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Initiatives taken by the international organizations towards better health

September 2015. The goals include world s urgent issues that should be solved over the next 15 years by the all countries - developed and developing - in a global partnership (146). SDGs are the blueprint to achieve a better and more sustainable future for all.

They address the global challenges we face, including those related to ending poverty, reducing inequality, improving health and education. The WHO also gave commitment to help the world meet the SDGs by championing health across all the goals. WHO core mission is to promote health, alongside keeping the world safe and serving the vulnerable. Beyond fighting disease, they will work to ensure healthy lives and promote

wellbeing for all at all ages, leaving no-one behind. WHO has targeted 1 billion more people to enjoy better health and well-being by 2023.

Tackling noncommunicable diseases like CVDs, cancer, chronic respiratory diseases, diabetes (124), through the reduction of exposure to hazardous environmental and occupational risks is essential in achieving the SDGs, notably, SDG3. The health goal, SDG3 is to ensure healthy lives and promote well-being at all ages. Health target 3.4, related to SDG3, aims to reduce premature mortality from noncommunicable diseases, through prevention and treatment, by one third by 2030.

Effective strategies can be undertaken by the policy makers and associated bodies only when they are able to recognize the effects of environmental factors, e.g. heavy metals, at molecular level (Fig. 3.6). I hope that the review topic discussed in the later part of this thesis will get people to reconsider the strategy to prevent CVDs by improving the environment. As we all know prevention is better than cure.

Acknowledgements

Firstly, I would like to take the opportunity to express the deepest appreciation and my sincere gratitude to my benevolent supervisor Dr. Akio Ebihara, Professor, Laboratory of Biological Chemistry, Faculty of Applied Biological Sciences, Gifu University, Japan for the continuous support of my Ph.D. study and related research, for his patience, motivation, and immense knowledge. His guidance helped me in all the time of research and writing of this thesis. I could not have imagined having a better advisor and mentor for my Ph.D. study.

Besides my supervisor, I would like to thank Dr. Tsutomu Nakagawa, Professor, Laboratory of Biological Chemistry, Faculty of Applied Biological Sciences, Gifu University, Japan and Dr. Akio Morita, Professor, Laboratory of Functional Plant Physiology, Shizuoka University, Japan for not only their insightful comments and encouragement as co-supervisors, but also for the constructive criticism which incented me to widen my research from various perspectives.

I owe a debt of gratitude to Dr. AHM Nurun Nabi, Professor, Department of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh for his motivation and assistance to pursue higher study in a foreign university. He is one of my Ph.D. co-supervisors and was my M.S. thesis supervisor also. Whenever I had faced any difficulties, I directly contacted him. His words inspired me to start my work with new spirit. I will always remain grateful to him.

I must express my gratefulness to Dr. Fumiaki Suzuki, Vice President and Executive Director for International Affairs and Public Relations, Gifu University, Japan who is one of the founders of the Laboratory of Biological Chemistry, Gifu University. He was often present during my midterm presentations in spite of his busy schedule. My Ph.D.

life would become harder without his guideline and valuable advices.

I would like to express my sincere thanks to Dr. Masateru Senge, Professor and Dean, The United Graduate School of Agricultural Science, Gifu University; and Dr. Kohei Nakano, Associate Dean, The United Graduate School of Agricultural Science, Gifu University for allowing me to pursue my doctoral course in their faculty.

I thank Dr. Atsuhiro Shimada, Dr. Misuzu Hashimoto and Dr. Chiharu Nakagawa for

their continuous support and constructive criticism. I also express my thanks to Miss Mayumi Matsui and Ms. Jyunko Mikami for their useful assistance over the study period. I am indebted to my fellow lab mates in the Laboratory of Biological Chemistry for their supports, the stimulating discussions, and for all the fun we have had in the last three years. Few names I must mention are- Miss Maki Kuzuya, Mr. Rui Zhang, Miss Midori Yui, Miss Hiromi Suzuki, Mr. Kota Onoda, Mr. Motoki Sugino, Mr. Seidai Nagai and Mr. Makoto Kousaka.

I would like to convey my gratitude to Dr. Laila N Islam, Professor, Department of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh for allowing me to use the laboratory space and instruments during my M.S. research activities. My sincere gratitude also goes to all the teachers of Department of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh for sharing their knowledge with the students and making them ambitious.

I would also like to thank all the professors of the United Graduate School of Agricultural Science, Gifu University for their valuable lectures, discussions and suggestions. I wish to thank all the office staffs of the United Graduate School of Agricultural Science for their sincere and unconditional help during my research period.

I also thank Ministry of Education, Science, Sports and Culture, Government of Japan for awarding me Monbukagakusho Scholarship to support my research and daily life in Japan.

