ORIGINAL_ARTICLE
Analysis of nitrate reductase mRNA expression and nitrate reductase activity in response to nitrogen supply
Nitrate is one of the major sources of nitrogen for the growth of plants. It is taken up by plant roots and transported to the leaves where it is reduced to nitrite in the. The main objective of this research was to investigate stimulatory effects of sodium nitrate, potassium nitrate, ammonia and urea on the production/generation of the nitrate reductase mRNA in Triticum aestivum plants. The plants were grown in standard nutrient solution for 21 days and then starved in a media without nitrate for seven days. Starved plants were stimulated with various concentrations of sodium nitrate, potassium nitrate, ammonia and urea, and the expression of nitrate reductase mRNA was analyzed by real-time PCR. Our results indicated that starvation caused significant decrease in the production of nitrate reductase mRNA in the plant leaf. Sodium and potassium nitrate were capable of restoring the production of nitrate mRNA in a dose-dependent manner, since 50 mM of each produced the highest level of the mRNA. The stimulatory effect of potassium nitrate was higher than sodium nitrate, while ammonia and urea did not show such activity. At low concentrations, sodium nitrate and potassium nitrate caused significant increase in the nitrate/nitrite mRNA production, whereas high concentrations of these salts suppressed the expression of this gene considerably.
https://mbrc.shirazu.ac.ir/article_1960_fc5b4896d8e7093cb7660c93df600781.pdf
2014-06-01
75
84
10.22099/mbrc.2014.1960
Triticum aestivum
nitrate
Potassium nitrate
nitrate reductase
Gholamreza
Kavoosi
ghkavoosi@shirazu.ac.ir
1
1Institute of Biotechnology , Shiraz University, Shiraz, Iran
LEAD_AUTHOR
Sadegh
Balotf
sbaotff@yahoo.com
2
Biotechnology Institute, Shiraz University, Shiraz, Iran
AUTHOR
Homeira
Eshghi
heshghi12@ yahoo.com
3
Biotechnology Institute, Guilan University, Guilan, Iran
AUTHOR
Hasan
Hasani
hhasani@ gmail.com
4
Biotechnology Institute, Guilan University, Guilan, Iran
AUTHOR
1.Castaings L, Marchive C, Meyer C, Krapp A. Nitrogen signaling in Arabidopsis: how to obtain insights into a complex signaling network. J Exp Bot 2011;62:1391-1397.
1
2.Cavagnaro TR, Jackson LE, Six J, Ferris H, Goyal S, Asami D, Scow KM. Arbuscular mycorrhizas, microbial communities, nutrient availability, and soil aggregates in organic tomato production. Plant Soil 2006;282:209-225.
2
3.North KA, Ehlting B, Koprivova A, Rennenberg H, Kopriva S. Natural variation in Arabidopsis adaptation to growth at low nitrogen conditions. Plant Physiol Biochem 2009;47:912-918.
3
4.Lam HM, Coschigano KT, Oliveira IC, Melo-Oliveira R, Coruzzi, GM.The molecular-genetics of nitrogen assimilation into amino acids in higher plants. Annu Rev Plant Biol 1996;47:569-593.
4
5.Loque D, von Wiren N. Regulatory levels for the transport of ammonium in plant roots. J Exp Bot 2004;55:1293-1305.
5
6.Maathuis FJ. Physiological functions of mineral macronutrients. Curr Opin Plant Biol 2009;12:250-258.
6
7.White PJ, Brown PH. Plant nutrition for sustainable development and global health. Annal Bot 2010;105:1073-1080.
7
8.Andrews M. The partitioning of nitrate assimilation between root and shoot of higher plants. Plant Cell Environ 1986;9:511-519.
8
9.Anjana SU, Iqbal M. Nitrate accumulation in plants, factors affecting the process, and human health implications. Agron Sustain Dev 2007;27:45-57.
9
10.Aslam M, Travis RL, Rains DW. Differential effect of amino acids on nitrate uptake and reduction systems in barley roots. Plant Sci 2001;160:219-228.
10
11.Chen BM, Wang ZH, Li SX, Wang GX, Song HX, Wang XN. Effects of nitrate supply on plant growth, nitrate accumulation, metabolic nitrate concentration and nitrate reductase activity in three leafy vegetables. Plant Sci 2004;167:635-643.
11
12.Stohr C, Strube F, Marx G, Ullrich WR, Rockel P. A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite. Planta 2001;212:835-841.
12
13.Tischner R. Nitrate uptake and reduction in higher and lower plants. Plant Cell Environ 200;23:1005-1024.
13
14.Vincentz M, Moureaux T, Leydecker MT, Vaucheret H, Caboche M. Regulation of nitrate and nitrite reductase expression in Nicotiana plumbaginifolia leaves by nitrogen and carbon metabolites. Plant J 1993;3:315-324.
14
15.Wang Z, Li S. Effects of nitrogen and phosphorus fertilization on plant growth and nitrate accumulation in vegetables. J Plant Nutr 2004;27:539-556.
15
16.Doane TA, Horwáth WR.Spectrophotometric determination of nitrate with a single reagent. Anal Lett 2003;36:2713-2722.
16
17.Schmidt B, Strack D, Weidner M. Nitrate reductase in needles, roots and trunk wood of spruce trees.Trees 1991;5:215-226.
17
18.Hellemans J, Mortier G, De Paepe A, Speleman F, Vandesompele J. Base relative quantification framework and software for management and automated analysis of real-time quantitative PCR data. Genome Biol 2007;8:R19.
18
19.Yuan JS, Reed A, Chen F, Stewart CN. Statistical analysis of real-time PCR data. BMC Bioinformatics 2006;7:85-90.
19
20.Glass AD, Britto DT, Kaiser BN, Kinghorn JR, Kronzucker HJ, Kumar A, Vidmar JJ. The regulation of nitrate and ammonium transport systems in plants. J Exp Bot 2002;53:855-864.
20
21.Okamoto M, Vidmar JJ, Glass AD. Regulation of NRT1 and NRT2 gene families of Arabidopsis thaliana: responses to nitrate provision. Plant Cell Physiol 2003;44: 304-317.
21
22.Forde BG. Local and long-range signaling pathways regulating plant responses to nitrate. Ann Rev Plant Biol 2002;53:203-224.
22
23.Chen G, Guo S, Kronzucker HJ, Shi W. Nitrogen use efficiency (NUE) in rice links to NH4+ toxicity and futile NH4+ cycling in roots. Plant Soil 2013; 369:351-363.
23
24.Little DY, Rao H, Oliva S, Daniel-Vedele F, Krapp A, Malamy JE. The putative high-affinity nitrate transporter NRT2. 1 represses lateral root initiation in response to nutritional cues. Proc Nati Acad Sci USA 2005;102:13693-13698.
24
25.Krouk G, Tillard P, Gojon A. Regulation of the high-affinity NO3- uptake system by NRT1.1-mediated NO3- demand signaling in Arabidopsis. Plant Physiol 2006; 42:1075-1086.
