Proteins derived from latex of C. procera maintain coagulation homeostasis in septic mice and exhibit thrombin- and plasmin-like activities

Ramos, Márcio V.; Viana, Carolina A.; Silva, Ayrles F.B.; Freitas, Cléverson D.T.; Figueiredo, Ingrid Samantha Tavares de; Oliveira, Raquel Sombra Basílio de; Alencar, Nylane Maria Nunes de; Lima‐Filho, José Vitor; Kumar, Vijay

doi:10.1007/s00210-012-0733-3

Cited by 33 publications

(23 citation statements)

References 30 publications

(37 reference statements)

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“…Curiously, although the CgLP and CgLP PI fraction have shown plasmin-like activity, the fractions were not able to hydrolyze the fibrin clot completely. Similar results regarding on the presence of fibrinogelolytic activity were obtained after analysis of latex protein fraction from Calotropis procera [12]. In this case, protein fractions from C. procera containing cysteine protease activity accelerated clot formation in a similar manner to the action of thrombin, but were also unable to completely hydrolyze the fibrin clot.…”

Section: Discussionsupporting

confidence: 78%

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Thrombin and plasmin-like activities in the latices of Cryptostegia grandiflora and Plumeria rubra

Viana¹,

Oliveira²,

Freitas³

et al. 2013

Blood Coagulation & Fibrinolysis

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Latex proteins have drawn attention because they have shown several pharmacological activities. Herein, the fibrin(ogen)olytic activity of Cryptostegia grandiflora (CgLP) and Plumeria rubra (PrLP) latices were evaluated and characterized. Ion-exchange chromatography separated CgLP in proteolytic (CgLP PI) and nonproteolytic proteins (CgLP PII). CgLP and CgLP PI hydrolyzed azocasein in a dose-dependent manner, whereas CgLP PII and PrLP showed negligible activities. CgLP and CgLP PI accelerated plasmatic clot formation and digested all fibrinogen chains in a time/dose-dependent manner, though in a nonspecific way. CgLP and CgLP PI did not fully hydrolyze the subunits of the fibrin clot since fibrin α-chain showed resistance to proteolysis. No fibrinogenolytic activity was noticed after incubation of CgLP and CgLP PI with E-64. These results suggested that fibrinogenolytic and procoagulant activities of C. grandiflora were performed by cysteine proteases and confirm the activity of latex cysteine proteases as thrombin and plasmin-like proteins.

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Section: Discussionsupporting

confidence: 78%

“…Many publications have shown that latex displays pharmacological properties such as anti-inflammatory, analgesic, anticancer, wound healing and procoagulant activities [7][8][9][10][11][12]. Studies indicate that some of these pharmacological activities were related to the presence of cysteine proteases in latex [13][14][15].…”

Section: Introductionmentioning

confidence: 99%

Thrombin and plasmin-like activities in the latices of Cryptostegia grandiflora and Plumeria rubra

Viana¹,

Oliveira²,

Freitas³

et al. 2013

Blood Coagulation & Fibrinolysis

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“…It is devoid of proteolytic activity while LP PII and LP PIII exhibit proteolytic activity. [1011] Like LP fraction, the LP PI sub-fraction has been shown to inhibit neutrophil infiltration at the site of inflammation and to afford protection in a murine model of sepsis. [1012]…”

Section: Introductionmentioning

confidence: 99%

Antiedematogenic and antioxidant properties of high molecular weight protein sub-fraction of Calotropis procera latex in rat

Chaudhary

Viana

Ramos

et al. 2015

J Basic Clin Pharma

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Objectives:The aim was to evaluate the effect of high molecular weight protein fraction of Calotropis procera latex on edema formation and oxidative stress in carrageenan-induced paw inflammation.Methods:A sub-plantar injection of carrageenan was given to induce edema in the hind paw of the rat. The inhibitory effect of high molecular weight protein fraction of C. procera latex was evaluated following intravenous administration (5 and 25 mg/kg body weight) and was compared with that of diclofenac given orally (5 mg/kg). The levels of reduced glutathione (GSH), thiobarbituric acid reactive substances (TBARS) and myeloperoxidase (MPO) were measured in the inflamed paw tissue at the end of the study.Results:The high molecular weight protein fraction obtained from the latex of C. procera produced a dose-dependent inhibition of edema formation that was accompanied by normalization of levels of oxidative stress markers (GSH and TBARS) and MPO, a marker for neutrophils in the paw tissue.Conclusions:The high molecular weight protein fraction of C. procera latex ameliorates acute inflammation in the paw through its antioxidant effect.

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“…Similar studies on various latex producing plants showed the involvement of their latex proteases in both blood coagulation and fibrinolysis. [1215] Cysteine proteases present in the latex of a closely related species, C. procera , exhibited thrombin- and plasmin-like activities in vivo suggesting its therapeutic potential in various conditions associated with coagulation abnormalities[37]…”

Section: Discussionmentioning

confidence: 99%

Hemostatic, milk clotting and blood stain removal potential of cysteine proteases from Calotropis gigantea (L.) R. Br. Latex

Sukumaran¹,

Singh²

2014

Phcog Mag

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Introduction:Plant latex is a natural source of biologically active compounds and several hydrolytic enzymes responsible for their diverse health benefits. Recent past has witnessed substantial progress in understanding their supplementary industrial and pharmaceutical utility. Calotropis gigantea is one of the important latex producing plants belonging to asclepediaceae family with wide ethnopharmacological applications and is rich in proteolytic enzymes. Present study investigates hemostatic, milk clotting and blood stain removal potential of C. gigantea latex proteases.Materials and Methods:The protease activity of crude enzyme (CE), obtained by centrifugation followed by ammonium sulphate precipitation and dialysis, was assayed using casein as the substrate. Effect of pH, temperature and specific inhibitors on protease activity was determined. Native PAGE and in gel protease activity of CE was performed. Hemostatic (Fibrinogen polymerization, fibrinogen agarose plate and blood clot lysis assays), milk clotting and blood stain removal efficacies of CE were determined.Results:CE exhibited high caseinolytic activity. Enzyme activity was optimum at 37-50ºC and pH 8.0. Fibrinogen polymerization assay showed concentration dependent increase in turbidity indicating thrombin like activity which was further confirmed by fibrinogen agarose plate assays. Clot lysis assay indicated 92.41% thrombolysis by CE in 90 min. CE also revealed significantly high ratio of milk clotting to protease activity (Milk Clotting Index, MCI = 827.59 ± 1.52). Complete destaining of blood stained fabric was observed when incubated with 1% detergent incorporated with 0.1mg/ml CE. The study highlights and validates the compound application potential of latex cysteine proteases from C. gigantea.

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Proteins derived from latex of C. procera maintain coagulation homeostasis in septic mice and exhibit thrombin- and plasmin-like activities

Cited by 33 publications

References 30 publications

Thrombin and plasmin-like activities in the latices of Cryptostegia grandiflora and Plumeria rubra

Thrombin and plasmin-like activities in the latices of Cryptostegia grandiflora and Plumeria rubra

Antiedematogenic and antioxidant properties of high molecular weight protein sub-fraction of Calotropis procera latex in rat

Hemostatic, milk clotting and blood stain removal potential of cysteine proteases from Calotropis gigantea (L.) R. Br. Latex

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