My thanks go to Dr. Kazal Boron Biswas, former Postdoc and Ph.D. student of the Laboratory of Biological Chemistry and his wife Swapna Paramanya who was not only my lab mate but also like elder sister for their constant support, providing me homely environment and making my Japan life pleasant. I will miss their son Karnik Biswas a lot. I also thank all of Japanese and Bangladeshi friends who made me feel a pleasant time in Japan.

I humbly extend my thanks to my family: my father, who is not with us but has been always supporting me spiritually, my mother, sisters, brother, all the relatives and in- for supporting me throughout writing this thesis and all the blessings towards me. Last but not the least, I want to thank my beloved husband, Dr. MD. Emon Hossain for his continuous support, inspiration, untiring patience and love in my life.

References

(1) (2005).

Angiotensin-converting enzyme inhibitors or angiotensin receptor blockers for prevention of type 2 diabetes: a meta-analysis of randomized clinical trials. J. Am.

Coll. Cardiol., 46, 821 826.

(2) Achparaki, M., Thessalonikeos, E., Tsoukali, H., Mastrogianni, O., Zaggelidou, E., Chatzinikolaou, F., Vasilliades, N., and Raikos, N. (2012). Heavy metals toxicity . Aristotle Univ. Med. J., 39, 29 34.

(3) Admiraal, P.J., Derkx, F.H., Danser, A.H., Pieterman, H., and Schalekamp, M.A.

(1990). Metabolism and production of angiotensin I in different vascular beds in subjects with hypertension. Hypertension, 15, 44 55.

(4) Akther, J., Ebihara, A., Nakagawa, T., Islam, L.N., Suzuki, F., Hosen, M.I., Hossain, M., and Nabi, A.H.M.N. (2016). Analyses of genetic variations of glutathione S-transferase Mu1 and theta1 genes in Bangladeshi tannery workers and healthy controls. Biomed Res. Int., 2016.

(5) Akther, J., Nurun Nabi, A.H.M., Ohno, S., Yokogawa, T., Nakagawa, T., Suzuki, F., Ebihara, A., and Nabi, A.H.M.N. (2019). Establishing a novel assay system for measuring renin concentration using cost effective recombinant ovine angiotensinogen. Heliyon, 5, 1409.

(6) Alderman, M.H., Ooi, W.L., Cohen, H., Madhavan, S., Sealey, J.E., and Laragh, J.H. (1997). Plasma renin activity: A risk factor for myocardial infarction in hypertensive patients. Am. J. Hypertens., 10, 1 8.

(7) Ali, F., Habiba, U., Naher, B., Chowdhury, A.M.S.U., and Rahman, G.M.S.

(2015). Investigation on Physicochemical Parameters of Tannery Effluent. J.

Environ. Res. Technol., 5, 122 130.

(8) Alissa, E.M., and Ferns, G.A. (2011). Heavy metal poisoning and cardiovascular disease. J. Toxicol., 2011.

(9) Alli, L.A. (2015). Blood level of cadmium and lead in occupationally exposed persons in Gwagwalada, Abuja, Nigeria. Interdiscip. Toxicol., 8, 146 150.

(10) Ambreen, K., Khan, F.H., Bhadauria, S., and Kumar, S. (2014). Genotoxicity and oxidative stress in chromium-exposed tannery workers in North India. Toxicol.

Ind. Health, 30, 405 414.

(11) Angeli, J.K., Cruz Pereira, C.A., de Oliveira Faria, T., Stefanon, I., Padilha, A.S., and Vassallo, D.V. (2013). Cadmium exposure induces vascular injury due to endothelial oxidative stress: the role of local angiotensin II and COX-2. Free Radic. Biol. Med., 65, 838 848.

(12) Antonia, C. (2008). Possible Role of Oxidative Stress in the Pathogenesis of Hypertension. Diabetes Care, 31, 5181 5184.

(13) Arner, E.S., and Holmgren, A. (2000). Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem., 267, 6102 6109.

(14) Atlas, S.A. (2007). The renin-angiotensin aldosterone system: pathophysiological role and pharmacologic inhibition. J. Manag. Care Pharm., 13, 9 20.

(15) ATSDR. (2007). ToxGuide for arsenic as CAS # 7440-38-2, Agency for Toxic Substances and Disease Registry.

(16) ATSDR. (2012). Toxicological Profile for Chromium, Agency for Toxic Substances and Diseases Registry, US Department of Health and Human Services, Public Health Service, Atlanta, GA.

(17) Bahorun, T., Soobrattee, M.A., Luximon-Ramma, V., and Aruoma, O.I. (2006).

Free radicals and antioxidants in cardiovascular health and disease. Internet J.

Med. Updat., 1, 25 41.

(18) Bajpai, M., and Singh, A. (2013). Plasma renin activity: An early marker of progressive renal disease in posterior urethral valves. J. Indian Assoc. Pediatr.

Surg., 18, 143.

(19) Barrera, G. (2012). Oxidative Stress and Lipid Peroxidation Products in Cancer

Progression and Therapy. ISRN Oncol., 2012, 1 21.

