Pennisetum glaucum Protein Extract Protects RBC, Liver, Kidney, Small Intestine from Oxidative Damage and Exhibits Anticoagulant, Antiplatelet Activity

References

• Girish KS, Paul M, Thushara RM, Hemshekhar M, Shanmuga Sundaram M, Rangappa KS, Kemparaju K. Melatonin elevates apoptosis in human platelets via ROS mediated mitochondrial damage. Biochem Biophys Res Commun. 2013;438(1):198–204. doi:10.1016/j.bbrc.2013.07.053.
   Web of Science ®Google Scholar
• Valko M, Rhodes CJ, Moncol J, Izakovic M, Mazur M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact. 2006;160(1):1–40. doi:10.1016/j.cbi.2005.12.009.
   PubMed Web of Science ®Google Scholar
• Valko M, Izakovic M, Mazur M, Rhodes CJ, Telser J. Role of oxygen radicals in DNA damage and cancer incidence. Mol Cell Biochem. 2004;266(1–2):37–56. doi:10.1023/B:MCBI.0000049134.69131.89.
   PubMed Web of Science ®Google Scholar
• Taniyama Y, Griendling KK . Reactive oxygen species in the vasculature: molecular and cellular mechanisms. Hypertension. 2003;42(6):1075–81. doi:10.1161/01.HYP.0000100443.09293.4F.
   PubMed Web of Science ®Google Scholar
• Park HJ, DiNatale DA, Chung M-Y, Park Y-K, Lee J-Y, Koo SI, O’Connor M, Manautou JE, Bruno RS. Green tea extract attenuates hepatic steatosis by decreasing adipose lipogenesis and enhancing hepatic antioxidant defenses in ob/ob mice. J Nutr Biochem. 2011;22(4):393–400. doi:10.1016/j.jnutbio.2010.03.009.
   PubMed Web of Science ®Google Scholar
• Bonora E, Targher G. Increased risk of cardiovascular disease and chronic kidney disease in NAFLD. Nat Rev Gastroenterol Hepatol. 2012;9(7):372–81. doi:10.1038/nrgastro.2012.79.
   PubMed Web of Science ®Google Scholar
• Freikman I, Fibach E. Distribution and shedding of the membrane phosphatidylserine during maturation and aging of erythroid cells. Biochim Biophys Acta. 2011;1808(12):2773–80. doi:10.1016/j.bbamem.2011.08.014.
   Web of Science ®Google Scholar
• Whelihan MF, Zachary V, Orfeo T, Mann KG. Prothrombin activation in blood coagulation: the erythrocyte contribution to thrombin generation. Blood. 2012;120(18):3837–45. doi: 10.1182/blood-2012-05-427856.
   Web of Science ®Google Scholar
• Rother RP, Bell L, Hillmen P, Gladwin MT. The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease. JAMA. 2005;293(13):1653–62. doi:10.1182/blood-2012-05-427856.
   PubMed Web of Science ®Google Scholar
• Camus SM, De Moraes JA, Bonnin P, Abbyad P, Le Jeune S, Lionnet F, Loufrani L, Grimaud L, Lambry J-C, Charue D, et al. Circulating cell membrane microparticles transfer heme to endothelial cells and trigger vasoocclusions in sickle cell disease. Blood. 2015;125(24):3805–14. doi:10.1182/blood-2014-07-589283.
   PubMed Web of Science ®Google Scholar
• Davenport RD. Pathophysiology of hemolytic transfusion reactions. Semin Hematol. 2005;42(3):165–8. doi:10.1053/j.seminhematol.2005.04.006.
   Web of Science ®Google Scholar
• Malaguarnera L, Madeddu R, Palio E, Arena N, Malaguarnera M. Heme oxygenase-1 levels and oxidative stress-related parameters in non-alcoholic fatty liver disease patients. J Hepatol. 2005;42(4):585–91. doi:10.1016/j.jhep.2004.11.040.
   PubMed Web of Science ®Google Scholar
• Ruiz S, Pergola PE, Zager RA, Vaziri ND . Targeting the transcription factor Nrf2 to ameliorate oxidative stress and inflammation in chronic kidney disease . Kidney Int. 2013;83(6):1029–41. doi:10.1038/ki.2012.439.
   PubMed Web of Science ®Google Scholar
• Bradford MM. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72(1-2):248–54. doi:10.1016/0003-2697(76)90527-3.
