ORIGINAL_ARTICLE
Therapeutic Potential of Glucose Regulated Protein 78 in Cancer
Endoplasmic reticulum has a critical role in the synthesis and folding of secretory and membrane proteins. High accumulation of proteins in ER activates the unfolded protein response and glucose regulated protein 78 or GPR78 plays an essential role in this pathway. Unfolded protein response is activated in cancerous cells due to their adverse condition to survive and it has been shown that GRP78 can be expressed in tumor cell membrane. Overexpresion and localization of GRP78 makes it a suitable target for the treatment of cancer. This review describes cellular localization, biological function, and role of GRP78 in cancer induction. Methods for tumor inhibition via GRP78 are also discussed.
https://www.biotechrep.ir/article_69195_953e78cc29570628a9fba31a0d35ebfd.pdf
2015-12-01
305
310
GRP78
Biological Function
cancer
Tumor
Hosssein
Aghamollaei
1
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Seyed Latif
Mousavi Gargari
slmousavi@shahed.ac.ir
2
Department of Biology, Faculty of Basic Science, Shahed University, Tehran Iran
LEAD_AUTHOR
Mostafa
Ghanei
3
Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
ORIGINAL_ARTICLE
Cotton Ovule Culture: A Tool for Biological and Biotechnological Studies of Cotton
Cotton is one of the most important crops in the world and increasing cotton yield is the main goal in the cotton industry. One important factor for crop improvement is increasing produced fibers by each developing seed. It is very interesting to manipulate fiber properties such as length, micronaire, color and strength which necessitate cotton ovule culture. Ovule culture is used as a tool to study physiology and biochemistry of secondary cell wall synthesis, effects of plant growth regulators, nutrition and environmental conditions on fiber and ovule development, inter-specific hybridization and embryo recue. This technique can be used for analysis of functional genes in fibers as transient expression systems. In this regard, fiber-specific promoters should be identified in developing fibers. Optimum growth regulator combinations can increase fiber yield and uniformity in vitro conditions. Despite mature ovules exogenous Indole-3-acetic acid and gibberellic acid are required for fiber development of unfertilized ovules in vitro condition even though these two hormones also induce fiber production in fertilized ovules. On the whole cotton ovule culture can be used as a model before permanent cotton transformation and field trials.
https://www.biotechrep.ir/article_69196_a6a1a4e06ef894702653334bb3faad7b.pdf
2015-12-01
311
314
Ovule Culture
cotton
Transformation
Fiber
Maryam
Behnam
1
Department of Biotechnology, Faculty of Agricultural Sciences, Payam Nour University, Tehran, Iran
AUTHOR
Seyed Javad
Davarpanah
davarpanah@bmsu.ac.ir
2
Applied Biotechnology Research Center, Baqiyatallah University of Medical Science, Tehran, Iran
LEAD_AUTHOR
Ramin
Karimian
karimian.r@gmail.com
3
Applied Biotechnology Research Center, Baqiyatallah University of Medical Science, Tehran, Iran
AUTHOR
ORIGINAL_ARTICLE
Computer Aided Design of a Luciferase Like Haloalkane Dehalogenase Enzyme by Homology Based Rational Protein Design (HRPD) Method
Rational protein design is an important aspect to introduce novel characters to the enzymes. In this report, we describe a procedure for in-silico design of a novel haloalkane dehalogenase protein that exhibits luciferase property, which can be potentially used in biosensor applications. The haloalkane dehalogenase have a close structural homology with a lucifearse was used as the starting structure for design. Amino acids that are frequently interacts with the chromophre (colentrizine) was analyzed by docking and molecular dynamics simulation. The amino acids Asp170, Lys192, Arg193, Lys259, and Lys261 were selected in the enzyme structure for substitution purpose to generate mutant enzyme. Following several selection strategies, it was observed that the protein substituted with Phe in all the positions is the best one which was further validated by a 10 ns molecular dynamics simulation. The designed protein is then analyzed for its substrate specificity towards 10 selected toxic haloalkane compounds. The result shows, that the designed protein has also improved the substrate specificity towards four toxic pollutants.