(20) Bautista, L.E., Stein, J.H., Morgan, B.J., Stanton, N., Young, T., and Nieto, F.J.

(2009). Association of blood and hair mercury with blood pressure and vascular reactivity. WMJ, 108, 250 252.

(21) Benson, S.C., Pershadsingh, H.A., Ho, C.I., Chittiboyina, A., Desai, P., Pravenec, M., Qi, N., Wang, J., Avery, M.A., and Kurtz, T.W. (2004). Identification of telmisartan as a unique angiotensin II receptor antagonist with selective PPARgamma-modulating activity. Hypertension, 43, 993 1002,

(22) Betteridge, D.J. (2000). What is oxidative stress? Metabolism., 49, 3 8.

(23) Bhatnagar, A. (2004). Cardiovascular pathophysiology of environmental pollutants. Am. J. Physiol. Circ. Physiol., 286, H479 H485.

(24) Biswas, S., and Rahman, T. (2013).

Health in a Tannery in Bangladesh. Adv. Anthropol., 03, 46 53.

(25) Bonsignore, M., Andolfi, N., Barra, M., Madeddu, A., Tisano, F., Ingallinella, V., Castorina, M., and Sprovieri, M. (2016). Assessment of mercury exposure in human populations: A status report from Augusta Bay (southern Italy). Environ.

Res., 150, 592 599.

(26) Boscolo, P., and Carmignani, M. (1988). Neurohumoral blood pressure regulation in lead exposure. Environ. Health Perspect., 78, 101 106.

(27) Bradl, H.B. (2005). Heavy Metals in the Environment: Origin, Interaction and Remediation. Elsevier, 6.

(28) Brigelius-Flohe, R. (1999). Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med., 27, 951 965.

(29) Brook, R.D., Franklin, B., Cascio, W., Hong, Y., Howard, G., Lipsett, M., Luepker, R., Mittleman, M., Samet, J., and Smith Jr, S.C. (2004). Air pollution and cardiovascular disease: a statement for healthcare professionals from the Expert Panel on Population and Prevention Science of the American Heart

Association. Circulation, 109, 2655 2671.

(30) Campbell, D.J., Nussberger, J., Stowasser, M., Danser, A.H.J., Morganti, A., Frandsen, E., and Ménard, J. (2009). Activity assays and immunoassays for plasma renin and prorenin: Information provided and precautions necessary for accurate measurement. Clin. Chem., 55, 867 877.

(31) Carey, R.M., and Siragy, H.M. (2003). Newly recognized components of the renin-angiotensin system: potential roles in cardiovascular and renal regulation.

Endocr. Rev., 24, 261 271.

(32) Carlsson, P.-O., Berne, C., and Jansson, L. (1998). Angiotensin II and the endocrine pancreas: effects on islet blood flow and insulin secretion in rats.

Diabetologia, 41, 127 133.

(33) Carmignani, M., Boscolo, P., Poma, A., and Volpe, A.R. (1999). Kininergic system and arterial hypertension following chronic exposure to inorganic lead.

Immunopharmacology, 44, 105 110.

(34) Caruso-Neves, C., Kwon, S.-H., and Guggino, W.B. (2005). Albumin endocytosis in proximal tubule cells is modulated by angiotensin II through an AT2 receptor-mediated protein kinase B activation. Proc. Natl. Acad. Sci., 102, 17513 17518.

(35) Casalino, E., Sblano, C., and Landriscina, C. (1997). Enzyme activity alteration by cadmium administration to rats: the possibility of iron involvement in lipid peroxidation. Arch. Biochem. Biophys., 346, 171 179.

(36) Catena, C., Colussi, G.L., Nadalini, E., Chiuch, A., Baroselli, S., Lapenna, R., and Sechi, L.A. (2007). Relationships of plasma renin levels with renal function in patients with primary aldosteronism. Clin. J. Am. Soc. Nephrol., 2, 722 731.

(37) Cervantes Gracia, K., Llanas-Cornejo, D., and Husi, H. (2017). CVD and Oxidative Stress. J. Clin. Med., 6, 22.

(38) Chatterjee, M., Saluja, R., Kanneganti, S., Chinta, S., and Dikshit, M. (2007).

Biochemical and molecular evaluation of neutrophil NOS in spontaneously

hypertensive rats. Cell. Mol. Biol., 53, 84.

(39) Chaudhary, K., Promsote, W., Ananth, S., Veeranan-Karmegam, R., Tawfik, A., Arjunan, P., Martin, P., Smith, S.B., Thangaraju, M., Kisselev, O., Ganapathy, V., and Gnana-Prakasam, J.P. (2018). Iron Overload Accelerates the Progression of Diabetic Retinopathy in Association with Increased Retinal Renin Expression.

Sci. Rep., 8, 3025.