25
26.Remans T, Nacry P, Pervent M, Filleur S, Diatloff E, Mounier E, Gojon A. The Arabidopsis NRT1. 1 transporter participates in the signaling pathway triggering root colonization of nitrate-rich patches. Proc Nati Acad Sci USA 2006;103:19206-19211.
26
27.Remans T, Nacry P, Pervent M, Girin T, Tillard P, Lepetit M, Gojon A. A central role for the nitrate transporter NRT2.1 in the integrated morphological and physiological responses of the root system to nitrogen limitation in Arabidopsis. Plant Physiol 2006;140:909-921.
27
28.Wang WH, Kohler B, Cao FQ, Liu LH. Molecular and physiological aspects of urea transport in higher plants. Plant Sci 2008;175:467-477.
28
29.Wojciechowska R, Rosek S, Leja M. The effect of differentiated nitrogen fertilization on nitrate reduction in broccoli heads of ‘Lord F1’in spring cultivation. Folia Hort 2006;18:101-110.
29
30.Wojciechowska R, Rosek S, Rydz A. Broccoli yield and its quality in spring growing cycle as dependent on nitrogen fertilization. Folia Hort 2005;17:141-152.
30
31.Sady W, Rożek S, Domagala-Swiątkiewicz I, Wojciechowska R, Kolton A. Effect of nitrogen fertilization on yield, NH4+ and NO3-content of white cabbage. Acta Sci Pol Hortorum Cultus 2007;7:41-51.
31
32.Debouba M, Maâroufi-Dghimi H, Suzuki A, Ghorbel MH, Gouia H. Changes in growth and activity of enzymes involved in nitrate reduction and ammonium assimilation in tomato seedlings in response to NaCl stress. Annals Bot 2007;99: 1143-1151.
32
33.Rana NK, Mohanpuria P, Yadav SK. Expression of tea cytosolic glutamine synthetase is tissue specific and induced by cadmium and salt stress. Biol Plantarum 2008;52:361-364.
33
34.Roberts MR. 14-3-3 proteins find new partners in plant cell signaling. Trends Plant Sci 2003;8:218-223.
34
35.Lillo C, Meyer C, Lea US, Provan F, Oltedal S. Mechanism and importance of post‐translational regulation of nitrate reductase. J Exp Bot 2004;55:1275-1282.
35
36.Lambeck IC, Fischer-Schrader K, Niks D, Roeper J, Chi JC, Hille R, Schwarz G. Molecular mechanism of 14-3-3 protein-mediated inhibition of plant nitrate reductase. J Biol Chem 2012;287:4562-4571.
36
37.Grimsrud PA, den Os D, Wenger CD, Swaney DL, Schwartz D, Sussman MR, Coon JJ. Large-scale phosphoprotein analysis in Medicago truncatula roots provides insight into in vivo kinase activity in legumes. Plant physiol 2010;152:19-28
37
38.Barjaktarovic Z, Schütz W, Madlung J, Fladerer C, Nordheim A, Hampp R. Changes in the effective gravitational field strength affect the state of phosphorylation of stress-related proteins in callus cultures of Arabidopsis thaliana. J Exp Bot 2009;60:779-789.
38
39.Kronenberger J, Lepingle A, Caboche M, Vaucheret H. Cloning and expression of distinct nitrite reductases in tobacco leaves and roots. Mol General Genetics 1993; 236:203-208.
39
40.Koch K. Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and plant development. Curr Opin Plant Biol 2004;7:235-246.
40
41.Cera ED.A structural perspective on enzymes activated by monovalent cations. J Biol Chem 2006;281:1305-1308.
41
42.Tetlow IJ, Morell MK, Emes MJ. Recent developments in understanding the regulation of starch metabolism in higher plants. J Exp Bot 2004;55:2131-2145.
42
43.Prasad S, Wright KJ, Roy DB, Bush LA, Cantwell AM, Di Cera E. Redesigning the monovalent cation specificity of an enzyme. Proc Nati Acad Sci USA 2003;100: 13785-13790.
43
44.Amtmann A, Troufflard S, Armengaud P. The effect of potassium nutrition on pest and disease resistance in plants. Physiol Plantarum. 2008;133:682-691.
44
45.Watanabe M, Hubberten HM, Saito K, Hoefgen R. General regulatory patterns of plant mineral nutrient depletion as revealed by serat quadruple mutants disturbed in cysteine synthesis. Mol plant 2010;3:438-466.
45
46.Crawford NM, Glass AD. Molecular and physiological aspects of nitrate uptake in plants. Trends Plant Sci 1998;3:389-395.
46
47.Clarkson DC, Saker LR, Purves JV. Depression of nitrate and ammonium transport in barley plants with diminished sulphate status. Evidence of co-regulation of nitrogen and sulphate intake. J Exp Bot 1989;40:953-963.
47
48.Karley AJ, White PJ. Moving cationic minerals to edible tissues: potassium, magnesium, calcium. Curr Opin Plant Biol 2009;12:291-298.
48
49.Pilon-Smits EA, Quinn CF, Tapken W, Malagoli M, Schiavon M. Physiological functions of beneficial elements. Curr Opin Plant Biol 2009;12:267-274.
49
50.Bates GW, Rosenthal DM, Sun J, Chattopadhyay M, Peffer E, Yang J, Jones AM. A comparative study of the Arabidopsis thaliana guard-cell transcriptome and its modulation by sucrose. PLOS one 2012;7:e49641.
50
51.Kim MJ, Ciani S, Schachtman DP. A peroxidase contributes to ROS production during Arabidopsis root response to potassium deficiency. Mol plant 2010;3:420-427.
51
52.Rolland F, Moore B, Sheen J. Sugar sensing and signaling in plants. The Plant Cell Online 2002;14:S185-S205.
52
53.Wang Y, Wu WH. Plant sensing and signaling in response to K+-deficiency. Mol plant 2010;3:280-287.
53
54.Wang W, Vinocur B, Altman A. Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance. Planta 2003;218:1-14.
54
55.Seki M, Narusaka M, Ishida J, Nanjo T, Fujita M, Oono Y, Shinozaki K. Monitoring the expression profiles of 7000 Arabidopsis genes under drought, cold and high‐salinity stresses using a full‐length cDNA microarray. Plant J 2002;31:279-292.
55
56.Rodriguez-Navarro A, Rubio F. High-affinity potassium and sodium transport systems in plants. J Exp Bot 2006;57:1149-1160.
56
57.Haro R, Banuelos MA, Senn ME, Barrero-Gil J, Rodriguez-Navarro A. HKT1 mediates sodium uniport in roots.Pitfalls in the expression of HKT1 in yeast. Plant Physiol 2005;139:1495-1506.
