggested that autoproteolysis of plasmin results in the digestion of the plasmin heavy and light chains in vitro (16)(17)(18)(19)(20). The digestion of the plasmin light chain has also been suggested to best correlate with the loss in plasmin activity in vitro (22).…”

Section: Discussionmentioning

confidence: 99%

“…The autoproteolysis reaction is retarded by fibrinogen, by ε-aminocaproic acid, by increasing ionic strength, and by glycerol. Although the autoproteolysis reaction involves the breakdown of both the A and B chains of plasmin, it is the breakdown of the B chain that has been suggested to contribute to the irreversible inactivation of the enzyme ( − ).…”

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confidence: 99%

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Regulation of Plasmin Activity by Annexin II Tetramer

et al. 2000

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Annexin II tetramer (AIIt) is a major Ca(2+)-binding protein of the endothelial cell surface which has been shown to stimulate the tissue plasminogen activator (t-PA)-dependent conversion of plasminogen to plasmin. In the present report, we have examined the regulation of plasmin activity by AIIt. The incubation of plasmin with AIIt resulted in a 95% loss in plasmin activity. SDS-PAGE analysis established that AIIt stimulated the autoproteolytic digestion of plasmin heavy and light chains. The kinetics of AIIt-stimulated plasmin autoproteolysis were first-order, suggesting that binding of plasmin to AIIt resulted in the spontaneous autoproteolysis of the bound plasmin. AIIt did not affect the activity of other serine proteases such as t-PA or urokinase-type plasminogen activator. Furthermore, other annexins such as annexin I, II, V, or VI did not stimulate plasmin autoproteolysis. Increasing the concentration of AIIt on the surface of human 293 epithelial cells increased cell-mediated plasmin autoproteolysis. Thus, in addition to stimulating the formation of plasmin, AIIt also promotes plasmin inactivation. These results therefore suggest that AIIt may function to provide the cell surface with a transient pulse of plasmin activity.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Regulation of Plasmin Activity by Annexin II Tetramer

et al. 2000

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Role of Annexin II Tetramer in the Regulation of Plasmin Activity

Choi¹,

Fogg²,

Fitzpatrick³

et al. 2003

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Melanotransferrin stimulates t-PA-dependent activation of plasminogen in endothelial cells leading to cell detachment

Rolland

Demeule

Béliveau

2006

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Tissue plasminogen activator (t-PA) is an extracellular serine protease that converts the proenzyme plasminogen into the broad-spectrum substrate serine protease, plasmin. Plasmin, one of the most potent pro-angiogenic factors, is a key element in fibrinolysis, cell migration, tissue remodeling and tumor invasion. In the present investigation, we assessed the impact of the truncated form of soluble melanotransferrin (sMTf) on plasminogen activation by t-PA and subsequent endothelial cell detachment. Co-treatment of human endothelial microvessel cells with plasminogen, t-PA and sMTf significantly increased plasmin formation and activity in the culture medium. Plasmin generated in the presence of sMTf also led to a 30% reduction in fibronectin detection within cell lysates and to a 9-fold increase within the corresponding cell medium. Moreover, the presence of sMTf increases EC detachment by 6-fold compared to cells treated only with plasminogen and t-PA. Although the addition of alpha(2)-antiplasmin completely prevented plasmin formation and EC detachment, epigallocatechin gallate, GM6001 and a specific antibody directed against MMP-2 prevented cellular detachment without interfering with plasminogen activation. Overall, these data suggest that the anti-angiogenic properties of sMTf may result from local overstimulation of plasminogen activation by t-PA, thus leading to subsequent degradation of the Fn matrix and EC detachment.

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Evidence for high-molecular weight active peptides originating from porcine plasmin autolysis

Cited by 4 publications

References 14 publications

Regulation of Plasmin Activity by Annexin II Tetramer

Regulation of Plasmin Activity by Annexin II Tetramer

Role of Annexin II Tetramer in the Regulation of Plasmin Activity

Melanotransferrin stimulates t-PA-dependent activation of plasminogen in endothelial cells leading to cell detachment

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