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680–5. doi:10.1038/227680a0.
   PubMed Web of Science ®Google Scholar
• Leach BS, Collawn JF, Fish WW . Behavior of glycopolypeptides with empirical molecular weight estimation methods. 1. In sodium dodecyl sulfate. Biochemistry. 1980;19(25):5734–41. doi:10.1021/bi00566a012.
   Web of Science ®Google Scholar
• Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxidation in animal tissue by thiobarbituric acid reaction. Anal Biochem. 1979;95(2):351–8. doi:10.1016/0003-2697(79)90738-3.
   PubMed Web of Science ®Google Scholar
• Levine RL, Garland D, Oliver CN, Amici A, Climent I, Lenz AG. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol. 1951;186:464–78. doi:10.1016/0076-6879(90)86141-H.
   Google Scholar
• Quick AJ, Stanley-Brown M, Bancroft FW. A study of the coagulation defect in haemophilia and in jaundice. Am J Med Sci. 1935;90:501–11. doi:10.1055/s-0038-1650068
   Google Scholar
• Ardlie NG, Han P. Enzymatic basis for platelet aggregation and release: the significance of the ‘platelet atmosphere’ and the relationship between platelet function and blood coagulation. Br J Haematol. 1974;26(3):331–56. doi:10.1111/j.1365-2141.1974.tb00477.
   Web of Science ®Google Scholar
• Born GV. Aggregation of blood platelets by adenosine diphosphate and its reversal. Nature. 1962;194:927–9. doi:10.1038/194927b0.
   PubMed Web of Science ®Google Scholar
• Vishwanath BS, ManajnathaKini R, Veerabasappagowda T. Characterization of three edema-inducing phospholipase A2 enzyme from habu (Trimeresurusflavoviridis) venom and their interaction with the alkaloid arisatolochic acid. Toxicon. 1987;25:501–15. doi:10.1016/0041-0101(87)90286-8.
   PubMed Web of Science ®Google Scholar
• Kondo H, Kondo S, Itezawa H, Murata R, Ohasaka A . Studies on the quantitative method for determination of hemorrhagic activity of Habu snake venom. Jpn J Med Sci Biol. 1960;13:43–51. doi:10.7883/yoken1952.13.43.
   PubMedGoogle Scholar
• Angelo DA, Hansen KC, Eisenmesser EZ, Zimring JC. Protect, repair, destroy or sacrifice: a role of oxidative stress biology in inter-donor variability of blood storage? Blood Transfus. 2019;17(4):281–8. doi:10.2450/2019.0072-19.
   Web of Science ®Google Scholar
• Agrawal H, Joshi R, Gupta M. Isolation, purification and characterisation of antioxidative peptide of pearl millet (Pennisetum glaucum) protein hydrolysate. Food Chem. 2016;204:365– 136. doi:10.1016/j.foodchem.2016.02.127.
   PubMed Web of Science ®Google Scholar
• Ramana T, Radhakrishnan TM. Denovo synthesis of protease during germination of pearl millet seeds. Current Science. 1987;56(9):397–400.
   Web of Science ®Google Scholar
• Sehgal Kwatra AS. A. Nutritional evaluation of pearl millet based sponge cake. J Food Sci Technol. 2006;43:312–3.
   Web of Science ®Google Scholar
• Malik M, Singh U, Dahiya S. Nutrient composition of pearl millet as influenced by genotypes and cooking methods. J Food Sci,Technol. 2002;39:463–8.
   Web of Science ®Google Scholar
• Jayanna K, Nandish M, Chethana R, Chandramma S, Ashwini S, Vishalakshi GJ, Paul M, Santhosh S, Shankar RL, Devaraja S. Protective effect of tamarind seed coat ethanol extract on eryptosis induced by oxidative stress. Biochemistry (Moscow). 2020; 85(1):119–29. doi:10.1134/S0006297920010113.
   Web of Science ®Google Scholar
• Lang F, Lang KS, Lang PA, Huber SM, Wieder T. Mechanisms and significance of eryptosis. Antioxid Redox Signal. 2006;8(7-8):1183–92. doi:10.1089/ars.2006.8.1183.
