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      Thrombus Degradation by Fibrinolytic Enzyme of Stenotrophomonas sp. Originated from Indonesian Soybean-Based Fermented Food on Wistar Rats

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          Abstract

          Objective. To evaluate thrombus degrading effect of a fibrinolytic enzyme from food origin Stenotrophomonas sp. of Indonesia. Methods. Prior to animal study, the enzyme safety was tested using cell culture. The effect on expression of tissue plasminogen activator was also analysed in the cell culture. For in vivo studies, 25 Wistar rats were used: normal control, negative control, treatment groups with crude and semipurified enzyme given orally at 25 mg/kg, and positive control group which received Lumbrokinase at 25 mg/kg. Blood clot in the tail was induced by kappa carrageenan injection at 1 mg/kg BW. Results. Experiment with cell culture confirmed the enzyme safety at the concentration used and increased expression of tPA. Decreasing of thrombus was observed in the positive group down to 70.35 ± 23.11% of the negative control animals (100%). The thrombus observed in the crude enzyme treatment was down to 56.99 ± 15.95% and 71.5 ± 15.7% for semipurified enzyme. Scanning electron microscopy showed clearly that bood clots were found in the animals injected with kappa carrageenan; however, in the treatment and positive groups, the clot was much reduced. Conclusions. Oral treatment of enzyme from Stenotrophomonas sp. of Indonesian fermented food was capable of degrading thrombus induced in Wistar rats.

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          Most cited references30

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          Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo.

          Accumulation of fibrin in the blood vessels usually results in thrombosis, leading to myocardial infarction and other cardiovascular diseases. For thrombolytic therapy, microbial fibrinolytic enzymes have now attracted much more attention than typical thrombolytic agents because of the expensive prices and the undesirable side effects of the latter. The fibrinolytic enzymes were successively discovered from different microorganisms, the most important among which is the genus Bacillus from traditional fermented foods. The physiochemical properties of these enzymes have been characterized, and their effectiveness in thrombolysis in vivo has been further identified. Therefore, microbial fibrinolytic enzymes, especially those from food-grade microorganisms, have the potential to be developed as functional food additives and drugs to prevent or cure thrombosis and other related diseases.
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            Tissue-type plasminogen activator: a historical perspective and personal account.

            Over the past two decades tissue-type plasminogen activator (t-PA), the main physiological plasminogen activator, has been developed as a fibrin-specific thrombolytic agent for the treatment of various thromboembolic diseases. Milestones in this development include: first purification of human t-PA from uterine tissue, elucidation of the interactions regulating physiological fibrinolysis, thus providing a molecular basis for the concept of fibrin-specific plasminogen activation, first animal models of thrombosis and pilot studies in patients supporting the therapeutic potential of t-PA, cloning and expression of recombinant t-PA providing sufficient amounts for large scale clinical use, and demonstration of its therapeutic benefit in large multicenter clinical trials, mainly in patients with acute myocardial infarction (AMI), but also in patients with massive pulmonary embolism, ischemic stroke, deep vein thrombosis and peripheral arterial occlusion. Genetically modified variants of t-PA have been developed for bolus administration in patients with AMI.
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              A novel fibrinolytic enzyme extracted from the earthworm, Lumbricus rubellus.

              A strong fibrinolytic enzyme was readily obtained in saline extracts of the earthworm, Lumbricus rubellus. It hydrolyzed not only plasminogen-rich fibrin plates, but also plasminogen-free fibrin plates. The average fibrinolytic activity was about 100 CU (plasmin units) or 250 IU (urokinase units)/g wet weight. The molecular weight and isoelectric point were about 20,000 and 3.4, respectively. The enzyme was heat-stable and displayed a very broad optimal pH range. DFP and SBTI strongly inhibited the enzyme, but the anti-plasmin agent, t-AMCHA, exerted little effect under the same conditions. Purification of the enzyme was performed and three partially purified fractions were obtained. These three fractions were further subdivided. The first fraction (F-I) was divided into three fractions (F-I-0, F-I-1, and F-I-2), which exhibited similar biochemical characteristics. The second fraction (F-II) could not be subdivided. The third fraction (F-III) was divided into two fractions (F-III-1 and F-III-2). Based on results for their enzymatic activities against various substrates, the fraction I enzymes are thought to represent a chymotrypsin-like enzyme and the fraction III enzymes to represent a trypsin-like enzyme. The fraction II enzyme appears to be neither a trypsin- or chymotrypsin-like enzyme nor an elastase. The amino acid compositions of the six enzymes were estimated. Compared with other serine enzymes, these enzymes contained very abundant asparagine or aspartic acid, and there was very little proline or lysine. From the above data, these enzymes are regarded as novel fibrinolytic enzymes, and we name them collectively as Lumbrokinase from the generic name of the earthworm.
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                Author and article information

                Journal
                Adv Pharmacol Sci
                Adv Pharmacol Sci
                APS
                Advances in Pharmacological Sciences
                Hindawi Publishing Corporation
                1687-6334
                1687-6342
                2016
                21 August 2016
                : 2016
                : 4206908
                Affiliations
                1Dexa Laboratories of Biomolecular Sciences, Jalan Industri Selatan V Blok PP/7, Jababeka II, Cikarang 17550, Indonesia
                2Faculty of Biotechnology, Atmajaya University, Jalan Jenderal Sudirman 51, Jakarta Selatan 12930, Indonesia
                3Department of Food Science and Technology, Faculty of Agricultural Engineering and Technology, Bogor Agricultural University, Bogor 16002, Indonesia
                Author notes
                *Maggy T. Suhartono: mthenawidjaja@ 123456yahoo.com

                Academic Editor: Paola Patrignani

                Author information
                http://orcid.org/0000-0003-1085-0984
                http://orcid.org/0000-0002-0295-6554
                Article
                10.1155/2016/4206908
                5011239
                0aca9bee-086b-4a0e-9fee-15056d08161c
                Copyright © 2016 Florensia Nailufar et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 11 March 2016
                : 11 July 2016
                : 26 July 2016
                Funding
                Funded by: Dexa Laboratories of Biomolecular Sciences
                Funded by: Atma Jaya University
                Categories
                Research Article

                Pharmacology & Pharmaceutical medicine
                Pharmacology & Pharmaceutical medicine

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