ORIGINAL_ARTICLE
Association between T-786C polymorphism of endothelial nitric oxide synthase gene and level of the vessel dilation factor in patients with coronary artery disease
Various polymorphisms on endothelial nitric oxide synthase (eNOs) gene cause reduced production of NO, the endothelial relaxing factor, and may accelerate the process of atherosclerosis. The study designed to investigate the frequency of T-786C polymorphism of the eNOs gene in patients suffering from coronary artery disease (CAD) in north-west of Iran. One hundred twenty subjects including 60 patients with angiographically diagnosed CAD and 60 age and sex matched CAD-free subjects as control were studied. The levels of nitric oxide in the samples were measured with the Griess Method. The genotype studies were carried using allele specific PCR. Comparing with the control, reduced levels of NO were noticed in the patient group (P<0.05). Statistical analysis showed that the genotype TC associated with risk of CAD (OR=2.50, 95% CI: 1.13-5.50, P=0.023). The prevalence of C allele was significantly higher in patients compared to control group (OR=2.04, 95% CI: 1.16-3.57, P=0.013). The low levels of NO and increased frequency of T-786C polymorphism might be a risk factor in progression of coronary artery disease in the studied subjects.
https://mbrc.shirazu.ac.ir/article_198_f4fdfc503625127b6a30a50ec91e37cc.pdf
2012-07-16
1
7
10.22099/mbrc.2012.198
Coronary artery disease
endothelial nitric oxide synthase gene
T-786C polymorphism
Nitric oxide
Fatemeh
Khaki-Khatibi
fatemeh.khakikhatibi@yahoo.com
1
Tabriz University of Medical Sciences
LEAD_AUTHOR
Ali Reza
Yaghoubi
alireza_yaghoubi@yahoo.com
2
Cardiovascular Research Center, and Department of Clinical Biochemistry, Faculty of Medicine, Tabriz University of Medical sciences. Tabriz, Iran.
AUTHOR
Morteza
Ghojazadeh
gojazadeh@yahoo.com
3
Department of Clinical Phisiuology Medicine, Tabriz University of Medical sciences. Tabriz, Iran.
AUTHOR
Mohammad
Rahbani-Nobar
Rahbanim@Hotmail.com
4
Cardiovascular Research Center, and Department of Clinical Biochemistry, Faculty of Medicine, Tabriz University of Medical sciences. Tabriz, Iran.
AUTHOR
ORIGINAL_ARTICLE
Molecular identification of Dunaliella viridis Teod. strain MSV-1 utilizing rDNA ITS sequences and its growth responses to salinity and copper toxicity
In addition to biochemical, physiological and morphological analysis, molecular studies provide additional information for establishing phylogenetic relationships among different species and strains of the genus Dunaliella. In the present study, based on neighbor- joining analysis of the nuclear rDNA ITS sequence, a novel strain of the green algae Dunaliella viridis was identified from Maharlu salt lake in Shiraz, Iran. The phylogenetic tree shows that the new strain is part of a clade containing several strains of D. viridis. The new strain was designated Dunaliella viridis MSV-1 and submitted to the GenBank under the accession number HQ864830. The optimum salinity for MSV-1 growth is between 1.0 to 1.5 M NaCl and does not turn red up to 4.5 M NaCl, confirming identity of the isolated strain. With respect to growth response to copper toxicity, increase in Cu2+ concentration from 1 to 30 µM, caused progressive increase in cell number ml-1 of culture over time, whereas reduction in cell number occurred at 100 and 200 µM Cu+2. Nano copper (colloidal copper with 40 nm dimensions) showed less toxicity compared to the ionic form. Cell number ml-1 of culture did not change up to 200 µM nano copper but decreased at 500 µM. In conclusion, the analysis of the ITS sequence is a reliable basis for establishing evolutionary relationships among species and strains of the genus Dunaliella and due to rapid growth at 1.5 M NaCl and high cell density, D. viridis MSV-1 is a good candidate for biofuel production from microalgae.