57
ORIGINAL_ARTICLE
In silico investigation of lactoferrin protein characterizations for the prediction of anti-microbial properties
Lactoferrin (Lf) is an iron-binding multi-functional glycoprotein which has numerous physiological functions such as iron transportation, anti-microbial activity and immune response. In this study, different in silico approaches were exploited to investigate Lf protein properties in a number of mammalian species. Results showed that the iron-binding site, DNA and RNA-binding sites, signal peptides and transferrin motifs in the Lf structure were highly conserved. Examined sequences showed three conserved motifs which were repeated twice in the Lf structure, demonstrating ancient duplication events in its gene. Also, results suggest that the functional domains in mammalian Lf proteins are Zinc finger, Tubulin/FtsZ, GTPase, α/β hydrolase and Zinc knuckle. The potential site for nucleic acid binding and the major DNA and RNA-binding sites in this protein were found in the lactoferricin (Lfc) fragment. Due to its high positive charge, Lf is able to bind a large number of compounds. Our analysis also revealed that the interactions between Lf and ITLN1, LYZ, CSN2, and CD14 proteins played an important role in the protective activities of Lf. Analysis for the prediction of secondary structures indicated that high amounts of α-helix, β-strand and β-sheet were present in Lf. The high degree of conservation among mammalian Lf proteins indicates that there is a close relationship between these proteins, reflecting their important role.
https://mbrc.shirazu.ac.ir/article_2001_7a8b871773bed61fd196efa9778ae619.pdf
2014-06-01
85
100
10.22099/mbrc.2014.2001
Bioinformatics tools
Mammalian species
Anti-microbial activity
Lactoferrin
Lactoferricin
In silico study
Seyyed Mohsen
Sohrabi
ms.seyyed@gmail.com
1
Institute of Biotechnology Shiraz university
AUTHOR
Ali
Niazi
niazi@shirazu.ac.ir
2
Head of Biotechnology Institute, Shiraz University, Shiraz, Iran
LEAD_AUTHOR
Mahmood
Chahardoli
m.chahardooli@gmail.com
3
Institute of Biotechnology Shiraz University
AUTHOR
Ali
Hortamani
hortamania@gmail.com
4
Institute of Biotechnology Shiraz University
AUTHOR
Payam
Setoodeh
payam_setoodeh@yahoo.com
5
Institute of Biotechnology Shiraz University School of Petroleum and Chemical engineering, Shiraz University, Shiraz, IR Iran
AUTHOR
1.Shanbacher FL, Goodman RE, Talhouk RS. Bovine mammary lactoferrin: Implications from messenger ribonucleic acid (mRNA) sequence and regulation contrary to other milk proteins. J Dairy Sci 1992; 76: 3812-3831.
1
2.Rodriguez DA, Vazquez L, Ramos G. Antimicrobial mechanisms and potential clinical application of lactoferrin [in Spanish]. Rev Latinoam Microbiol 2005; 47:102–11.
2
3.Wally J, Buchanan SK. A structural comparison of human serum transferrin and human lactoferrin. BioMetals 2007; 20: 249-262.
3
4.OztasYesim ER, Ozgunes N. Lactoferrin: a multifunctional protein. Adv Mol Med 2005; 1: 149-54.
4
5.Anderson BF, Baker HM, Dodson EJ, Norris GE, Rumball SV, Waters JM, Baker EN. Structure of human lactoferrin at 3.2-A° resolution. Proc Natl Acad Sci 1987; 84:1769-1773.
5
6.Khan JA, Kumar P, Paramasivam M, Yadav RS, Sahani MS, Sharma S, Srinivasana A, Singh TP. Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6 Å resolution and structural basis of its dual role. J Mol Biol 2001; 309: 751-761.
6
7.Baker HM, Anderson BF, Baker EN. Dealing with iron: common structural principles in proteins that transport iron and heme. Proc Natl Acad Sci USA 2004; 100: 3579-3583.
7
8.Van der Strate BWA, Belijaars L, Molema G, Harmsen MC, Meijer DK. Antiviral activities of lactoferrin. Antiviral Res 2001; 52: 225–39.
8
9.Ellison RT, Giehl TJ, Laforce FM. Damage of the membrane of enteric Gram-negative bacteria by lactoferrin and transferrin. Infect Immun 1988; 56: 2774-81.
9
10. Leitch EC, Willcox MDP. Elucidation of the antistaphylococcal action of lactoferrin and lysozyme. J med Microbial 1999; 48: 867-871.
10
11. Legrand D, Vigie K, Said EA, Elass E, Masson M, Slomianny MC. Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells. Eur J Biochem 2004; 271: 303-17.
11
12. Bennett RM, Davis J. Lactoferrin interacts with deoxyribonucleic acid: a preferential reactivity with double-stranded DNA and dissociation of DNA-anti-DNA complex. J Lab Clin Med 1982; 99: 127-38.
12
13. Yamauchi K, Wakabayashi H, Shin K, Takase M. Bovine lactoferrin: benefits and mechanism of action against infections. Biochem Cell Biol 2006; 84: 291-6.
13
14. Connely OM. Antiinflammatory activities of lactoferrin. J Am Coll Nutr 2001; 20: 389-95.
14
15. Kalmar JR, Arnold RR. Killing of Actinobacillus actinomycetemcomitans by human lactoferrin. Infect Immun 1988; 56: 2552-2557.
15
16. Baker EN. Structure and reactivity of transfer­rins. Advances in Inorganic Chemistry 1994; 41: 389-463.
16
17. Zarember KA, Sugui JA, Chang YC, Kwon-Chung KJ, Gallin JI. Human polymorpho nuclear leukocytes inhibit Aspergillus fumigates conidial growth by lactoferrin-mediated iron depletion. J Immunol 2007; 178: 6367-73.
17
18. Baker EN, Baker HM. Lactoferrin molecular structure, binding properties and dynamics of lactoferrin. Cell Mol Life Sci 2005; 62: 2531-9.
18
19. Utsugi T, Schroit AJ, Connor J, Bucana CD, Fidler IJ. Elevated expression of phosphatidyl serine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes. Cancer Res 1991; 51: 3062-3066.
19
20. Bellamy W, Takase M, Wakabayashi H. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 1992; 73:472-479.
20
21. Kanyshkova TG, Babina SE, Semenov DV, Isaeva N, Valssov AV, Neustroev KN. Multiple enzymatic activities of human milk lactoferrin. Eur J Biochem 2003; 270: 3353-61.
21
22. Bailey TL, Boden M, Buske FA, Frith M, Grant CE, Clementi L, Ren J, Li WW, Noble WS. MEME SUITE: tools for motif discovery and searching. Nucleic Acids Res 2009; 37: 202-208.
22
23. Rost B. protein secondary structure prediction continues to rise. J Struct Biol 2001; 134: 204-218
23
24. Yamauchi K, Tomita M, Giehl TJ, Ellison RT. Antibacterial activity of lactoferrin and a pepsin derived lactoferrin peptide fragment. Infect Immun 1993; 61: 719-728.
24
25. Felsenstein J. Confidence limits on phylogenies: An approach using the bootstrap. Evolution 1985; 39: 783–791
25
26. Wang L, Brown SJ. BindN: a web-based tool for efficient prediction of DNA and RNA binding sites in amino acid sequences. Nucleic Acids Res 2006; 34: 243-248.
26
27. Lambert LA, Perri H, Meehan TJ. Evolution of duplications in the transferrin family of proteins. Comp Biochem Physiol B Biochem Mol Biol 2005; 140: 11-25.
27
28. Marra AK, Jenssenb H, RoshanMoniria M, Hancock b REW, Pante N. Bovine lactoferrin and lactoferricin interfere with intracellular trafficking of Herpes simplex virus-1. Biochimie 2009; 91: 160-164.
