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Indian Journal of Hematology and Blood Transfusion
Published in: Indian Journal of Hematology and Blood Transfusion 2/2018

01-04-2018 | Original Article

Cupincin: A Novel Cupin Domain Containing Protease from Rice (Oryza sativa L.) Bran Comprising of Procoagulant and Fibrinogenolytic Activity

Authors: Roopesh Sreedhar, Purnima Kaul Tiku

Published in: Indian Journal of Hematology and Blood Transfusion | Issue 2/2018

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Abstract

The current study was carried out to evaluate the pharmacological properties of cupincin- A novel cupin domain containing metalloprotease with limited proteolysis from rice bran on blood coagulation and hydrolysis of human fibrinogen. Cupincin preferentially hydrolyzed the Aα chain of fibrinogen and then the Bβ-chain, but not the γ-chain. Cupincin reduced the re-calcification time of citrated human plasma dose dependently. Analysis of citrated whole blood in the presence of cupincin by rotem showed a decrease in coagulation time and clot formation time. Sonoclot analysis indicated that cupincin cleaved fibrinogen of whole citrated blood. SDS-PAGE and sonoclot analysis (LI-30) indicated that cupincin lacked plasmin-like activity. Global hemostasis tests like rotem and sonoclot analysis determined cupincin as a procoagulant enzyme. Cupincin did not show any effect on prothrombin time and activated partial thromboplastin time tests suggesting its action on the common pathway of coagulation. The involvement of proteases from rice (Oryza sativa L.) in haemostasis has never been exploited before. This study could provide the basis for the development of new procoagulant agents from a nontoxic source like rice.
Literature
1.
2.
Costa JO, Fonseca KC, Garrote FMS, Cunha CC, de Freitas MV, Silva S, Araújo RB, Penha SN, de Oliveira F (2010) Structural and functional comparison of proteolytic enzymes from plant latex and snake venoms. Biochimie 2:1760–1765CrossRef
3.
Rajesh R, Shivaprasad HV, Gowda RC, Nataraju A, Dhananjaya BL, Vishwanath BS (2007) Comparative study on plant latex proteases and their involvement in hemostasis: a special emphasis on clot inducing and dissolving properties. Planta Med 73:1061–1067CrossRefPubMed
4.
Richter G, Hans PS, Friedrich D, Peter L (2002) Activation and inactivation of human factor X by proteases derived from Ficus carica. Br J Haematol 119:1042–1051CrossRefPubMed
5.
Shivaprasad HV, Riyaz M, Kumar VR, Dharmappa KK, Tarannum S, Siddesha JM (2008) Cysteine proteases from the Asclepiadaceae plants latex exhibited thrombin and plasmin like activities. J Thromb Thrombolysis 28:304–308CrossRefPubMed
6.
Rajesh R, Gowda CD, Nataraju A, Dhananjaya BL (2006) Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: action on human fibrinogen and fibrin clot. Biochimie 88:1313–1322CrossRefPubMed
7.
Salas CE, Gomes MTR, Hernandez M, Lopes MTP (2008) Plant cysteine proteinases: evaluation of the pharmacological activity. Phytochemistry 69:2263–2269CrossRefPubMed
8.
Satish S, Sairam F, Ahmed AU (2012) Moringa oleifera Lam: protease activity against blood coagulation cascade. Pharmacogn Res 4:44–49
9.
Priyanka U, Raghu RA, Poojitha B, Rinimol VR, Bindu J, Zohara N, Nanjunda S (2015) Laticiferous plant proteases in wound care. Int J Pharm Sci 7:44–49
10.
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254CrossRefPubMed
11.
Ouyang C, Teng CM (1976) Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom. Biochim Biophys Acta 420:298–308CrossRefPubMed
12.
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685CrossRefPubMed
13.
Diganta D, Nanjaraj U, Vilas H, Bannikuppe SB, Robin D (2013) Biochemical and biological characterization of Naja kaouthia venom from North-East India and its neutralization by polyvalent antivenom. J Venom Res 4:31–38
14.
Devaraja S, Girish KS, Devaraj VR, Kemparaju K (2010) Factor Xa-like and fibrin(ogen)olytic activities of a serine protease from Hippasa agelenoides spider venom gland extract. J Thromb Thrombolysis 29:119–126CrossRefPubMed
15.
Condrea E, Mammon Z, Aloof S, Devries A (1964) Susceptibility of erythrocytes of various animal species to the hemolytic and phospholipid spitting action of snake venom. Biochim Biophys Acta 84:365–375PubMed
16.
Ferraris VA, Ferraris SP, Saha SP, Eugene AH, Constance KH, Royston BD, Charles RB, Higgins RSD, George D, Jeremiah RB (2007) Perioperative blood transfusion and blood conservation in cardiac surgery: The Society of Thoracic Surgeons and The Society of Cardiovascular Anesthesiologists clinical practice guideline. Ann Thorac Surg 83(5 Suppl):S27–S86CrossRefPubMed
17.
18.
Luddington R, Baglin T (2004) Clinical measurement of thrombin generation by calibrated automated thrombography requires contact factor inhibition. J Thromb Haemost 11:1954–1959CrossRef
19.
Lang T, Bauters A, Braun SL, Pötzsch B, Von Pape KW, Kolde HJ, Lakner M (2004) Multi-centre investigation on reference ranges for ROTEM thromboelastometry. Blood Coagul Fibrinolysis 16:301–310CrossRef
Metadata
Title
Cupincin: A Novel Cupin Domain Containing Protease from Rice (Oryza sativa L.) Bran Comprising of Procoagulant and Fibrinogenolytic Activity
Authors
Roopesh Sreedhar
Purnima Kaul Tiku
Publication date
01-04-2018
Publisher
Springer India
Published in
Indian Journal of Hematology and Blood Transfusion / Issue 2/2018
Print ISSN: 0971-4502
Electronic ISSN: 0974-0449
DOI
https://doi.org/10.1007/s12288-017-0856-2

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