https://mbrc.shirazu.ac.ir/article_205_f3787dd39844276e4ece8f741aac618a.pdf
2012-07-29
8
15
10.22099/mbrc.2012.205
Dunaliella viridis MSV-1
ITS sequences
nano copper
biofuel
Mansour
Kharati-Koupaei
kharati_k@yahoo.com
1
Department of Biology, Collage of Sciences, Shiraz University, Shiraz, Iran
AUTHOR
Hajar
Zamani
hhzamani@gmail.com
2
Department of Biology, Collage of Sciences, Shiraz University, Shiraz ,Iran
AUTHOR
Ali
Moradshahi
moradshahi@susc.ac.ir
3
Department of Biology, Collage of Sciences, Shiraz University, Shiraz,Iran
LEAD_AUTHOR
1. Ak I, Cirik S, Goksan T. Effects of light intensity, salinity and temperature on growth in Camalti strain of Dunaliella viridis Teodoresco from Turkey. J Biol Sci 2008;8: 1356-1359.
1
2. Massyuk NP. Morphology, taxonomy, ecology and geographic distribution of the genus Dunaliella Teod. and prospects for its potential utilization. Naukova Dumka, Kiev 1973; p 242-263.
2
3. Jimenez C, Niell FX. Growth of Dunaliella viridis Teodoresco: effect of salinity, temperature and nitrogen concentration. J Appl Phycol 1991;3:319- 327.
3
4. Borowitzka MA, Siva CJ. The taxonomy of the genus Dunaliella (Chlorophyta, Dunaliellales) with emphasis on the marine and halophilic species. J Appl Phycol 2007;19:567-590.
4
5. Gomez PI, Gonzalez MA. Genetic variation among seven strains of Dunaliella salina (chlorophyta) with industrial potential based on RAPD banding patterns and on nuclear ITS rDNA sequences. Aquaculture 2004;233:149-162.
5
6. Zamani H, Moradshahi A, Karbalaei-Heidari HR. Characterization of a new Dunaliella salina strain MSI-1 based on nuclear rDNA ITS sequences and its physiological response to changes in composition of growth media. Hydrobilogia 2011;658: 67-75.
6
7. Coleman AW, Mai JC. Ribosomal DNA ITS-1 and ITS-2 sequences comparisons as a tool for predicting genetic relatedness. J Mol Evol 1997;45:168-177.
7
8. Raven JA, Evans MCW, Korb R. The role of trace metals in photosynthetic electron transport in O2-evolving organisms. Photosynth Res 1999;60:111-149.
8
9. Gledhill M, Nimmo M, Hill SJ. The toxicity of copper (II) species to marine algae, with particular reference to macroalge. J Phycol 1997;32:2-11.
9
10. De Freitas J, Wints H, Kim JH, Poynton H, Fox T, Vulpe C. Yeast, a model organism for iron and copper metabolism studies. BioMetals 2003;16:185-197.
10
11. Yruela I, Alfonso M, Baron M, Picorel R. Copper effect on the protein composition of photosystem II. Physiol Plantarum 2000;110:551-557.
11
12. Stauber JL, Florence TM. Mechanism of toxicity of ionic copper and copper complexes to algae. Mar Biol 1987;94:511-519.
12
13. Blinova I, Ivask A, Heinlaan M, Mortimer M, Kahru A. Ecotoxicity of nanoparticles of CuO and ZnO in natural water. Environ Pollut 2010;158:41-47.
13
14. Gomez PI, Gonzalez MA. Genetic polymorphism in eight Chilean of the carotenogenic microalga Dunaliella salina Teodoresco (Chlorophyta). Biol Res 2001;34:23-30.
14
15. Goff LJ, Moon DA, Coleman AW. Molecular delineation of species and species relationships in the red algal agarophytes Gracilariopsis and Gracilaria (Gracilariales). J Phycol 1994;30: 521-537.
15
16. Tamura K, Dudley J, Nei M, Kumar S. MEGA 4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 2007;24:1596-1599.
16
17. Oren A. A hundred years of Dunaliella research: 1905-2005. Saline Systems 2005;1:1-14.
17
18. Garcia F, Freile-Pelegrin Y, Robledo D. Physiological characterization of Dunaliella sp. (Chlorophyta, Volvocales) from Yucatan, Mexico. Bioresource Technol 2007;98:1359- 1365.
18
19. Bryan GW, Langston WJ. Bioavailability, accumulation and effects of heavy metals in sediments with special reference to United Kingdom estuaries: a review. Environ Pollut 1992; 76:89-131.
19
20. Nowack B, Bucheli TD. Occurrence, behavior and effect of nanoparticles in the environment. Environ Pollut 2007;150:5-22.
20
21. Lee WM, An YJ, Yoon H, Kweon HS. Toxicity and bioavailability of copper nanoparticle to the terrestrial plants phaseolus radiatus and Triticum aestivum : plant agar test for water – insoluable nano particle. Environ Toxicol Chem 2008;27:1915-1921.
21
22. Musante C, White JC. Toxicity of silver and copper to Cucurbita pepo: differential effects of nano and bulk-size particle. Environ Toxicol 2010;27:1-8.
22
23. Chen Z, Meng H, Xing G, Chen C, Zhao Y, Jia G, Wang T, Yuan H, Ye C, Zhao F, Chai Z, Zhu C, Fang X, Ma B, Wan L. Acute toxicological effects of copper nanoparticles in vivo. Toxicol Lett 2006;163:109–120.
23
24. Drazkewicz M, Skorzynska-Polit E, Krupa Z. Copper induced oxidative stress and antioxidant defense in Arabidobpsis thaliana. Biometals 2004;17:379-387.
24
25. Sakar A, Das J, Manna P, Sil PC. Nano copper induces oxidative stress and apoptosis in kidneg via both extrinsic pathways. Toxicology 2011;240:208-217.
25
26. Gouveia L, Olivera AC. Microalgae as a raw material for boifuels production. J Ind Microbiol Biot 2009;36:169-174.
26
ORIGINAL_ARTICLE
Effect of Cyclosporine A on the expression of GSTO2 metabolizing enzyme in Jurkat cell line
Cyclosporine A (CsA), a cyclic polypeptide metabolite extracted from the fungus, is used clinically to combat organ graft rejection in transplant subjects. Previous studies have shown that CsA exposure enhances the production of reactive oxygen species (ROS) and lipid peroxidation, which are directly involved in CsA toxicity. To protect cells and organs against ROS, the human body has evolved a highly antioxidant protection system to neutralize free radicals. The aim of this study was to investigate the effect of CsA on mRNA expression of anti-oxidant GSTO2. To do this, Jurkat cells were incubated for 24 h with different doses of CsA, ranging from 1-80 µg/ml, and the IC50 of CsA was calculated to be 40 µg/ml. Subsequently, Jurkat cells were treated with 3 µg/ml CsA for 24 h and the gene expression of GSTO2 was quantified by quantitative Real-time PCR. Results showed that the mean (SD) expression of the GSTO2 gene in CsA treated cells was 1.10 (0.07) (when assuming an expression level in untreated cells of 1.0). However, statistical analyses showed that the alterations were not significant (t=2.29, df=2, P=0.149). These findings suggest that at this concentration of CsA, other antioxidant enzymes are up-regulated in Jurkat cell lines to detoxify free radicals induced by CsA.
https://mbrc.shirazu.ac.ir/article_236_65344c7ae51faad43a47597f69dd2820.pdf
2012-08-19
16
20
10.22099/mbrc.2012.236
Cyclosporine A
GSTO2
Gene expression
Real Time PCR
Nioosha
Nekooie-Marnany
newshanekooiee@yahoo.com
1
Department of Biology, College of Sciences and Institute of Biotechnology, Shiraz University, Shiraz 71454, Iran
AUTHOR
Iraj
Saadat
isaadat@shirazu.ac.ir
2
Department of Biology, College of Sciences and Institute of Biotechnology, Shiraz University, Shiraz 71454, Iran
LEAD_AUTHOR
Kahan BD. Cyclosporine: arevolution in transplantation. Transplant Proc 1999;31:14S-15S.