28
29. Yi M, Kaneko S, Yu DY, Murakami S. Hepatitis C virus envelope proteins bind lactoferrin. J Virol 1997; 71: 5997-6002.
29
30. Geerts MEJ, Van Heen HA, Mericskay M, De Boer HA, Nuijens JH. N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. Biochem J 1997; 328: 145-151.
30
31. He J., Furmanski p. Sequence specificity and tran­scriptional activation in the binding of lactoferrin to DNA. Nature 1995; 373: 721–724.
31
32. Parillo JE. Pathogenetic mechanisms of septic shock. N Engl J Med 1993; 328:1471–1477.
32
33. Shin K, Wakabayashi H, Yamauchi K, Yaeshima T, Iwatsuki K. Recombinant Human Intelectin Binds Bovine Lactoferrin and Its Peptides. Biol Pharm Bull 2008; 3:1605-1608.
33
34. Ohashi A, Murata E. New functions of lactoferrin and β-casein in mammalian milk as cysteine protease inhibitors. Biochemical and Biophysical Research Communications 2003; 306: 98–103.
34
35. Orla M, Conneely PhD. Anti-inflammatory Activities of Lactoferrin. J Amer Col Nutri. 2001; 5: 389–395.
35
ORIGINAL_ARTICLE
A tri state mechanism for oxygen release in fish hemoglobin: Using Barbus sharpeyi as a model
Hemoglobin is a porphyrin containing protein with an a2b2 tetrameric structure and like other porphyrin compounds shows spectral behavior of species specific characteristics. Researchers tend to relate bands in the hemoglobin spectra to certain structural and/or functional features. Given the fact that hemoglobin is the main oxygen carrier in animals functioning through the Oxy«Deoxy equilibrium, the determination of oxy and deoxy conformations of hemoglobins of different animals may shed light on their oxygen binding properties. Absorption spectra at 280 and 373nm have been widely used to quantitate the formation of hemoglobin deoxy conformation. In the present work, however, we used an optical density ratio of OD373/OD280 as an index for deoxy formation. This ratio was determined for Barbus sharpeyi and human hemoglobins at different SDS concentrations, pH levels and temperatures to compare them from a structure-function point of view. Our data showed that under low concentrations of SDS (Barbus sharpeyi hemoglobin folds in a tri-state pattern while human hemoglobin folds through a two-state phenomenon. This finding indicates that in contrast to those of other non aquatic animals, the hemoglobin of Barbus sharpeyi has a loosely folded tetrameric structure with remarkably more oxygen affinity
https://mbrc.shirazu.ac.ir/article_2026_698d7d533bd10e1d0e27af8f9dff552f.pdf
2014-06-01
101
113
10.22099/mbrc.2014.2026
Barbus sharpeyi
Hemoglobin
Tri State Mechanism
Mohammad
Dayer
mrdayer@yahoo.com
1
Department of Biology, Faculty of Science, Shahid Chamran University, Ahvaz, Iran
LEAD_AUTHOR
Mohammad Saaid
Dayer
dayer@modares.ac.ir
2
Department of Parasitology and Medical Entomology, Tarbiat Modares University, Tehran, Iran
AUTHOR
Ali Akbar
Moosavi-Movahedi
moosavi@ut.ac.ir
3
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
AUTHOR
1.Nelson L, Cox M. Protein Function. In: Lehinger Principles of Biochemistry (4th Ed), Freeman WH and Company, New York, 2005.
1
2.Vasirev AS, Luk'yanenko VI. Spectrophotometrie parameters of conformational states of hemoglobin and its complexes with ligands in the sturgeons. J Evol Biochem Physiol 2000;36:5-10.
2
3.Nagatomo S, Jin Y, Nagai M, Hori H, Kitagawa T. Changes in the abnormal a-subunit upon CO-binding to the normal b-subunit of Hb M Boston: resonance Raman, EPR and CD study. Biophys Chem 2002;98:217-232.
3
4.Reinot T, Hayes JM, Small GJ, Zerner MC. Q-band splitting and relaxation of aluminum phthalocyanine tetrasulfonate. Chem Phys Lett 1999;299:410-416.
4
5.Eaton WA, Hofrichter J. Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods Enzymol 1981;76:175-261.
5
6.El-Nahass MM, Zeyada HM, Aziz MS, Makhlouf MM. Optical absorption of tetraphenylporphyrin thin films in UV-vis-NIR region. Spectrochimica Acta Part A 2005;62:11-15.
6
7.Mandal P, Bardhan M, Ganguly T. A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin. J Photochem Photobiol B 2010;99:78-86.
7
8.Akuwudike AR, Chikezie PC, Chilaka FC. Absorption spectra of normal adult and sickle cell haemoglobins treated with hydrogen peroxide at two pH values. Adv Biores 2010;1:55-60.
8
9.Dayer MR, Moosavi-Movahedi AA, Dayer MS. Band assignment in hemoglobin porphyrin ring spectrum: Using four-orbital model of Gouterman. Protein Pept Lett 2009;17:473-479.
9
10.Li R, Nagai Y, Nagai M. Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: near- and far-UV circular dichroism of isolated chains and recombined hemoglobin. J Inorg Biochem. 2000;82:93-101.
10
11. Zhu Y, Cheng G, Dong S. Structural electrochemical study of hemoglobin by in situ circular dichroism thin layer spectroelectrochemistry. Biophys Chem 2002;97:129-138.
11
12. Yokoyama T, Chong KT, Miyazaki G, Morimoto H, Shih DT, Unzai S, Tame JR, Park SY. Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect. J Biol Chem 2004;279:28632-28640.
12
13. Venkateshrao S, Manoharan PT. Conformational changes monitored by fluorescence study on reconstituted hemoglobins. Spectrochim. Acta Part A 2004; 60:2523-2526
13
14. Jin Y, Sakurai H, Nagai Y, Nagai M. Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding: a study of mutants at alpha 42, alpha 140, beta 145 tyrosine or beta 37 tryptophan. Biopolymers 2004;74:60-63.
14
15. Patel N, Seward HE, Svensson A, Gurman SJ, Thomson AJ, Raven EL. Exploiting the conformational flexibility of leghemoglobin: a framework for examination of heme protein axial ligation. Arch Biochem Biophys 2003;418:197-204.
15
16. Sage JT, Morikis D, Champion PM. Spectroscopic studies of myoglobin at low pH: heme structure and ligation. Biochemistry 1991;30:1227-1237.
16
17. Appleby CA. The separation and properties of low-spin (haemochrome) and native, high-spin forms of leghaemoglobin from soybean nodule extracts. Biochim Biophys Acta 1969;189:267-279.
17
18. Qiu Y, Maillett DH, Knapp J, Olson JS, Riggs AF. Lamprey hemoglobin. Structural basis of the Bohr effect. J Biol Chem 2000;275:13517-13528.
18
19. Giardina B, Mosca D, De Rosa MC. The Bohr effect of haemoglobin in vertebrates: an example of molecular adaptation to different physiological requirements. Acta Physiol Scand 2004;182:229-244.