(40) Chiba, M., Shinohara, A., Matsushita, K., Watanabe, H., and Inaba, Y. (1996).

Indices of lead-exposure in blood and urine of lead-exposed workers and concentrations of major and trace elements and activities of SOD, GSH-Px and catalase in their blood. Tohoku J. Exp. Med., 178, 49 62.

(41) Chin-Thin, W., Wei-Tun, C., Tzu-Ming, P., and Ren-Tse, W. (2002). Blood concentrations of selenium, zinc, iron, copper and calcium in patients with hepatocellular carcinoma. Clin. Chem. Lab. Med., 40, 1118 1122.

(42) Chowdhury, R., Lawrence, R., van Daalen, K., Hawkes, S., and Feldmann, J.

(2018). Reducing NCDs globally: the under-recognised role of environmental risk factors. Lancet, 392, 212.

(43) Chowdhury, R., Ramond

Muka, T., Gregson, J., Willeit, P., Warnakula, S., Khan, H., Chowdhury, S., Gobin, R., Franco, O.H., and Di Angelantonio, E. (2018). Environmental toxic metal contaminants and risk of cardiovascular disease: Systematic review and meta-analysis. BMJ, 362, 14 16.

(44) Colacino, J.A., Arthur, A.E., Ferguson, K.K., and Rozek, L.S. (2014). Dietary antioxidant and anti-inflammatory intake modifies the effect of cadmium exposure on markers of systemic inflammation and oxidative stress. Environ.

Res., 131, 6 12.

(45) Cooper, S.A., Whaley-Connell, A., Habibi, J., Wei, Y., Lastra, G., Manrique, C., Stas, S., and Sowers, J.R. (2007). Renin-angiotensin-aldosterone system and oxidative stress in cardiovascular insulin resistance. Am. J. Physiol. Circ.

Physiol., 293, H2009 H2023.

(46) Cosselman, K.E., Navas-Acien, A., and Kaufman, J.D. (2015). Environmental Factors in Cardiovascular Disease Doctoral Thesis [Online]. Nat. Rev. Cardiol., 12, 627 642.

(47) Deinum, J., Derkx, F.H.M., and Schalekamp, M.A.D.H. (1999). Improved immunoradiometric assay for plasma renin. Clin. Chem., 45, 847 854.

(48) Derkx, F.H.M., De Bruin, R.J.A., Van Gool, J.M.G., Van Den Hoek, M.J., Beerendonk, C.C.M., Rosmalen, F., Haima, P., and Schalekamp, M.A.D.H.

(1996). Clinical validation of renin monoclonal antibody-based sandwich assays of renin and prorenin, and use of renin inhibitor to enhance prorenin immunoreactivity. Clin. Chem., 42, 1051 1063.

(49) Dhalla, N.S., Temsah, R.M., and Netticadan, T. (2000). Role of oxidative stress in cardiovascular diseases. J. Hypertens., 18, 655 673.

(50) Do, Y.S., Shinagawa, T., Tam, H., Inagami, T., and Hsueh, W.A. (1987).

Characterization of pure human renal renin. Evidence for a subunit structure. J.

Biol. Chem., 262, 1037 1043.

(51) Droge, W. (2002). Free radicals in the physiological control of cell function.

Physiol. Rev., 82, 47 95.

(52) Dzau, V.J., Colucci, W.S., Hollenberg, N.K., and Williams, G.H. (1981).

Relation of the renin-angiotensin-aldosterone system to clinical state in congestive heart failure. Circulation, 63, 645 651.

(53) Ebihara, A., Kondou, T., Mizuno, S., Nakagawa, T., Nasir, U.M., Inui, Y., Fukamizu, A., Suzuki, F., Nakamura, Y., and Murakami, K. (2000). Molecular properties of recombinant ovine angiotensinogen. Biomed. Res., 21, 247 254.

(54) Ebihara, A., Nasir, U.M., Yoshida, S., Kondou, T., Nakagawa, T., Fukamizu, A., Suzuki, F., Nakamura, Y., and Murakami, K. (2000). Sialic acid residue of ovine angiotensinogen does not affect the reactivity to human renin. Biomed. Res., 21, 105 109.

(55) Ferrario, C.M. (2006). Role of angiotensin II in cardiovascular disease

therapeutic implications of more than a century of research. J.

Renin-Angiotensin-Aldosterone Syst., 7, 3 14.

(56) Fleischer, N., Mouw, D.R., and Vander, A.J. (1980). Chronic effects of lead on renin and renal sodium excretion. Transl. Res., 95, 759 770.

(57) Flora, S.J.S., Bhadauria, S., Kannan, G.M., and Singh, N. (2007). Arsenic induced oxidative stress and the role of antioxidant supplementation during chelation: a review. J. Environ. Biol., 28, 333 347.

