scholarly journals Organic Azide Inhibitors of Cysteine Proteases [J.Am. Chem. Soc.2006,128, 12396−12397].

2007 ◽  
Vol 129 (30) ◽  
pp. 9532-9532
Author(s):  
Giang Thanh Le ◽  
Giovanni Abbenante ◽  
Praveen K. Madala ◽  
Huy N. Hoang ◽  
David P. Fairlie
Keyword(s):  
Cysteine Proteases ◽  
Organic Azide

Organic Azide Inhibitors of Cysteine Proteases

2006 ◽  
Vol 128 (38) ◽  
pp. 12396-12397 ◽  
Author(s):  
Giang Thanh Le ◽  
Giovanni Abbenante ◽  
Praveen K. Madala ◽  
Huy N. Hoang ◽  
David P. Fairlie
Keyword(s):  
Cysteine Proteases ◽  
Organic Azide

Caspases and apoptosis

2002 ◽  
Vol 38 ◽  
pp. 9-19 ◽  
Author(s):  
Guy S Salvesen
Keyword(s):  
Cysteine Proteases ◽  
Signalling Pathways ◽  
Term Survival ◽  
Mature Adult ◽  
Intracellular Signalling Pathways ◽  
Adult Cell ◽  
Caspase Family ◽  
Cell Fragments ◽  
Pro Inflammatory Cytokines

The ability of metazoan cells to undergo programmed cell death is vital to both the precise development and long-term survival of the mature adult. Cell deaths that result from engagement of this programme end in apoptosis, the ordered dismantling of the cell that results in its 'silent' demise, in which packaged cell fragments are removed by phagocytosis. This co-ordinated demise is mediated by members of a family of cysteine proteases known as caspases, whose activation follows characteristic apoptotic stimuli, and whose substrates include many proteins, the limited cleavage of which causes the characteristic morphology of apoptosis. In vertebrates, a subset of caspases has evolved to participate in the activation of pro-inflammatory cytokines, and thus members of the caspase family participate in one of two very distinct intracellular signalling pathways.

Stem Bromelain Proteolytic Machinery: Study of the Effects of its Components on Fibrin (ogen) and Blood Coagulation

2020 ◽  
Vol 27 (11) ◽  
pp. 1159-1170
Author(s):  
Mohamed Azarkan ◽  
Mariana Marta González ◽  
Rafaèle Calvo Esposito ◽  
María Eugenia Errasti
Keyword(s):  
Blood Coagulation ◽  
Proteolytic Activity ◽  
Fibrinolytic Activity ◽  
Cysteine Proteases ◽  
Antithrombotic Agent ◽  
Proteolytic System ◽  
Total Extract ◽  
Low Concentrations ◽  
Fibrin Plate ◽  
Stem Bromelain

Background: Antiplatelet, anticoagulant and fibrinolytic activities of stem bromelain (EC 3.4.22.4) are well described, but more studies are still required to clearly define its usefulness as an antithrombotic agent. Besides, although some effects of bromelain are linked to its proteolytic activity, few studies were performed taking into account this relationship. Objective: We aimed at comparing the effects of stem bromelain total extract (ET) and of its major proteolytic compounds on fibrinogen, fibrin, and blood coagulation considering the proteolytic activity. Methods: Proteolytic fractions chromatographically separated from ET (acidic bromelains, basic bromelains, and ananains) and their irreversibly inhibited counterparts were assayed. Effects on fibrinogen were electrophoretically and spectrophotometrically evaluated. Fibrinolytic activity was measured by the fibrin plate assay. The effect on blood coagulation was evaluated by the prothrombin time (PT) and activated partial thromboplastin time (APTT) tests. Effects were compared with those of thrombin and plasmin. Results: Acidic bromelains and ananains showed thrombin-type activity and low fibrinolytic activity, with acidic bromelains being the least effective as anticoagulants and fibrinolytics; while basic bromelains, without thrombin-like activity, were the best anticoagulant and fibrinolytic proteases present in ET. Procoagulant action was detected for ET and its proteolytic compounds by the APTT test at low concentrations. The measured effects were dependent on proteolytic activity. Conclusion: Two sub-populations of cysteine proteases exhibiting different effects on fibrin (ogen) and blood coagulation are present in ET. Using well characterized stem bromelain regarding its proteolytic system is a prerequisite for a better understanding of the mechanisms underlying the bromelain action.

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