19
20. Dumoulin A, Manning LR, Jenkins WT, Winslow RM, Manning JM. Exchange of subunit interfaces between recombinant adult and fetal hemoglobins. Evidence for a functional inter-relationship among regions of the tetramer. J Biol Chem 1997;272: 31326-31332.
20
21. Mylvaganam S, Bonaventura C, Bonaventura J, Getzoff ED. Structural basis for the root effect in haemoglobin. Nat Struct Biol 1996;3:275-283.
21
22. Verde C, Giordano D, Russo R, Riccio A, Coppola D, di Prisco G. Evolutionary adaptations in antarctic fish: the oxygen-transport system. Oecologia Australis 2011; 15:40-50.
22
23. Blanco E, Ruso JM, Sabín J, Prieto G, Sarmiento F. Thermodynamic study of the thermal denaturation of a globular protein in the presence of different ligands. J Therm Anal Cal 2007;87:143-147.
23
24. Val AL, Almeida-Val VMF, Affonso EG. Adaptative features of Amazon fishes: hemoglobins, hematology, intraerythrocytic phosphates and whole blood Bohr effect of Pterygoplichthys multiradiatus. Comp Biochem Physiol B 1990;97:435-440.
24
25. Dayer MR, Moosavi-Movahedi AA, Dayer MS, Mousavy SJ. Comparison of human and shirbot (Cyprinidae: Barbus grypus) hemoglobin: a structure-function prospective. Protein Pept Lett 2011;11:1072-1077.
25
26. Dayer MR, Moosavi-Movahedi AA, Norouzi P, Ghourchian HO, Safarian S. Inhibition of human hemoglobin autoxidation by sodium n-dodecyl sulphate. J Biochem Mol Biol. 2002;35:364-370.
26
27. Moosavi-Movahedi AA, Dayer MR, Norouzi P, Shamsipur M, Yeganeh-faal A, Chaichi MJ, Ghourchian HO. Aquamethemoglobin reduction by sodium n-dodecyl sulfate via coordinated water oxidation. Colloids and Surfaces B. Biointerfaces 2003;30:139-146.
27
28. William RC Jr, Tsay KY. A convenient chromatographic method for the preparation of human hemoglobin. Anal Biochem 1973;54:137-145.
28
29. Riggs A. Preparation of blood hemoglobins of vertebrates. Methods Enzymol 1981; 76:5-29.
29
30. Berman M, Benesch R, Benesch RE. The removal of organic phosphates from hemoglobin. Arch Biochem Biophys 1971;145:236-239.
30
31. Sugita Y, Nagai M, Yoneyama Y. Circular dichroism of hemoglobin in relation to the structure surrounding the heme. J Biol Chem 1971;246:383-388.
31
32. Harvey D. in Analytical Chemistry 2.0: An Electronic Textbook for Introductory Courses in Analytical Chemistry. 2009. http://acad.depauw.edu/harvey_web/eText %20Project/AnalyticalChemistry2.0.html
32
33. Moosavi-Movahedi AA. Thermodynamics of protein denaturation by sodium dodecyl sulfate. J Iran Chem Society 2005;2:189-196.
33
34. Chilaka FC, Nwamba CO, Moosavi-Movahedi AA. Cation modulation of hemoglobin interaction with sodium n-dodecyl sulfate (SDS). I: calcium modulation at pH 7.20. Cell Biochem Biophys 2011;60:187-197.
34
ORIGINAL_ARTICLE
Designing and analyzing the structure of Tat-BoNT/A(1-448) fusion protein: An in silico approach
Clostridium botulinum type A (BoNT/A) produces a neurotoxin recently found to be useful as an injectable drug for the treatment of abnormal muscle contractions. The catalytic domain of this toxin which is responsible for the main toxin activity is a zinc metalloprotease that inhibits the release of neurotransmitter mediators in neuromuscular junctions. A cell penetrating cationic peptide, Tat, which is a truncated N-terminal part of the Tat protein from human immunodeficiency virus, can help the toxin penetrate the skin uninvasively. This study aimed at an in silico analyses of the Tat-BoNT/A(1-448) fusion protein structure. A genomic construct was designed and optimized based on E. coli codon usage. The structure of mRNA as well as the properties of hypothetical chimeric protein was then analyzed by bioinformatic tools. Afterwards, the secondary and tertiary structures of the fusion protein were predicted by GOR4 and I-TASSER online web servers. The interaction with synaptosomal associated protein 25kDa (SNAP-25) was also analyzed as a natural substrate for the toxin. Based on the studied secondary and tertiary structures of the protein, the selected order of fusion proteins provides the natural activity of each peptide. Energy calculating data show that the acquired thermodynamic ensemble related to the mRNA structure was-1473.2 kJ/mol (-352.10 kcal/mol) and both total protein energy (Etotal) and shape related energy (Eshape) were calculated as -2294.2kJ/mol (-548.32 kcal/mol). The stability index of TAT-BoNT/A was computed to be 27.22 which has an acceptable stability as compared to that of native BoNT/A (22.39).
https://mbrc.shirazu.ac.ir/article_2038_4bd6673b01f2fb3a48ef1155ae3fbdd2.pdf
2014-06-01
115
127
10.22099/mbrc.2014.2038
In silico analysis
Botulinum neurotoxin
Cell penetrating peptides
(CPPs)
TAT peptide
Jafar
Amani
jafar.amani@gmail.com
1
Applied Microbiology Research center, Baqiyatallah University of Medical Sciences, Tehran, Iran.
AUTHOR
Parvaneh
Saffarian
seveneart@yahoo.com
2
Department of Bacteriology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran.
AUTHOR
Shahin
Najar-Pirayeh
3
Department of Bacteriology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran
AUTHOR
Abbas Ali
Imani-Fooladi
imanifouladi.a@gmail.com
4
Applied Microbiology Research center, Baqiyatallah University of Medical Sciences, Tehran, Iran.
LEAD_AUTHOR
1.Montecucco C, Molgo J (2005) Botulinal neurotoxins: revival of an old killer. Curr Opin Pharmacol 5:274-9
1
2.Proft T, editor. Microbial Toxins: Current Research and Future Trends: Horizon Scientific Press; 2009.
2
3.Thanongsaksrikul J, Chaicumpa W (2011) Botulinum neurotoxins and botulism: a novel therapeutic approach. Toxins (Basel) 3:469-88.
3
4.Yang Y, Xia Z, Liu Y (2000) SNAP-25 functional domains in SNARE core complex assembly and glutamate release of cerebellar granule cells. The Journal of biological chemistry 275:29482-7.
4
5.Dhaked RK, Singh MK, Singh P, Gupta P (2010) Botulinum toxin: bioweapon & magic drug. Indian J Med Res 132:489-503.
5
6.Turton K, Chaddock JA, Acharya KR (2002) Botulinum and tetanus neurotoxins: structure, function and therapeutic utility. Trends Biochem Sci 27:552-8.
6
7.Munchau A, Bhatia KP (2000) Uses of botulinum toxin injection in medicine today. BMJ 320:161-5.
7
8.Johnson EA (1999) Clostridial toxins as therapeutic agents: benefits of nature's most toxic proteins. Annu. Rev. Microbiol. 53:551-75.