(58) Floyd, R.A., and Lewis, C.A. (1983). Hydroxyl Free Radical Formation from Hydrogen Peroxide by Ferrous Iron-Nucleotide Complexes. Biochemistry, 22, 2645 2649.

(59) Forrester, S.J., Booz, G.W., Sigmund, C.D., Coffman, T.M., Kawai, T., Rizzo, V., Scalia, R., and Eguchi, S. (2018). Angiotensin II Signal Transduction: An Update on Mechanisms of Physiology and Pathophysiology. Physiol. Rev., 98, 1627 1738.

(60) Frassetto, L., Morris, R.C.J., Sellmeyer, D.E., Todd, K., and Sebastian, A. (2001).

Diet, evolution and aging--the pathophysiologic effects of the post-agricultural inversion of the potassium-to-sodium and base-to-chloride ratios in the human diet. Eur. J. Nutr., 40, 200 213.

(61) Freis, E.D. (1974). The Veterans Administration cooperative study on antihypertensive agents. Implications for stroke prevention. Stroke, 5, 76 77.

(62) Fridovich, I. (1997). Superoxide anion radical (O· 2), superoxide dismutases, and related matters. J. Biol. Chem., 272, 18515 18517.

(63) Frohlich, E.D. (1999). Risk mechanisms in hypertensive heart disease.

Hypertension, 34, 782 789,

(64) Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D., and Bairoch, A. (2005). The Proteomics Protocols Handbook. In: The Proteomics Protocols Handbook, p. 571 605.

(65) Gil, F., Hernández, A.F., Márquez, C., Femia, P., Olmedo, P., López-Guarnido, O., and Pla, A. (2011). Biomonitorization of cadmium, chromium, manganese, nickel and lead in whole blood, urine, axillary hair and saliva in an occupationally exposed population. Sci. Total Environ., 409, 1172 1180.

(66) Gillespie, E.L., White, C.M., Kardas, M., Lindberg, M., and Coleman, C.I.

(2005). The impact of ACE inhibitors or angiotensin II type 1 receptor blockers on the development of new-onset type 2 diabetes. Diabetes Care, 28, 2261 2266.

(67) Gonzalez, M.C., Cohen, H.W., Sealey, J.E., Laragh, J.H., and Alderman, M.H.

(2011). Enduring direct association of baseline plasma renin activity with all-cause and cardiovascular mortality in hypertensive patients. Am. J. Hypertens., 24, 1181 1186.

(68) Goodfriend, T.L., Elliott, M.E., and Catt, K.J. (1996). Angiotensin receptors and their antagonists. N. Engl. J. Med., 334, 1649 1654.

(69) Goto, T., Imai, N., Hirose, S., and Murakami, K. (1984). An improved method for determination of active and total renin concentration in human plasma using an excess of sheep substrate. Clin. Chim. Acta, 138, 87 98.

(70) Griendling, K.K., and Ushio-Fukai, M. (2000). Reactive oxygen species as mediators of angiotensin II signaling. Regul. Pept., 91, 21 27.

(71) Hall, M., Chen, Y., Ahsan, H., Slavkovich, V., van Geen, A., Parvez, F., and Graziano, J. (2006). Blood arsenic as a biomarker of arsenic exposure: Results from a prospective study. Toxicology, 225, 225 233.

(72) Halliwell, B. (2011). Free radicals and antioxidants - quo vadis? Trends Pharmacol. Sci., 32, 125 130.

(73) Herr, D., Rodewald, M., Fraser, H.M., Hack, G., Konrad, R., Kreienberg, R., and Wulff, C. (2008). Regulation of endothelial proliferation by the renin-angiotensin system in human umbilical vein endothelial cells. Reproduction, 136, 125.

(74) Herse, F., Dechend, R., Harsem, N.K., Wallukat, G., Janke, J., Qadri, F., Hering, L., Muller, D.N., Luft, F.C., and Staff, A.C. (2007). Dysregulation of the

circulating and tissue-based renin-angiotensin system in preeclampsia.

Hypertension, 49, 604 611.

(75) Higaki, J., Ogihara, T., Imai, N., Kumahara, Y., Hontani, S., Nishiura, M., Ogawa, H., Hirose, S., and Murakami, K. (1984). A new sensitive direct radioimmunoassay for human plasma renin and its clinical application. J. Lab.

Clin. Med., 104, 947 954.

(76) Hitomi, H., Kiyomoto, H., and Nishiyama, A. (2007). Angiotensin II and oxidative stress. Curr. Opin. Cardiol., 22, 311 315.

(77) Hossain, E., Ota, A., Takahashi, M., Karnan, S., Damdindorj, L., Konishi, Y., Konishi, H., and Hosokawa, Y. (2013). Arsenic upregulates the expression of angiotensin II Type I receptor in mouse aortic endothelial cells. Toxicol. Lett., 220, 70 75.