1
Shaw JP, Utz PJ, Durand DB, Toole JJ, Emmel EA, Crabtree GR. Identification of a putative regulator of early T cell activation genes. Science 1998;241:202-205.
2
Yoshimura N, Okamoto M, Akioka K, Kaihara S. Optimization of the use of cyclosporine in renal transplantation. Transplant Proc 2004;36:181S-185S.
3
Kahan BD, Flechner SM, Lorber MI, Golden D, Conley S, Van Buren CT. Complications of cyclosporine-prednisone immunosuppression in 402 renal allograft recipients exclusively followed at a single center for from one to five years. Transplantation 1987;43:197-204.
4
Bach JF. The contribution of cyclosporine A to the understanding and treatment of autoimmune diseases. Transplant Proc 1999;31:16S-18S.
5
Muellenhoff MW, Koo JY. Cyclosporine and skin cancer: an international dermatologic perspective over 25 years of experience. A comprehensive review and pursuit to define safe use of cyclosporine in dermatology. J Dermatolog Treat 2011;23:290-304.
6
Haw S, Shin MK, Haw CR. The efficacy and safety of long-term oral cyclosporine treatment for patients with atopic dermatitis. Ann Dermatol 2010;22:9-15.
7
Kavanagh GM, Ross JS, Cronin E, Smith NP, Black MM. Recalcitrant pyoderma gangrenosum--two cases successfully treated with cyclosporin A. Clin Exp Dermatol 1992; 17:49-52.
8
Pham CQ, Efros CB, Berardi RR. Cyclosporine for severe ulcerative colitis. Ann Pharmacother 2006;40:96-101.
9
Utine CA, Stern M, Akpek EK. Clinical review: topical ophthalmic use of cyclosporin A. Ocul Immunol Inflamm 2010;18:352-61.
10
De Mattos AM, Olyaei AJ, Bennett WM. Nephrotoxicity of immunosuppressive drugs: long-term consequences and challenges for the future. Am J Kidney Dis 2000;35:333-346.
11
Olyaei AJ, de Mattos AM, Bennett WM. Nephrotoxicity of immunosuppressive drugs: new insight and preventive strategies. Curr Opin Crit Care 2001;7:384-389.
12
Ichikawa I, Kiyama S, Yoshioka T. Renal antioxidant enzymes: their regulation and function. Kidney Int 1994:45:1-9.
13
Stroes ESG, Lue Scher TF, De Groot FG, Koomans HA, Rabelink, TJ. Cyclosporin A increases nitric oxide activity in vivo. Hypertension 1997;29:570-575.
14
Ahmed SS, Strobel HW, Napoli KL, Grevel J. Adrenochrome reaction implicates oxygen radicals in metabolism of cyclosporine A and FK-506 in rat and human liver microsomes. J Pharmacol Exp Ther 1993;265:1047-1054.
15
Wang C, Salahudeen AK. Lipid peroxidation accompanies cyclosporine nephrotoxicity: effects of vitamin E. Kidney Int 1995;47:927-934.
16
Paller MS. Free radical scavengers in mercury chloride-induced acute renal failure in the rat. J Lab Clin Med 1985;105:459-463.
17
Chen HW, Chien CT, Yu SL, Lee YT, Chen WJ. Cyclosporine A regulate oxidative stress-induced apoptosis in cardiomyocytes: mechanisms via ROS generation, iNOS and Hsp70. Br J Pharmacol 2002;137:771-781.
18
Nebert DW, Vasiliou V. Analysis of the glutathione S-transferase (GST) gene family. Hum Genomics 2004;1:460-464.
19
Board PG, Coggan M, Chelvanayagam G, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J. Identification, characterization, and crystal structure of the omega class glutathione transferases. J Biol Chem 2000; 275:24798-24806.
20
Rezzani R. Exploring cyclosporine A: Side effects and the protective role-played by antioxidants: the morphological and immunehistochemical studies. Histol Histopathol 2006; 21:301-316.
21
ORIGINAL_ARTICLE
Isolation and characterization of Phi class glutathione transferase partial gene from Iranian barley
Glutathione transferases are multifunctional proteins involved in several diverse intracellular events such as primary and secondary metabolisms, signaling and stress metabolism. These enzymes have been subdivided into eight classes in plants. The Phi class, being plant specific, is the most represented. In the present study, based on the sequences available at GenBank, different primers were designed for amplifying the Phi class of glutathione transferase gene in the genome and transcriptome of Iranian barley, Karoun cultivar. After extraction of DNA and total RNA, Phi class was amplified and sequenced. Bioinformatics analysis predicted that the deduced protein sequence has two ß-sheets, eight α-helices and some intermediate loops in its secondary structure. Consequently, the sequences were submitted to NCBI GenBank with GS262333 and GW342614 accession numbers. Phylogenic relationships of the sequences were compared with existing sequences in GenBank.
https://mbrc.shirazu.ac.ir/article_237_bb70e0970cbc496ca13236b01af8abdc.pdf
2012-08-19
21
26
10.22099/mbrc.2012.237
Hordeum vulgare
Glutathione S-transferase
stress
Xenobiotics
Sasan
Mohsenzadeh
mohsenz@shirazu.ac.ir
1
Department of Biology, College of Sciences, Shiraz University, Shiraz 71454, Iran
LEAD_AUTHOR
Maryam
Esmaeili
mary_es_60@yahoo.com
2
Department of Biology, College of Sciences, Shiraz University, Shiraz 71454, Iran
AUTHOR
Hassan
Mohabatkar
mohabatkar@susc.ac.ir
3
Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan, Isfahan, Iran
AUTHOR
1. Edwards R, Dixon DP, Walbot V. Plant glutathione S-transferase: enzymes with multiple functions in sickness and in health. Trends Plant Sci 2000;5:193-198.
1
2. Dixon D, Lapthorn A, Edwards R. Plant glutathione transferases. Genome Biol 2002; 3:3004.
2
3. Wilce MCJ, Parker MW. Structure and function of glutathione S-transferases. Biochim Biophys Acta 1994;1205:1-18.
3
4. Wongsantichon J, Ketterman A. Alternative splicing of glutathione transferases. Method Enzymol 2005;401:100-116.
4
5. Hayes JD, Pulford DJ. The glutathione S-transferase super gene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol 1995;30:445-600.
5
6. Oztetik E (2008) A tale of plant glutathione Stransferases: since 1970. Bot Rev 74: 419-437.
6
7. Mohsenzadeh S, Saffari B, Mohabatkar H. A new member of Tau-class glutathione S-transferase from barley leaves. EXCLI Journal 2009;8:190-194.
7
8. McGonigle B, Keeler SJ, Lau SMC, Koppe MK, Okeefe DP. A genomics approach to the comprehensive analysis of the glutathione S-transferase gene family in soybean and maize. Plant Physiol 2000;124:1105-1120.
8
9. Basantani M, Srivastava A. Plant glutathione transferases - a decade falls short. Can J Bot 2007;85:443-456.
9
10. Noctor G, Arisi A, Jouanin L, Kunert K, Rennenberg H, Foyer C. Glutathione: biosynthesis metabolism and relationship to stress tolerance explored in transformed plants. J Exp Bot 1998;49:623-647.