8
9.Morris MC, Deshayes S, Heitz F, Divita G (2008) Cell-penetrating peptides: from molecular mechanisms to therapeutics. Biology of the cell / under the auspices of the European Cell Biology Organization 100:201-17.
9
10. Doolittle ED. Methods in Enzymology,R.F. 1996. p. 540-53.
10
11. Puigbo P, Guzman E, Romeu A, Garcia-Vallve S (2007) OPTIMIZER: a web server for optimizing the codon usage of DNA sequences. Nucleic Acids Res 35:W126-31.
11
12. Puigbo P, Romeu A, Garcia-Vallve S (2008) HEG-DB: a database of predicted highly expressed genes in prokaryotic complete genomes under translational selection. Nucleic Acids Res 36:D524-7.
12
13. Nazarian S, Mousavi Gargari SL, Rasooli I, Amani J, Bagheri S, Alerasool M (2012) An in silico chimeric multi subunit vaccine targeting virulence factors of enterotoxigenic Escherichia coli (ETEC) with its bacterial inbuilt adjuvant. Journal of microbiological methods 90:36-45.
13
14. Amani J, Mousavi SL, Rafati S, Salmanian AH (2009) In silico analysis of chimeric espA, eae and tir fragments of Escherichia coli O157:H7 for oral immunogenic applications. Theor Biol Med Model 6:28.
14
15. Zuker M (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31:3406-15.
15
16. Gruber AR, Lorenz R, Bernhart SH, Neubock R, Hofacker IL (2008) The Vienna RNA websuite. Nucleic Acids Res 36:W70-4.
16
17. Walker JM. The proteomics protocols handbook. Totowa, N.J.: Humana Press; 2005. xviii, 988 p. p.
17
18. Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5:725-38.
18
19. Zhang Y. I-TASSER server for protein 3D structure prediction [Research Support, Non-U.S. Gov't]. 2008 [cited 9]. 2008/01/25:[40]. Available from: http://www.ncbi.nlm.nih.gov/pubmed/18215316.
19
20. Roy A, Yang J, Zhang Y (2012) COFACTOR: an accurate comparative algorithm for structure-based protein function annotation. Nucleic Acids Res 40:W471-7.
20
21. Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4:363-71.
21
22. Lovell SC, Davis IW, Arendall WB, 3rd, de Bakker PI, Word JM, Prisant MG, et al. (2003) Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins 50:437-50.
22
23. Smialowski P, Martin-Galiano AJ, Mikolajka A, Girschick T, Holak TA, Frishman D (2007) Protein solubility: sequence based prediction and experimental verification. Bioinformatics 23:2536-42.
23
24. Ritchie DW (2008) Recent progress and future directions in protein-protein docking. Curr Protein Pept Sci 9:1-15.
24
25. Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40.
25
26. Asahi M, Rammohan R, Sumii T, Wang X, Pauw RJ, Weissig V, et al. (2003) Antiactin-targeted immunoliposomes ameliorate tissue plasminogen activator-induced hemorrhage after focal embolic stroke. Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 23:895-9.
26
27. Waugh A, Gendron P, Altman R, Brown JW, Case D, Gautheret D, et al. (2002) RNAML: a standard syntax for exchanging RNA information. Rna 8:707-17.
27
28. Rawat R, Ashraf Ahmed S, Swaminathan S (2008) High level expression of the light chain of botulinum neurotoxin serotype C1 and an efficient HPLC assay to monitor its proteolytic activity. Protein Expr Purif 60:165-9.
28
29. Mueller J, Kretzschmar I, Volkmer R, Boisguerin P (2008) Comparison of cellular uptake using 22 CPPs in 4 different cell lines. Bioconjug Chem 19:2363-74.
29
30. Rajagopalan R, Xavier J, Rangaraj N, Rao NM, Gopal V (2007) Recombinant fusion proteins TAT-Mu, Mu and Mu-Mu mediate efficient non-viral gene delivery. J Gene Med 9:275-86.
30
31. Yesylevskyy S, Marrink SJ, Mark AE (2009) Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers. Biophys J 97:40-9.
31
32. Thomas A, Lins L, Divita G, Brasseur R (2010) Realistic modeling approaches of structure-function properties of CPPs in non-covalent complexes. Biochim Biophys Acta 1798:2217-22.
32
ORIGINAL_ARTICLE
Heavy metal regulation of plasma membrane H+-ATPase gene expression in halophyte Aeluropus littoralis
The present study was conducted to find the effect of three heavy metals, Ag, Hg and Pb on the expression level of a gene encoding plasma membrane H+-ATPase in Aeluropus littoralis. The experiment was laid out in a completely random design with three replications. The expression of the main gene was normalized to the expression of the housekeeping gene actin. Two 259 and 187 bp fragments were amplified from plasma membrane H+-ATPase and actin genes using specific primers in polymerase chain reactions. The results indicated that higher concentrations of all three heavy metals declined the expression of plasma membrane H+-ATPase gene, whereas low concentrations changed the level of its transcript differently. A significant linear correlation was found between Ag concentrations of Aeluropus littoralis shoots and its external level; however, for Hg and Pb no correlations were observed. Root weight decreased when plants were grown at both concentrations of Ag and Hg but increased at both concentrations of Pb and NaCl. Maximum root weight was observed under lower levels of Pb, while maximum shoot weight was observed under lower levels of Hg. The greatest plant weight was obtained at low concentrations of Hg and Pb. Taken together these results show the regulation of plasma membrane H+-ATPase gene by heavy metals suggesting that Aeluropus littoralis can be regarded as a Phytoremediation accumulator of soils polluted with heavy metals.
https://mbrc.shirazu.ac.ir/article_2119_f2dd881de4925a723f0814cbca531085.pdf
2014-06-01
129
139
10.22099/mbrc.2014.2119
Gouan
lead
Mercury
Proton pump
Silver
Mohsen
Jam
mjam_62@yahoo.com
1
Department of Crop Production and Plant Breeding, College of Agriculture, Shiraz University, Shiraz, Iran
AUTHOR
Abbas
Alemzadeh
alemzadeh@shirazu.ac.ir
2
Department of Crop Production and Plant Breeding, College of Agriculture, Shiraz University, Shiraz, Iran
LEAD_AUTHOR
Ali Mohammad
Tale
ali.m.tale@gmail.com
3
Department of Crop Production and Plant Breeding, College of Agriculture, Shiraz University, Shiraz, Iran
AUTHOR
Sara
Esmaeili-Tazangi
sa.esmaeili7z@gmail.com
4
Biotechnology Department, School of Agriculture, Shahid Bahonar University, Kerman, Iran
AUTHOR
1.Sanita DI, Toppi L, Gabbrieli R. Response to cadmium in higher plants. Environ Exp Bot 1999;4:105- 130.
1
2.Wagner GJ. Accumulation of cadmium in crop plants and its consequences to human health. Adv Agron 1993;51:173-212
2
3.Haag-Kerwer A, Schäfer HJ, Heiss S, Walter C, Rausch T. Cadmium exposure in Brassica juncea causes a decline in transpiration rate and leaf expansion without effect on photosynthesis. J Exp Bot 1999;50:1827-1835.