(78) Howe, C.G., Liu, X., Hall, M.N., Slavkovich, V., Ilievski, V., Parvez, F., Siddique, A.B., Shahriar, H., Uddin, M.N., Islam, T., Graziano, J.H., Costa, M., and Gamble, M. V. (2016). Associations between blood and urine arsenic concentrations and global levels of post-translational histone modifications in Bangladeshi men and women. Environ. Health Perspect., 124, 1234 1240.

(79) Hsueh, W.A., Carlson, E.J., and Dzau, V.J. (1983). Characterization of inactive renin from human kidney and plasma. Evidence of a renal source of circulating inactive renin. J. Clin. Invest., 71, 506 517.

(80) Hsueh, W.A., and Wyne, K. (2011). Renin-Angiotensin-Aldosterone System in Diabetes and Hypertension. J. Clin. Hypertens., 13, 224 237.

(81) Hunyady, L., and Catt, K.J. (2006). Pleiotropic AT1 receptor signaling pathways mediating physiological and pathogenic actions of angiotensin II. Mol.

Endocrinol., 20, 953 970.

(82) IARC. (1989). Antimony trioxide and antimony trisulfide. IARC Monogr. Eval.

Carcinog. risks to humans, 47, 291 305.

(83) Inagami, T., Yokosawa, H., and Hirose, S. (1978). Definitive evidence for renin

in rat brain by affinity chromatographic separation from protease. Clin. Sci. Mol.

Med. Suppl., 4, 121s 123s.

(84) Islam, L.N., Nabi, A.H.M.N., Rahman, M.M., Khan, M.A., and Kazi, A.I. (2004).

Association of clinical complications with nutritional status and the prevalence of leukopenia among arsenic patients in Bangladesh. Int. J. Environ. Res. Public Health, 1, 74 82.

(85) Islam, L.N., Nurun Nabi, A.H.M., Rahman, M.M., and Zahid, M.S.H. (2007).

Association of respiratory complications and elevated serum immunoglobulins with drinking water arsenic toxicity in human. J. Environ. Sci. Heal. Part A, 42, 1807 1814.

(86) Islam, L.N., Zahid, M.S.H., Nabi, A.H.M.N., and Hossain, M. (2012). Function of serum complement in drinking water arsenic toxicity. J. Toxicol., 2012, 302817.

(87) Jandeleit-Dahm, K.A.M., Tikellis, C., Reid, C.M., Johnston, C.I., and Cooper, M.E. (2005). Why blockade of the renin angiotensin system reduces the incidence of new-onset diabetes. J. Hypertens., 23, 463 473.

(88) Jeong, E.M., Liu, M., Sturdy, M., Gao, G., Varghese, S.T., Sovari, A.A., and Dudley, Jr. S.C. (2012). Metabolic stress, reactive oxygen species, and arrhythmia. J. Mol. Cell. Cardiol., 52, 454 463.

(89) Jin, Y., Han, H.-C., and Lindsey, M.L. (2007). ACE inhibitors to block MMP-9 activity: new functions for old inhibitors. J. Mol. Cell. Cardiol., 43, 664 666.

(90) Kampf, C., Lau, T., Olsson, R., Leung, P.S., and Carlsson, P.-O. (2005).

Angiotensin II type 1 receptor inhibition markedly improves the blood perfusion, oxygen tension and first phase of glucose-stimulated insulin secretion in revascularised syngeneic mouse islet grafts. Diabetologia, 48, 1159 1167.

(91) Kasperczyk, A., Slowinska-Lozynska, L., Dobrakowski, M., Zalejska-Fiolka, J., and Kasperczyk, S. (2014). The effect of lead-induced oxidative stress on blood viscosity and rheological properties of erythrocytes in lead exposed humans. Clin.

Hemorheol. Microcirc., 56, 187 195.

(92) (2015). Evaluation of the effect of divalent metal transporter 1 gene polymorphism on blood iron, lead and cadmium levels. Environ. Res., 137, 8 13.

(93) Kehoe, B., Keeton, G.R., and Hill, C. (1986). Elevated plasma renin activity associated with renal dysfunction. Neprhon, 44, 51 7.

(94) Kelly, F.J. (2003). Oxidative stress: Its role in air pollution and adverse health effects. Occup. Environ. Med., 60, 612 616.

(95) Kuramitsu, S., Hayashi, H., Hiromi, K., Morino, Y., and Kagamiyama, H. (1990).

Pre-steady-state kinetics of Escherichia coliaspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry, 29, 5469 5476.

(96) Kusaka, Y., Kelly, R.A., Williams, G.H., and Kifor, I. (2000). Coronary microvascular endothelial cells cosecrete angiotensin II and endothelin-1 via a regulated pathway. Am. J. Physiol. Circ. Physiol., 279, H1087 H1096.

(97) Laragh, J. (2001). ology and clinical pearls for treating hypertension. Am. J. Hypertens., 14, 837 854.