10
11. Sumer A, Duran A, Yenilmez G. Isolation of DNA for RAPD analysis from dry leaf material of some Hesperis L. specimens. Plant Mol Biol Rep 2003;21:461a-461f.
11
12. Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987;4:406-425.
12
13. Thompson JD, Higgins DG, Gibson TG. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
13
14. Hall TA. BioEdit: a user friendly biological sequence alignment editor and analysis program for windows 95/98/NT. Nucleic Acids Symp Series 1999;41;95-98.
14
15. Dixon DP, McEwen AG, Lapthorn AJ, Edward R. Forced evolution of a herbicide detoxifying glutathione trasferase. J Biol Chem 2003;278:23930-23935.
15
16. Cho HY, Kong KH. Molecular cloning, expression and characterization of a phi-type glutathione S-transferase from Oryza sativa. Pest Biochem Physiol 2005;83:29-36.
16
17. Mohsenzadeh S, Esmaeili M, Moosavi F, Shahrtash M, Saffari B, Mohabatkar H. Plant glutathione S-transferase classification, structure and evolution. Afr J Biotech 2011;10:8160-8165.
17
18. Frova C. The plant glutathione transferase gene family: genomic structure, functions, expression and evolution. Physiol Plantarum 2003;119:469-479.
18
19. Muller LA, Goodman CD, Silady RA, Walbot V. AN9, a petunia glutathione S-transferase required for anthocyanin sequestration is a flavonoid-binding protein. Plant Physiol 2000; 123:1561-1570.
19
20. Loyall L, Uchida K, Braun S, Furuya M, Frohnmeyer H. Glutathione and a UV light-induced glutathione S-transferase are involved in signaling to chalcone synthase in cell cultures. Plant Cell 2000;12:1939-1950.
20
21. Basantani M, Srivastava A. Plant glutathione transferases- a decade falls short. Can J Bot 2007;85:443-456.
21
22. Wagner U, Edwards R, Dixon DP, Mauch F. Probing the diversity of the Arabidopsis glutathione s- transferase gene family. Plant Mol Biol 2002;49:515-532.
22
23. Cummins I, O’Hagan D, Jablonkai I, Cole DJ, Hehn A, Werck-Reichhart D, Edwards R. Cloning, characterization and regulation of a family of phi class glutathione transferase from wheat. Plant Mol Biol 2003;52:591-603.
23
24. Cho HY, Lee HJ, Kong KH. A Phi class glutathione S-transferase from Oryza sativa (OsGSTF5): Molecular cloning, expression and biochemical characteristics. J Biochem Mol Biol 2007;40:511-516.
24
25. Dixon DP, Cummins I, Cole DJ, Edwards R. Glutathione mediated detoxification systems in plants. Curr Opini Plant Biol 1998;1:258-266.
25
26. Rossini L, Frova C, Pe` ME, Mizzi L, Sari Gorla M. Alachlor regulation of maize glutathione S-transferase genes. Pestic Biochem Physiol 1998;60:205-211.
26
27. DeRidder BP, Dixon DP, Beussman DJ, Edwards R, Goldsbrough PB. Induction of glutathione S-transferases in Arabidopsis by herbicide safeners. Plant Physiol 2002;130:1497-1505.
27
28. Scalla R, Roulet A. Cloning and characterization of a glutathione S-transferase induced by an herbicide safener in barley (Hordeum vulgare). Plant Physiol 2002;116:336-344.
