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      Protection of CCl 4-Induced Liver and Kidney Damage by Phenolic Compounds in Leaf Extracts of Cnestis ferruginea (de Candolle)

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          Abstract

          Background:

          The chemoprevention of chemically-induced hepatotoxicity is a crucial means of minimizing susceptibility to hepatic carcinogenesis and plants remain a rich source of anti-hepatotoxicants with antioxidant properties.

          Objective:

          The protective role of defatted-methanol (MECF) and ethyl acetate fractions (EF), obtained from Leaves of Cnestis ferruginea in rats induced with carbon tetrachloride (CCl 4) toxicity was investigated.

          Materials and Methods:

          Adult male Wistar rats were orally administered MECF or EF (125 – 500 mg/kg bwt/5mL) or silymarin (25 mg/kg bwt/5 mL) separately for three days before intervention with an intraperitoneal dose of CCl 4. Biomarkers of liver and kidney toxicity as well as Ca 2+ regulation were evaluated.

          Results:

          Pre-treatment with MECF and EF significantly ( P < 0.05) decreased the activities of serum alanine and aspartate aminotransferases, levels of urea, creatinine and cholesterol. A significantly ( P < 0.05) enhanced Ca 2+ -ATPase activity and lowered levels of membrane cholesterol: Phospholipid ratio were observed in liver microsomes of pre-treated as compared to CCl 4 -only treated rats. Rat liver superoxide dismutase activity was enhanced by 125 mg/kg and 250 mg/kg of EF and MECF, while decreases were observed at 500 mg/kg. MECF and EF, like silymarin, attenuated CCl 4 -induced hepatotoxicity, microsomal membrane Ca 2+ -ATPase inactivation and renal dysfunction. Phytochemistry of MECF revealed the presence of anthraquinones, cardiac and flavone glycosides, tannins and trihydroxyl phenol.

          Conclusion:

          These findings suggest that the mechanism of hepatoprotection elicited by MECF and EF, involve its antioxidative properties and regulation of Ca 2+ homeostasis.

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          Most cited references44

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          Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression.

          Superoxide dismutases are an ubiquitous family of enzymes that function to efficiently catalyze the dismutation of superoxide anions. Three unique and highly compartmentalized mammalian superoxide dismutases have been biochemically and molecularly characterized to date. SOD1, or CuZn-SOD (EC 1.15.1.1), was the first enzyme to be characterized and is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. SOD3, or EC-SOD (EC 1.15.1.1), is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. What role(s) these SODs play in both normal and disease states is only slowly beginning to be understood. A molecular understanding of each of these genes has proven useful toward the deciphering of their biological roles. For example, a variety of single amino acid mutations in SOD1 have been linked to familial amyotrophic lateral sclerosis. Knocking out the SOD2 gene in mice results in a lethal cardiomyopathy. A single amino acid mutation in human SOD3 is associated with 10 to 30-fold increases in serum SOD3 levels. As more information is obtained, further insights will be gained.
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            Role of free radicals and catalytic metal ions in human disease: an overview.

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              Mechanisms of carbon tetrachloride toxicity.

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                Author and article information

                Journal
                Pharmacognosy Res
                Pharmacognosy Res
                PR
                Pharmacognosy Research
                Medknow Publications & Media Pvt Ltd (India )
                0976-4836
                0974-8490
                Jan-Mar 2014
                : 6
                : 1
                : 19-28
                Affiliations
                [1] Department of Biochemistry, College of Medicine, University of Ibadan, Ibadan, Nigeria
                [1 ] Pharmacology Unit, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi, Pakistan
                Author notes
                Address for correspondence: Dr. Adisa A. Rahmat, Department of Biochemistry, College of Medicine of the University of Lagos, P.M.B. 12003, Lagos, Nigeria. E-mail: radisa22@ 123456yahoo.com
                Article
                PR-6-19
                10.4103/0974-8490.122913
                3897004
                24497738
                5d545c61-6719-4181-b40a-2042c33cc2ec
                Copyright: © Pharmacognosy Research

                This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 01 March 2013
                : 15 March 2013
                : 12 December 2013
                Categories
                Original Article

                Pharmacology & Pharmaceutical medicine
                ccl4 -induced hepatotoxicity,ca2+ -atpase activity,hepatoprotection,renal protection,cnestis ferruginea

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