   PubMed Web of Science ®Google Scholar
• Andrisic L, Dudzik D, Barbas C, Milkovic L, Grune T, Zarkovic N . Short overview on metabolomics approach to study pathophysiology of oxidative stress in cancer. Redox Biol. 2018;14:47–58. doi:10.1016/j.redox.2017.08.009.
   Web of Science ®Google Scholar
• Grinberg L, Newmark H, Kitrossky N, Rahamim E, Chevion M, Rachmilewitz E. Protective effects of tea polyphenols against oxidative damage to red blood cells. Bioche Pharma. 1997;54(9):973–8. doi:10.1016/S0006-2952(97)00155-X.
   PubMed Web of Science ®Google Scholar
• Ratliff BB, Abdulmahdi W, Pawar R, Wolin MS. Oxidant mechanisms in renal injury and disease. Antioxid Redox Signal. 2016;25(3):119–46. doi:10.1089/ars.2016.6665.
   PubMed Web of Science ®Google Scholar
• Kanias T, Stone M, Page GP, Guo Y, Endres‐Dighe SM, Lanteri MC, Spencer BR, Cable RG, Triulzi DJ, Kiss JE, et al. Frequent blood donations alter susceptibility of red blood cells to storage- and stress-induced hemolysis. Transfusion. 2019;59(1):67–78. doi:10.1111/trf.14998.
   Web of Science ®Google Scholar
• Asadi H, Yan B, Dowling R, Wong S, Mitchell P . Advances in medical revascularisation treatments in acute ischemic stroke. Thrombosis. 2014;1–14. doi:10.1155/2014/714218.
   Google Scholar
• Drake TA, Morrissey JH, Edgington TS. Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. Am J Pathol. 1989;134(5):1087–1097.
   PubMed Web of Science ®Google Scholar
• Sims PJ, Wiedmer T, Esmon CT, Weiss HJ, Shattil SJ. Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. J Biol Chem. 1989;264(29):17049–17057.
   PubMed Web of Science ®Google Scholar
• Cimen MY. Free radical metabolism in human erythrocytes. Clin Chim Acta. 2008;390(1-2):1–1. doi:10.1016/j.cca.2007.12.025.
   PubMed Web of Science ®Google Scholar
• Devaraja S, Girish KS, Gowtham YJM, Kemparaju K. The Hag-protease-II is a fibrin(ogen)ase from Hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis. Toxicon. 2011;57(2):248–258. doi:10.1016/j.toxicon.2010.11.018.
   PubMed Web of Science ®Google Scholar
• Devaraja S, Nagaraju S, Mahadeswaraswamy YH, Girish KS, Kemparaju K. A low molecular weight serine protease: purification and characterization from Hippasa agelenoides (Funnel web) spider venom gland extract. Toxicon. 2008;52(1):130–138. doi:10.1016/j.toxicon.2008.04.168
   PubMed Web of Science ®Google Scholar
• Nandish SK, Kengaiah J, Ramachandraiah C, Shivaiah A, Chandramma, Girish KS, DS. Anticoagulant, antiplatelet and fibrin clot hydrolysing activities of flax seed buffer extract. Phcog Mag. 2018;14:175–183. doi:10.4103/pm.pm_320_17.
   Google Scholar
• Astrup T. The haemostatic balance. Thromb Diath Haemorrh. 1958;2(3-4):347–357. doi:10.1055/s-0038-1656192.
   Google Scholar
• Lewis SD, Janus TJ, Lorand L, Shafer JA. Regulation of formation of factor XIIIa by its fibrin substrates. Biochemistry. 1985;24(24):6772–6777. doi:10.1021/bi00345a007.
   Web of Science ®Google Scholar
• Sowmyashree G, Bhagyalakshmi M, Girish KS, Kemparaju K, Rangaiah SM, Jane HP. Jackfruit (Artocarpush eterophyllus) seed extract exhibits fibrino (geno)lytic activity. Pharmacogn J. 2015;7:171–177. doi:10.5530/pj.2015.3.5
   Google Scholar
• Bhagyalakshmi M, Sowmyashree G, Kesturu GS, Kempaiah K, Sathish JG. Momordica charantia seed extract exhibits strong anticoagulant effect by specifically interfering in intrinsic pathway of blood coagulation and dissolves fibrin clot. Blood Coagulation Fibrinolysis. 2015;26:191–199. doi:10.1097/MBC.0000000000000191.
   Web of Science ®Google Scholar