(98) Laragh, J.H., Baer, L., Brunner, H.R., Buhler, F.R., Sealey, J.E., and Vaughan, E.D.J. (1972). Renin, angiotensin and aldosterone system in pathogenesis and management of hypertensive vascular disease. Am. J. Med., 52, 633 652.

(99) Laragh, J.H., and Sealey, J.E. (2011). The plasma renin test reveals the contribution of body sodium-volume content (V) and renin angiotensin (R) vasoconstriction to long-term blood pressure. Am. J. Hypertens., 24, 1164 1180.

(100) Lee, R., Margaritis, M., Channon, K.M., and Antoniades, C. (2012). Evaluating oxidative stress in human cardiovascular disease: methodological aspects and considerations. Curr. Med. Chem., 19, 2504 2520.

(101) Li, Z.-H., Chen, L., Wu, Y.-H., Li, P., Li, Y.-F., and Ni, Z.-H. (2014). Effects of mercury on oxidative stress and gene expression of potential biomarkers in larvae

of the Chinese rare minnow Gobiocypris rarus. Arch. Environ. Contam. Toxicol., 67, 245 251.

(102) Lijnen, P.J., Van Pelt, J.F., and Fagard, R.H. (2010). Downregulation of manganese superoxide dismutase by angiotensin II in cardiac fibroblasts of rats:

Association with oxidative stress in myocardium. Am. J. Hypertens., 23, 1128 1135.

(103) Lijnen, P.J., Piccart, Y., Coenen, T., and Prihadi, J.S. (2012). Angiotensin II-induced mitochondrial reactive oxygen species and peroxiredoxin-3 expression in cardiac fibroblasts. J. Hypertens., 30, 1986 1991.

(104) Liu, J., Qu, W., and Kadiiska, M.B. (2009). Role of oxidative stress in cadmium toxicity and carcinogenesis. Toxicol. Appl. Pharmacol., 238, 209 214.

(105) Lonati, C., Bassani, N., Gritti, A., Biganzoli, E., and Morganti, A. (2014).

Measurement of plasma renin concentration instead of plasma renin activity decreases the positive aldosterone-to-renin ratio tests in treated patients with essential hypertension. J. Hypertens., 32, 627 634.

(106) Luetscher, J.A., Kraemer, F.B., Wilson, D.M., Schwartz, H.C., and Bryer-Ash, M.

(1985). Increased plasma inactive renin in diabetes mellitus. A marker of microvascular complications. N. Engl. J. Med., 312, 1412 1417.

(107) Lum, C., Shesely, E.G., Potter, D.L., and Beierwaltes, W.H. (2004).

Cardiovascular and renal phenotype in mice with one or two renin genes.

Hypertension, 43, 79 86.

(108) Ma, T.K.W., Kam, K.K.H., Yan, B.P., and Lam, Y. (2010).

Renin angiotensin aldosterone system blockade for cardiovascular diseases:

current status. Br. J. Pharmacol., 160, 1273 1292.

(109) Mahajan, A., and Tandon, V. (2004). Antioxidants and rheumatoid arthritis. J Indian Rheumatol Assoc, 12, 139 142.

(110) Maher, W., Duncan, E., Martin, H., Snell, P., Krikowa, F., Jagtap, R., Foster, S., Ezaz, T., and Ellwood, M.J. (2018). Arsenic concentrations and speciation in

Australian and imported rice and commercial rice products [Online]. Environ.

Chem., 15, 387 402.

(111) Marrocco, I., Altieri, F., and Peluso, I. (2017). Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans. Oxid. Med. Cell.

Longev., 2017, 6501046.

(112) Martinez-Finley, E.J., Chakraborty, S., Fretham, S.J.B., and Aschner, M. (2012).

Admit One: How Essential and Nonessential Metals Gain Entrance into the Cell.

Metallomics, 4, 593 605.

(113) Massadeh, A.M., and Al-Massaedh, A.A.T. (2018). Determination of heavy metals in canned fruits and vegetables sold in Jordan market. Environ. Sci. Pollut.

Res. Int., 25, 1914 1920.

(114) Masson, S., Solomon, S., Angelici, L., Latini, R., Anand, I.S., Prescott, M., Maggioni, A.P., Tognoni, G., and Cohn, J.N. (2010). Elevated plasma renin activity predicts adverse outcome in chronic heart failure, independently of pharmacologic therapy: Data from the Valsartan heart failure trial (Val-HeFT). J.

Card. Fail., 16, 964 970.

(115) Matsubara, H. (1998). Pathophysiological role of angiotensin II type 2 receptor in cardiovascular and renal diseases. Circ. Res., 83, 1182 1191.

(116) Mavrakanas, T.A., and Lipman, M.L. (2018). Angiotensin-Converting Enzyme Inhibitors vs. Angiotensin Receptor Blockers for the Treatment of Hypertension in Adults With Type 2 Diabetes: Why We Favour Angiotensin Receptor Blockers.

Can. J. diabetes, 42, 118 123.

(117) McAllister, R.G.J., Michelakis, A.M., and Sandstead, H.H. (1971). Plasma renin activity in chronic plumbism. Effect of treatment. Arch. Intern. Med., 127, 919 923.

(118) McCord, J.M. (2004). Iron, Free Radicals, and Oxidative Injury. J. Nutr., 134, 3171S 3172S.

(119) Mehta, J.L., Saldeen, T.G.P., and Rand, K. (1998). Interactive role of infection,

inflammation and traditional risk factors in atherosclerosis and coronary artery disease. J. Am. Coll. Cardiol., 31, 1217 1225.

(120) Meister, A., and Anderson, M.E. (1983). Glutathione. Annu. Rev. Biochem., 52, 711 760.

(121) De Mello, W.C. (2015). Chemical communication between heart cells is disrupted by intracellular renin and angiotensin II: Implications for heart development and disease. Front. Endocrinol., 6, 1 1.

(122) De Mello, W.C. (2015). Aldosterone disrupts the intercellular flow of glucose in cardiac muscle. Front. Endocrinol., 6, 185.

(123) Mendis, S, Puska, P., and Norrving, B. (2011). Global atlas on cardiovascular disease prevention and control. Geneva, Switzerland: World Health Organization.

(124) Mendis, S. (2014). Global status report on noncommunicable diseases. Geneva, Switzerland: World Health Organization.

(125) Morgan, L., Broughton Pipkin, F., and Kalsheker, N. (1996). Angiotensinogen:

molecular biology, biochemistry and physiology. Int. J. Biochem. Cell Biol., 28, 1211 1222.

(126) Morgan, T., Craven, C., and Ward, K. (1998). Human spiral artery renin-angiotensin system. Hypertension, 32, 683 687.

(127) Morganti, A. (2010). A comparative study on inter and intralaboratory reproducibility of renin measurement with a conventional enzymatic method and a new chemiluminescent assay of immunoreactive renin. J. Hypertens., 28, 1307 1312.

(128) Muhlestein, J.B., May, H.T., Bair, T.L., Prescott, M., Brede, Y., and Horne, B.D.

(2011). Elevated plasma renin activity (PRA) is associated with adverse renal outcomes in patients with coronary artery disease. In: Abstract presented at the World Congress of Nephrology.

(129) Muhlestein, J.B., May, H.T., Bair, T.L., Prescott, M.F., Horne, B.D., White, R.,

and Anderson, J.L. (2010). Relation of elevated plasma renin activity at baseline to cardiac events in patients with angiographically proven coronary artery disease.

Am J Cardiol., 106(6), 764 769.

(130) Mulrow, P.J. (1999). Angiotensin II and aldosterone regulation. Regul. Pept., 80, 27 32.

(131) Murphy, T.J., Alexander, R.W., Griendling, K.K., Runge, M.S., and Bernstein, K.E. (1991). Isolation of a cDNA encoding the vascular type-1 angiotensin II receptor. Nature, 351, 233 236.

(132) Murtaza, I., Wang, H.-X., Feng, X., Alenina, N., Bader, M., Prabhakar, B.S., and Li, P.-F. (2008). Down-regulation of catalase and oxidative modification of protein kinase CK2 lead to the failure of apoptosis repressor with caspase recruitment domain to inhibit cardiomyocyte hypertrophy. J. Biol. Chem., 283, 5996 6004.

(133) Nabi, A.H.M., Biswas, K.B., Ebihara, A., Nakagawa, T., and Suzuki, F. (2013).

Renin angiotensin system in the context of renin, prorenin, and the (pro)renin receptor. Rev. Agric. Sci., 1, 43 60.

(134) Nabi, A.H.M.N., Rahman, M.M., and Islam, L.N. (2005). Evaluation of biochemical changes in chronic arsenic poisoning among Bangladeshi patients.

Int. J. Environ. Res. Public Health, 2, 385 393.

(135) Naftilan, A.J., Zuo, W.M., Inglefinger, J., Ryan, T.J.J., Pratt, R.E., and Dzau, V.J.

(1991). Localization and differential regulation of angiotensinogen mRNA expression in the vessel wall. J. Clin. Invest., 87, 1300 1311.

(136) Nagase, M., Suzuki, F., Fukamizu, A., Takeda, N., Takeuchi, K., Murakami, K., and Nakamura, Y. (1994). Sequencing and expression of sheep angiotensinogen cDNA. Biosci. Biotechnol. Biochem., 58, 1884 1885.

(137) Nagase, M., Suzuki, F., Sawai, Y., Inui, Y., Nakagawa, T., and Nakamura, Y.

(1997). Purification and some properties of recombinant sheep angiotensinogen expressed in Chinese hamster ovary cells. Biomed. Res., 18, 439 443.

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