Welcome to Open Science
Contact Us
Home Books Journals Submission Open Science Join Us News
Inhibition Studies of RNase a in Invitro Condition by Drug Metosartan
Current Issue
Volume 6, 2018
Issue 4 (August)
Pages: 34-38   |   Vol. 6, No. 4, August 2018   |   Follow on         
Paper in PDF Downloads: 20   Since Sep. 3, 2018 Views: 850   Since Sep. 3, 2018
Eswari Beeram, Department of Biochemistry, Sri Venkateswara University, Tirupati, India.
RNase A is majorly involved in efficient cleavage of single-stranded RNA, double-stranded RNA and double-stranded RNA-DNA hybrids, digestion of dietary RNA, regulation of vascular homeostasis, inactivation of the HIV, activation of immature dendritic cells and induction of cytokine production; and furthermore shows potential as an anti-tumor agent. So, identification of potent inhibitors of the enzyme is necessary for better understanding of deviation in gene regulation. In this study metosartan inhibitory effect on RNase A was studied by simple technique UV- Visible spectroscopy and the A260/280 ratio was calculated to know the potentiality of drug on enzyme which is shown as degradation of RNA. Proteinase K along with SDS and EDTA was used to stop the reaction. Drug metosartan inhibits RNase A exactly between 3rd and 4th hr and the enzyme regains its activity after 4th hr. However the drug effect on RNase A in invivo condition was not studied and from the reports up to now it can be use as inhibitor of RNase A in biological preparations and also as cancer therapeutic drug as it causes apoptosis in normal tissues.
Proteinase K, EDTA, Metosartan, Telmisartan and Metoprolol
Claudi, M., Victòria, N. M., and Ronald Raines T., (2011) Bovine Pancreatic Ribonuclease: 50 Years of the First Enzymatic Reaction Mechanism NIH Public Access Biochemistry.; 50 (37): 7835–7841. doi: 10.1021/bi201075b.
Chang J. Y., (2011) Folding of Disulfide Proteins Protein reviews 14, springer, Vol 14, pp. X, 286 Springer- Verlag New York
June M. Messmore, Dana N. Fuchs, and Ronald T. Raines (1995). Ribonuclease A: Revealing Structure–Function Relationships with Semisynthesis. J Am Chem Soc.; 117 (31): 8057–8060.
National Institute of Drug Abuse (2010). Prescription Drugs: Abuse and Addiction. Report Research Series.
Subodh K., (2006) Spectroscopy of Organic Compounds by PS Kalsi. Dept. of Chemistry Guru Nanak Dev University Amritsar -143005
Jesus Fominaya, M., and Hofsteenge, J., (1992). Inactivation of Ribonuclease Inhibitor by Thiol-disulfide Exchange J. Biol. Chem. Vol. 267, No. 34, pp. 24655-24660.
Jinghao Sheng and Zhengping Xu (2016). Three decades of research on angiogenin: a review and perspective Acta Biochim Biophys Sin, 48 (5), 399–410.
Jörg Haupenthal, Christina Baehr, Simone Kiermayer, Stefan Zeuzem, Albrecht Piiper, (2006). Inhibition of RNAse family enzymes prevents degradation and loss of silencing activity of siRNAs in serum, Biochemical Pharmacology, Volume 71, Issue 5, Pages 702-710
Frank S. Lee, Robert Shapiro, and Bert L. ValleeTight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitorBiochemistry, 1989, 28 (1), pp 225–230
Conner C. Earl a, Mark T. Smitha, Richard A. Lease b, and Bradley C. Bundy (2018). Polyvinylsulfonic acid: A Low-cost RNase inhibitor for enhanced RNA preservation and cell-free protein translation BIOENGINEERED, VOL. 9, NO. 1, 90–97.
Mendelsohn SL, Young DA. (1978). Inhibition of ribonuclease. Efficacy of sodium dodecyl sulfate, diethyl pyrocarbonate, protein ase K and heparin using a sensitive ribonuclease assay. Biochim Biophys Acta.; 5 19 (2): 461-73
Kaustav Chakraborty, Swagata Dasgupta andTanmaya Pathak (2015). Carboxylated Acyclonucleosides: Synthesis and RNase A Inhibition. Molecules, 20 (4), 5924-5941
Benjamin M. Fontaine, Kevin S. Martin, Jennifer M. Garcia-Rodriguez, Claire Jung, Laura Briggs, Jessica E. Southwell, Xin Jia, Emily E. Weinert (2018). RNase I Regulates E. coli 2',3'-Cyclic Nucleotide Monophosphate Levels and Biofilm Formation. Biochemical Journal, BCJ20170906; DOI: 10.1042/BCJ20170906.