https://www.biotechrep.ir/article_69197_06a6b4d042c02067406af8a9a2f78a80.pdf
2015-12-01
315
323
Protein Design
Chromophore
Luciferase
Haloalkane Dehalogenase
Docking
Mo-lecular Dynamics Simulation
Raghunath
Satpathy
rnsatpathy@gmail.com
1
School of Life science, Sambalpur University, Jyoti vihar, Burla, Odisha, India
LEAD_AUTHOR
V. Badireenath
Konkimalla
2
School of Biological Sciences, National Institute of Science Education and Research (NISER), Bhubaneswar, Odisha, India
AUTHOR
Jagnyeswar
Ratha
3
School of Life science, Sambalpur University, Jyoti vihar, Burla, Odisha, India
AUTHOR
ORIGINAL_ARTICLE
Colchicine Induced Embryogenesis in Date Palm (Phoenix dactylifera L.) Anther Culture
An efficient method to produce doubled haploid plants of date palm (Phoenix dactylifera L.) was established using in vitro colchicine treatment of anthers. For this study end male in florescences were harvested in the appropriate developmental stage. Separated anthers after one day cold (4°C) pretreatment, in uninucleate stage of microspore were transferred to the modified Y3 medium containing different concentrations of colchicines (125- 250-500- 1000 mg/L) for one of four treatment durations (12- 24- 36- 48 hours) and were compared to control anthers (without colchicine treatment). Based on results, different concentrations of colchicine, different exposure times and their interaction had a significant different effect on callus induction. No callus and embryo were produced from control anthers; however, the callus and embryo were induced from colchicine-treated anthers. Among used concentration in the1000 mg/L and 125 mg/L colchicine, the rate of callus induction was very low. In contrast concentration of 500 mg/L and duration of 12 hours had the highest rate of callus induction. In concentration of 500 mg/L and duration of 36 hours some direct embryos were observed. These results indicate that the colchicine treatment of date palm anthers can induce callus and embryo for the production of doubled haploid lines.
https://www.biotechrep.ir/article_69198_8dcf12e7ad533bfe4559e1364f72b8be.pdf
2015-12-01
325
331
Anther Culture
Date Palm
Colchicine Treatment
Haploids
Somatic Embryogenesis
Fatemeh
Farhadi Kolahkaj
1
Department of Plant Biotechnology, Ramin University of Agriculture and Natural Resources, Ahvaz, Iran
AUTHOR
Payam
Pour Mohammadi
mohammadi@ramin.ac.ir
2
Department of Agronomy and Plant Breading, Ramin University of Agriculture and Natural Resources, Ahvaz, Iran
LEAD_AUTHOR
Mohammad
Farkhari
3
Department of Agronomy and Plant Breading, Ramin University of Agriculture and Natural Resources, Ahvaz, Iran
AUTHOR
Khalil
Alami-Saeid
4
Department of Plant Biotechnology, Ramin University of Agriculture and Natural Resources, Ahvaz, Iran
AUTHOR
ORIGINAL_ARTICLE
Synthesis of Copper (II) Oxide (CuO) Nanoparticles and Its Application as Gas Sensor
Copper sulfate was used as a precursor to prepare CuO nanoparticles in reverse micelles (o/w microemulsion). This is a technique which allows the preparation of ultrafine metal oxide nanoparticles within the size ranging from 50 to 60 nm. The preparation of nano copper (II) oxide studied was investigated in the inverse microemulsion system. Therefore the nucleation of metal particles proceeds in the water capsules of the microemulsion. Tween 80 was added as surfactant. The products were characterized by X-ray diffraction (XRD), scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The study provides a simple and efficient route to synthesize CuO nanoparticles at room temperature.