3
4.Alloway BJ, Jackson AP. The behaviour of heavy metals in sewage sludge-amended soils. Sci Total Environ 1991;100:151-176.
4
5.Yadav SK. Heavy metals toxicity in plants: An overview on the role of glutathione and phytochelatins in heavy metal stress tolerance of plants. S Afr J Bot 2010;76(2):167-179.
5
6.Cargnelutti D, Tabaldi LA, Spanevello RM, Jucoski GO, Battisti V. Toxicity induces oxidative stress in growing cucumber seedlings. Chemosphere 2006;65:999-1006.
6
7.Zhou ZS, Huang SQ, Gouk-Mehta SK. Metabolic adaptations to Hg-induced oxidative stress in roots of alfalfa. J Inorg Biochem 2007;101:1- 9.
7
8.Morsomme P, Boutry M. The plant plasma membrane H+-ATPase: structure, function and regulation. Biochim Biophys Acta 2000;1465:1-16.
8
9.Devi S, Prasad M. Heavy metal stress in plants. From molecules to ecosystems. Second Edition. Springer.Berlin1999;pp.99-116.
9
10.Breckle SW, Kahle H. Effects of toxic heavy metals (Cd, Pb) on growth and mineral nutrition of beech (Fagus sylvatica L.). Plant Ecol 1992;101:43-53.
10
11.Serrano R, Gaxiola R. Microbial models and salt stress tolerance in plants. Crit Rev Plant Sci 1994;13:121–138.
11
12.Korashy HM, El-Kadi AOS. Regulatory mechanisms modulating the expression of cytochrome P450 1A1 gene by heavy metals. Toxicol Sci 2005:88(1):39-51.
12
13.Woo S, Yum S, Park HS, Lee TK, Ryu JC. Effects of heavy metals on antioxidants and stress-responsive gene expression in Javanese medaka (Oryzias javanicus). Comp Biochem Phys C 2009;149(3):289-299.
13
14.Jonak C, Nakagami H, Hirt H. Heavy metal stress. Activation of distinct mitogen-activated protein kinase pathways by copper and cadmium. Plant Physiol 2004;136(2):3276-3283.
14
15.DalCorso G, Farinati S, Maistri S, Furini A. How plants cope with cadmium: staking all on metabolism and gene expression. J Integ Plant Biol 2008;50(10):1268-1280.
15
16.Janicka-Russak M, Kabata K, Burzyński M, Ktobus C. Response of plasma membrane H+-ATPase to heavy metal stress in Cucumis sativus roots. J Exp Bot 2008;59(13):3721-3728.
16
17.Kabata K, Janicka-Russak M, Burzyński M, Ktobus C. Comparison of heavy metal effect on the proton pumps of plasma membrane and tonoplast in cucumber root cells. J Plant Physiol 2007;165:278-288.
17
18.Wang RZ. Plant functional types and their ecological responses to salinization in saline grasslands,Northeastern China. Photosynthetica 2004;42:511-519.
18
19.Rastgoo L, Alemzadeh A. Biochemical response of gouan (Aeluropus littoralis) to heavy metals stress. Aust J Crop Sci 2011;5(4):375-383.
19
20.Rezvani M, Zaefarian F, Miransari M, Nematzadeh GA. Uptake and translocation of cadmium and nutrients By Aeluropus littoralis. Arch Agron Soil Sci 2012;58(12):1413-1425.
20
21.Rastgoo L, Alemzadeh A, Afsharifar A. Isolation of two novel isoforms encoding zinc- and copper transporting P1B-ATPase from gouan (Aeluropus littoralis). Plant Omics J 2011;4 (7):377-383.
21
22.Morel M, Crouzet J, Gravot A, Auroy P, Leonhhardt N, Vavasseur A, Richaud P. AtHMA3 a P1B-ATPase allowing Cd/Zn/Co/Pb vacuolar storage in Arabidopsis. Plant Physiol 2009;149:894-904.
22
23.Wang C, Zhang SH, Wang PF, Qian J, Hou J, Zhang WJ, Lu J. Excess Zn alters the nutrient uptake and induces the antioxidative responses in submerged plant Hydrilla verticillata (L.f.) Royle. Chemosphere 2009;76 (7):938-945.
23
24.Chapman HD, Pratt PF. Methods for analysis for soils, plants and waters.Berkeley,UniversityofCalifornia, Division of Agricultural Science 1961;pp.71-85.
24
25.Sayed SA. Effects of lead and kinetin on the growth, and some physiological components of safflower. Plant Growth Regul 1999;29:167-174.
25
26.Liu D, Jiang W, Wang W, Zhao F, Lu C. Effects of lead on root growth, cell division, and nucleolus of Allium cepa. Environ Pollut 1994;86(1):1-4.
26
27.Brandt AP, Karlsson ML, Wennergren U. Lettuce growth in silver laden soil at two different activity levels of soil microorganisms. J Appl Bot Food Qual 2005;79:33-37.
27
28.Maggio A, Reddy MP, Joly RJ. Leaf gas exchange and solute accumulation in the halophyte Salvadora persica grown at moderate salinity. Environ Exp Bot 2000;44(1):31-38.
28
29.Benlloch-González M, Fournier JM, Ramos J, Benlloch M. Strategies underlying salt tolerance in halophytes are present in Cynara cardunculus. Plant Sci 2005;168:653-659.
29
30.Liu T, Liu S, Guan H, Ma L, Chen Z, Gu H, QU LJ. Transcriptional profiling of Arabidopsis seedlings in response to heavy metal lead (Pb). Environ Exp Bot 2009;67(2):377-386.
30
31.Lee M, Lee K, Lee J, Noh EW, Lee Y. AtPDR12 contributes to lead resistance in Arabidopsis. Plant Physiol 2005;138(2):827-836.
31
32.De Filippis LF, Pallaghy CK. The effect of sub-lethal concentrations of mercury and zinc on Chlorella l. growth characteristics uptake of metals. Z Pflanzenphysiol 1976;78(3): 197-207.
32
33.Golldack D, Dietz KJ. Salt-induced expression of the vacuolar H+-ATPase in the common ice plant is developmentally controlled and tissue specific. Plant Physiol 2001;125:1643-1654.
33
34.López Pérez L, Martínez-Ballesta MC, Maurel C, Carvajal M. Changes in plasma membrane lipids, aquaporins and proton pump of broccoli roots, as an adaptation to salinity. Phytochemistry 2009;70:492-500.
34
35.Islam E, Yang X, Li T, Liu D, Jin X, Meng F. Effect of Pb toxicity on root morphology, physiology and ultrastructure in the two ecotypes of Elsholtzia argyi. J Hazard Mater 2007;147:806-816.