Nadezhda Mironova, Olga Patutina, Evgenyi Brenner, Alexander Kurilshikov, Valentin Vlassov and Marina Zenkova (2017). The systemic tumor response to RNase A treatment affects the expression of genes involved in maintaining cell malignancy Oncotarget, Vol. 8, (No. 45), pp: 78796-78810.
Elena Lomonosova, Adam Zlotnick, John E. Tavis (2017). Synergistic Interactions between Hepatitis B Virus RNase H Antagonists and Other Inhibitors Antimicrobial Agents and Chemotherapy, Volume 61 Issue 3 e02441-16.
Vijaykumar Chennupati, Trang Hoang, Ramanjaneyulu Allam (2018). Ribonuclease inhibitor 1 regulates erythropoiesis by controlling GATA1 translation. J Clin Invest.; 128 (4): 1597-1614.
Maxim V. Gerashchenko Vadim N. Gladyshev (2017). Ribonuclease selection for ribosome profiling Nucleic Acids Research, Vol 45, 2 (25), Pages e6.
Huimin Duan, Leilei Li, Xiaojiao Wang, Yanhui Wang, Jianbo Li and Chuannan Luo (2015). Biorecognition and highly sensitive determination of Ribonuclease A with chemiluminescence sensor based on Fe3O4/multi- walled carbon nanotubes/SiO2-surface molecular imprinting polymer, RSC advances; issue 24.
Jay S. Roth Studies on the Inactive Ribonuclease in the supernatant fraction of rat liver (1957). Journal of biological chemistry
Eswari Beeram (2017) INHIBITION OF RNase BY DRUG METOSARTAN IN TESTIS TISSUE International Journal of Recent Scientific Research Vol. 8, Issue, 6, pp. 17394- 17395.
Deepak Gaur, Janendra K. Batra (2005). Role of aspartic acid 121 in human pancreatic ribonuclease catalysis Molecular and cellular Biochemistry, 275 (1-2); pp 95-101.
Kover, K. E., Bruix, M., Santoro, J., Batta, G., Laurents, D. V., Rico, M. (2008) The solution structure and dynamics of human pancreatic ribonuclease determined by NMR spectroscopy provide insight into its remarkable biological activities and inhibition. J. Mol. Biol. 379: 953-965
Thomas Schirrmann, André Frenzel, Lars Linden, Beatrix Stelte-Ludwig, Jörg Willuda, Axel Harrenga, Stefan Dübel, Beate Müller-Tiemann, and Mark Trautwein (2014). Evaluation of human pancreatic RNase as effector molecule in a therapeutic antibody platform, mAbs 6: 2, 367–380.
Yang Wei, Aby A. Thyparambil, Yonnie Wu, and Robert A. (2014). Latour Adsorption-Induced Changes in Ribonuclease A Structure and Enzymatic Activity on Solid Surfaces Langmuir, 30 (49), pp 14849–14858.
Kanwar SS and Kumar R (2017). Ribonuclease as Anticancer Therapeutics Enz Eng, 6: 1
Krasniqi B, Lee JS (2014) RNase A Does Not Translocate the Alpha-Hemolysin Pore. PLoS ONE 9 (2): e88004. doi: 10.1371/journal.pone.0088004
Makiko Tanaka, Narumi Shigi, and Makoto Komiyama (2016) Ribonuclease A as Effective Promoter for Unimolecular Invasion of Peptide Nucleic Acid to Double-stranded DNA Vol. 45, No. 7, 767-769
Eswari Beeram and Thyagaraju Kedam (2018) Apoptosis of testis tissue by drug metosartan through activation of intrinsic pathway by the release of Cyt C from mitochondria International Journal of Chemical Studies 2018; 6 (1): 614-617.
Open Science Scholarly Journals
Open Science is a peer-reviewed platform, the journals of which cover a wide range of academic disciplines and serve the world's research and scholarly communities. Upon acceptance, Open Science Journals will be immediately and permanently free for everyone to read and download.
Office Address:
228 Park Ave., S#45956, New York, NY 10003
Phone: +(001)(347)535 0661
Copyright © 2013-, Open Science Publishers - All Rights Reserved