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Published on:09th Mar, 2015
Pharmacognosy Journal, 2015; 7(3):171-177
Original Article | doi:10.5530/pj.2015.3.5

Jackfruit (Artocarpus heterophyllus) seed extract exhibits fibrino(geno)lytic activity


Authors and affiliation (s):

Sowmyashree Gangaraju1, Bhagyalakshmi Manjappa1, Girish Kesturu Subbaiah1, Kemparaju Kempaiah2, Rangaiah Shashidhara Murthy3, Jane Hoover Plow4, Sebastin Santhosh Martin5, Manohar Shinde1, and Devaraja Sannaningaiah1*

1,*Department of Studies and Research in Biochemistry and Centre for Bioscience and Innovation, Tumkur University, Tumkur- 572103, India

2Departments of Studies in Biochemistry, University of Mysore, Manasagangothry, Mysore-570 006, India

3Department of Pharmaceutical Sciences, Philadelphia College of Osteopathic Medicine. Atlanta, Georgia, USA

4Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Lerner Research Institute, Cleveland, OH

5Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE 17177, Stockhlm, Sweden

Abstract:

Objective: The current study assesses the fibrinogen and fibrin clot hydrolyzing activities of aqueous seed extract of Jackfruit (AqSEJ). Methods: The protein banding pattern of AqSEJ (100 μg) was analyzed on SDS-PAGE. The proteolytic activity of AqSEJ was confirmed by spectrophotometer and zymography experiments. Fibrinogen, fibrin and plasma protein hydrolyzing activities of AqSEJ were analyzed on SDS-PAGE under reduced conditions. Plasminogen activation and indirect hemolytic activities was analyzed using spectrophotometer. The non-toxic property of AqSEJ was tested by edema, hemorrhage in experimental mice. Results: AqSEJ exhibited proteolytic activity and the specific activity was found to be 1.04 units/mg/min. Furthermore, AqSEJ non-specifically hydrolyzed Aα, followed by Bβ and γ chains of human fibrinogen and specifically hydrolyzed α polymer and α chain of partially cross linked human fibrin clot without affecting β chain and γ-γ dimer even up to the tested dose of 30 µg for the incubation period of 8 hours. Importantly, AqSEJ did not hydrolyze other plasma proteins and devoid of plasminogen activation property. The proteolytic activity of AqSEJ was completely neutralized by PMSF and IAA, while EDTA, EGTA, 1,10-Phenanthroline did not, suggesting the presence of serine and cysteine family proteases. Moreover, AqSEJ did not cause edema and hemorrhage in experimental mice up to the tested dose of 200 µg and nontoxic to RBC cells. Conclusion: AqSEJ hydrolyzes fibrinogen and fibrin clot and non-toxic in nature. Hence, this work showcases the potential applications of Jack fruit seed proteases in the treatment of thrombotic disorders.

Key words: Fibrino(geno)lysis, Hemostasis, Jackfruit, Moraceae, Non-hemorrhagic, Serine/cysteine protease.

 

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