35
ORIGINAL_ARTICLE
Effects of associated SCF and G-CSF on liver injury two weeks after liver damage: A model induced by thioacetamide administration
The present study aimed at investigating the beneficial effects of co-administering granulocyte colony–stimulating factor (G-CSF) and stem cell factor (SCF) in a model of chronic liver injury induced by thioacetamide (TAA). Biochemical and histopathology- cal examinations were performed on serum and liver specimens. At the end of the treatment period, the rats were anesthetized with ether, serum was collected and sections of randomly selected fixed liver specimens from each group were embedded in paraffin and processed for light microscopy by staining individual sections with hematoxylin-eosin (HE) stain. Administration of a combination of G-CSF+SCF was carried out two weeks after the TAA treatment. Livers of rats treated with TAA alone exhibited damage, which was significantly less in the group treated with the combination of SCF and G-CSF. Albumin level was 2.35 (g/dl) in the G-CSF+SCF and 1.03 in the TAA-alone group. These differences were statistically significant (P0.05). The albumin level was 2,35 (g/dl) in the G-CSF +SCF and versus 1.03 in the TAA-alone group. These differences in the albumin level were statistically significant (P0.05).
https://mbrc.shirazu.ac.ir/article_2194_2f62da33098684d105c4d63f8909feb4.pdf
2014-06-01
141
147
10.22099/mbrc.2014.2194
Granulocyte colony–stimulating factor
Liver injury
Stem cell factor
Thioacetamide
Mohsen
Esmaili
1
Department of Biochemistry and Biophysics, Faculty of Medicine, Babol University of Medical Sciences, Babol, Iran
AUTHOR
Durdi
Qujeq
dqujeq@gmail.com
2
Cellular and Molecular Biology Research Center (CMBRC), Babol University of Medical Sciences, Babol, Iran
LEAD_AUTHOR
Ali Asghar
Yoonesi
3
Department of Biochemistry and Biophysics, Faculty of Medicine, Babol University of Medical Sciences, Babol, Iran
AUTHOR
Farideh
Feizi
4
Department of Anatomical Sciences, Faculty of Medicine, Babol University of Medical Sciences, Babol, Iran
AUTHOR
Mohammad
Ranaee
5
Department of Pathology, Faculty of Medicine, Babol University of Medical Sciences, Babol, Iran
AUTHOR
1.Li N, Zhang L, Li H, Fang B. Human CD34
1
+ cells mobilized by granulocyte colony-stimulating factor ameliorate radiation-induced liver damage in mice. Stem Cell Res Ther 2010;1:1-8.
2
2.Zhang L, Kang W, Lei Y , Han Q, Zhang G, Lv Y, Li Z , Lou S, Liu Z. Granulocyte colony-stimulating factor treatment ameliorates liver injury and improves survival in rats with d-galactosamine-induced acute liver failure. Toxicol Lett 2011;204:92-99.
3
3.Takayama H, Miyake Y, Nouso K, Ikeda F, Shiraha H, Takaki A, Kobashi H, Yamamoto K. Serum levels of platelet-derived growth factor-BB and vascular endothelial growth factor as prognostic factors for patients with fulminant hepatic failure. J Gastroenterol Hepatol 2011;26:116-121.
4
4.Orlic D, Kajstura J, Chimenti S, Limana F, Jakoniuk I, Quaini F, Nadal-Ginard B, Bodine DM, Leri A, Anversa P. Mobilized bone marrow cells repair the infracted heart , improving function and survival. Proc Natl Acad Sci USA 2001;98:10344-10349.
5
5.Andrews RG, Briddell RA, Knitter Gh, Rowley SO, Appelbaum FR, Mc Niece IK. Rapid engraftment by peripheral blood progenitor cells mobilized by recombinant human stem cell factor and recombinant human granulocyte colony-stimulating factor in non human primates. Blood 1995;85:15-20.
6
6.Hunter AL, Holscher MA, Neal RA. Thioacetamide-induced hepatic necrosis: I. Involvement of the mixed function oxidase enzyme system. J Pharmacol Exp Ther 1977;200:439-448.
7
7.Porter WR, Neal RA. Metabolism of thioacetamide and thioacetamide S-oxide by rat liver microsomes. Drug Metab Dispos 1978;6:379-388.
8
8.Fitzhugh OG, Nelson AA. Liver tumors in rats fed thiourea or thioacetamide. Science1948;108:626-628.
9
9.Trennery PN, Waring RH. Early changes in thioacetamide induced liver damage.
10
Toxicol Lett 1983;19:299-307.
11
10. Qujeq D, Abassi R, Faeizi F, Parsian H, Sohan-Faraji A, Taheri H, Tatar M, Elmi MM, Halalkhor S. Effect of granulocyte colony-stimulating factor administration on tissue regeneration due to carbon tetrachloride–induced liver damage in experimental model. Toxicol Ind Health 2012;29:498-503.
12
11. Qujeq D, Abassi R, Faeizi F, Parsian H, Tahhery H, Halallkhor S. Effect of granulocyte colony-stimulating factor on liver injury induced by CCl
13
4: A correlation between biochemical parameter. Kuwait Med J 2012;44:46-49.
14
12. Qujeq D, Abassi R, Faeizi F, Parsian H, Faraji A, Tatar M, Elmi M, Halalkhor S, Tahhery H. Assessment effect of granulocyte colony-stimulating factor in experimental models of liver injury. Sci Res Essays 2011;6:4646-4650.
15
13. Liu F, Pan X, Chen C, Jiang D, Cong X, Fei R, Wei L. Hematopoietic stem cells mobilized by granulocyte colony-stimulating factor partly contribute to liver graft regeneration after partial orthotopic liver transplantation. Liver Transpl 2006;12: 1129-1137.
16
14. Ekam VS, Johnson JT, Dasofunjo K, Odey MO, Anyahara SE. Total protein, albumin and globulin levels following the administration of activity directed fractions of
17
Vernonia amygdalina during acetaminophen induced hepatotoxicity in wistar rats .Ann Biol Res 2012;3:5590-5594.
18
15. Yoonesi A, Qujeq D, Esmaili M, Feizi F. Effects of combination of G-CSF and SCF one week prior to liver injury in acute liver damage model induced by thioacetamide admistration. Res Mol Med 2014,1:1-5.
19
16. Theocharis SE, Papadimitriou LJ, Retsou ZP, Margeli AP, Ninos SS, Papadimitriou JD. Granulocyte colony stimulating factor administration ameliorates liver regeneration in animal model of fulminant hepatic failure and encephalopathy. Dig Dis Sci 2003;48:1797-1803.
20
17. Yannaki E, Athanasiou E, Xagorari A, Constantinou V, Batsis I, Kaloyannidis P, Proya E, Anaqnostopoulos A, Fassas A. G-CSF-primed hematopoietic stem cells or G-CSF per se accelerate recovery and improve survival after liver injury, predominantly by promoting endogenous repair programs. Exp Hematol 2005;33: 108-119.
21
18. Theocharis SE, Margeli AP, Kittas CN. Effect of granulocyte colony-stimulating-factor administration on tissue regeneration due to thioacetamide-induced liver injury in rats. Dig Dis Sci 1999;44:1990-1996.
22
19. Caraceni P, Giannone F, Catani L, Talarico S, Pertosa M, Domenicali M, Fogli M, Principe A, Trevisani F, Baccarani M, Bernardi M, Lemoli RM. Liver, pancreas and biliary tract effects of granulocyte colony stimulating-factor in a rat model of acute liver injury. Dig Liver Dis 2007;39:943-951.
23