28
ORIGINAL_ARTICLE
Inhibition of chickpea seedling copper amine oxidases by tetraethylenepentamine
Copper amine oxidases are important enzymes, which contribute to the regulation of mono- and polyamine levels. Each monomer contains one Cu(II) ion and 2,4,5-trihydroxyphenylalanine (TPQ) as cofactors. They catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. The mechanism is followed by the transfer of two electrons to molecular oxygen which is reduced to hydrogen peroxide. Inhibitors are important tools in the study of catalytic properties of copper amine oxidases and they also have a wide application in physiological research. In this study, purification of the chickpea seedling amine oxidase, was done via salting out by ammonium sulfate and dialysis, followed by DEAE-cellulose column chromatography. By using the Lineweaver - Burk plot, the Km and Vm of the enzyme were found to be 3.3 mM and 0.95 mmol/min/mg, respectively. In this study, the interaction of chickpea diamino oxidase with tetraethylene- pentamine was studied. Analysis of kinetic data indicated that tetraethylenepentamine (with Ki=0.1 mM) inhibits the enzyme by linear mixed inhibitory effect.
https://mbrc.shirazu.ac.ir/article_238_5a2a3e5d850bcf7d77885214c6a69bdf.pdf
2012-08-19
27
32
10.22099/mbrc.2012.238
Chickpea
Copper-containing amine oxidases
Tetraethylenepentamine
Linear mixed
Sona
Talaei
sonatalaye@yahoo.com
1
Deptarment of Biology, Faculty of Science, University of Mohaghegh Ardabili, Ardabil, Iran
AUTHOR
Asadollah
Asadi
asady@uma.ac.ir
2
Deptarment of Biology, Faculty of Science, University of Mohaghegh Ardabili, Ardabil, Iran
LEAD_AUTHOR
Mojtaba
Amani
amani@ibb.ut.ac.ir
3
Deptarment of Science, Faculty of Medicine, University of Medical science, Ardabil, Iran
AUTHOR
1. Šebela, M, Tylichová M, Peč P. Inhibition of diamine oxidases and polyamine oxidases by diamine-based compounds. J Neural Transm 2007;114:793–798.
1
2. Frébort I, Adachi O.Copper/Quinone-Containing Amine Oxidases, an Exciting Class of Ubiquitous Enzymes. J Ferment Bioeng 1995;80:625-632.
2
3. Longu S, Mura A, Padiglia A, Medda R, Floris G. Mechanism -based inactivators of plant copper/quinone containing amine oxidases. Phytochemistry 2005;66:1751-1758.
3
4. Heli H, Amani M, Moosavi-Movahedi A, Jabbari A, Floris G, Mura A. Electroactive Centers in Euphorbia Latex and Lentil Seedling Amine Oxidase. Biosci Biotechnol Biochem 2008;72: 29-36.
4
5. Mura A, Padiglia A, Medda R, Pintus F, Agro A, Floris G. Properties of copper-free pig kidney amine oxidase: Role of topa quinine. FEBS Lett 2006;580:4317–4324.
5
6. Dawkes H, Phillips S. Copper amine oxidase: cunning cofactor and controversial copper. Curr Opin Struct Biol 2001;11:666–673.
6
7. Di Paolo M, Vianello F, Stevanato R, Rigo A. Kinetic Characterization of Soybean Seedling Amine Oxidase. Arch Biochem Biophys 1995;323:329-334.
7
8. Kivirand K, Rinken T. Purification and properties of amine oxidase from pea seedlings. Proc Estonian Acad Sci Chem 2007;56:164–171.
8
9. Liu YH, Liang WL, Lee CHCH, Tsai YF, Hou WCH. Antioxidant and semicarbazide-sensitive amine oxidase inhibitory activities of glucuronic acid hydroxamate. Food Chem 2011;129: 423–428.
9
10. Zhang YM, Livingstone JR, Hirasawa E. Purification and characterisation of monoamine oxidase from Avena sativa. Acta Physiol Plant 2012;34:1411–1419.
10
11. Šebela, M, Radová A, Angelini R, Tavladoraki P, Frébort I, Peč P. FAD containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants. Plant Sci 2001;160:197-207.
11
12. Medda R, Bellelli A, Peč P, Federico R, Cona A, Floris G. Copper amine oxidases of plants. In Copper Amine Oxidases, Floris G, Mondovì B, Ed. Boca Raton: CRC Press, p 2009;44.
12
13. Story KB. Functional Metabolism: Regulation and Adaptation. Hoboken, NJ: Wiley-Liss 2004.
13
14. Berg JM, Tymoczko JL, Stryer L. Biochemistry, 5th edition. W. H. Freeman and company 2002.
14
15. Laemmli UK. Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 1970;227:680-254.
15
16. Bardsley WG. Inhibitors of copper amine oxidases. In Structure and Functions of Amine Oxidases, Mondovì B, Ed. Boca Raton: CRC Press, p. 1985;135.
16
17. Padiglia A, Medda R, Pedersen JZ, Lorrai A, Pec P, Frébort G. Inhibitors of plant copper amine oxidases. J Enzyme Inhibi 1998;13:311-325.
17
18. Šebela M, Lamplot Z, Petřivalský M, Kopečný D, Lemr K, Frébort I, Peč P. Recent news related to substrates and inhibitors of plant amine oxidases. Biochim Biophys Acta 2003; 1647:355-360.
18
19. Macholán L. Substrate-like inhibitors of diamine oxidase: some relations between the structure of aliphatic aminoketones and their inhibitory effect. Arch Biochem Biophys 1969; 134:302-307.
19
20. Rotilio G. Spectroscopic and chemical properties of the amine oxidase copper. In Structure and Functions of Amine Oxidases, Mondovì B, Ed. Boca Raton: CRC Press, p.1985;127.
20
21. Devoto G, Massacesi M, Ponticelli G, Medda R, Floris G. Inhibitory activity of bivalent transition-metal complexes with diamines toward a diamine oxidase. Polyhedron 1986;5: 1023-1025.
21
22. Vianello F, Malek-Mirzayans A, Di Paolo ML, Stevanato R, Rigo A. Purification and Characterization of Amine Oxidase from Pea Seedlings. Protein Expr Purif 1995;15:196–201.
22
ORIGINAL_ARTICLE
The changes in lipid composition of Pythium irregulare LX oomycetes at a stressful situation created with crude oil
Pythium irregulare oomycetes adapts with environmental changes including crude oil concentration by changing the composition of lipids in the cytoplasmic membrane and providing the required characteristics for adaptation in improper and stressful environmental situations. It was found that cultivation of Pythium irregulare LX oomycetes in the nutrient media with different concentrations of crude oil with 1.0, 2.0, 3.0, 5.0 and 10.0 (%), incubated for 5 days at 26-28°C on a rotary shaker (200 rpm) in aerobic conditions and deep culturing caused an increase in the lipid content and the unsaturation degree of fatty acids, confirming the correspondence between the increase of polar lipid/free sterol in the composition of membrane lipids’ ratio and that of polar lipids in general lipid fractions. Represented data shows that the process of adaptation of oomycetes to a stressful situation created with crude oil motivated the increase of the rate of membrane phospholipids with a high quantity of unsaturated fatty acids.
https://mbrc.shirazu.ac.ir/article_240_928ac6425256c6fdbbb3f2c2d3613575.pdf
2012-09-02
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10.22099/mbrc.2012.240
stress
Oil
Pythium irregulare
lipid
phospholipids
Mehdi
Ghasemi
mehdi_aidin@yahoo.com
1
Department of Biology, Ardabil Branch, Islamic Azad University, Ardabil, Iran
LEAD_AUTHOR
Yemen
Atakishiyeva
y.atakishiyeva@mail.ru
2
Institute of Microbiology, Azerbaijan National Academy of Sciences, Baku, Azerbaijan
AUTHOR
Asadollah
Asadi
asady@uma.ac.ir
3
Department of Biology, Faculty of Science, University of Mohaghegh Ardabili, P.O. Box 179, Ardabil, Iran
AUTHOR
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