https://www.biotechrep.ir/article_69202_e635cabd52ca76595f432e1abbdde2e8.pdf
2015-12-01
329
332
CuO
Nanoparticle
Reverse Micelle
Gas Sensor
Seyed Javad
Davarpanah
davarpanah@bmsu.ac.ir
1
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Ramin
Karimian
karimian.r@gmail.com
2
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Farideh
Piri
3
Department of Chemistry, Faculty of Science, Zanjan University, Zanjan, Iran
AUTHOR
ORIGINAL_ARTICLE
Report on Biotechnological Applications of Proteolytic Enzymes from Lattices of Euphorbian Plants
Proteases catalyze the hydrolysis of peptide bonds in proteins. They are widely distributed in nature, nearly in all plants, animals and microorganisms. Plant latex is a rich source of proteases. Latex production is unique property of Euphorbian plant, which could be a potential source of proteolytic enzymes. The highest proteolytic activity was observed in the latex of Pedilanthus tithymaloides Linn., which is followed by lattices of Euphorbia tirucalli Linn., Euphorbia nivulia Buch.-Ham., and Euphorbia nerifolia Linn. Therefore, P. tithymaloides, E. tirucalli, E. nivulia, and E. nerifolia lattices were selected as potential sources of proteases. These proteases were effectively used to remove hair from goat skin indicating its potential in leather processing industry. These proteolytic enzymes showed potential environmental waste management applications such as degradation of chicken feather waste. Additionally, the crude enzymes of the selected plants exhibited potent gelatinolytic activity almost correlated to release of silver from waste X–ray film. They also showed remarkable destaining property, indicating their importance in detergent industry. These enzymes have remarkable silk degumming property demonstrating their use in textile industries.
https://www.biotechrep.ir/article_69203_2f2e441b9d348b03c0c2ccb31cb18289.pdf
2015-12-01
33
337
Plant Protease
Latex
Euphorbiaceae
Biotechnological Applications
Raghunath
Mahajan
rt_mahajan@rediffmail.com
1
Department of Zoology, Moolji Jaitha College, Jalgaon , India
LEAD_AUTHOR
Gunjan
Chaudhari
2
Department of Biochemistry, Moolji Jaitha College, Jalgaon, India
AUTHOR
Manoj
Chopadaa
3
Department of Zoology, Moolji Jaitha College, Jalgaon, India
AUTHOR
ORIGINAL_ARTICLE
Enzymatic Degradation of Organophosphate Compounds: Evaluation of High-level Production, Solubility and Stability
The use of organophosphorus hydrolase (OPH) enzyme to degrade Chemical Warfare Agents is one of the most frequently used decontamination methods. OPH is a ~36 kDa homodimeric metalloprotein that is found in the membrane of Flavobacterium sp. strain ATCC 27551 and Brevundimonas diminuta MG and is capable of hydrolyzing a wide range of oxon and thion , such as paraoxon and parathion. OPH gene (opd) has been expressed in many hosts, such as bacteria, insect cells, fungi, and Streptomyces spp. High level and soluble expression and correct folding of each protein are of important factors. Fusion proteins, including TRX, Gb1 and MBP, are commonly used to increase solubility, folding and in some cases, stability. The present study evaluated thioredoxin (TRX) role in OPH expression level, solubility and stability by cloning the opd gene into pET32a and pET21a and expressing the resulting vectors in E. coli shuffle T7. The pET32a vector encodes a fusion protein containing TRX that is not present in the pET21a. The results revealed an increased expression level, solubility and stability in OPH produced by the pET32a-opd construct compared to the pET21a vector due to the presence of the TRX fusion in pET32a vector.
https://www.biotechrep.ir/article_69204_efb018f085b44db307334f4fa6f3234d.pdf
2015-12-01
339
344
Organophosphorus Hydrolase
Thioredoxin
pET32a-opd
High Level Production
Solubility
Stability
Gholamreza
Farnoosh
rzfarnoosh@yahoo.com
1
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Ali Mohammad
Latifi
amlatifi290@gmail.com
2
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Khosro
Khajeh
3
Department of Biochemistry, Faculty of Biologic Science, Tarbiat Modares University, Tehran, Iran
AUTHOR
Hossein
Aghamollaei
aghamolaei22@gmail.com
4
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Ali
Najafi
najafi74@ibb.ut.ac.ir
5
Molecular Biology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR