Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add filters








Language
Year range
1.
JBUMS-Journal of Birjand University of Medical Sciences. 2017; 23 (4): 22-30
in English | IMEMR | ID: emr-189797

ABSTRACT

Background and Aim: Jujube [Ziziphus Jujuba Mill.] is one of the medicinal herbs with grows in dry and semi-dry areas in Iran; mainly in the South Khorasan province. The present study aimed at evaluating antioxidant and free radical scavenging capacity in different types of Jujuba


Materials and Methods: Four ecotypes of Jujubes were collected from different parts of the South Khorasan providence [Sarayan, Quaen, Arish, and Boshad]. The collected samples were air dried and then their aqueous extract was prepared in different dilutions. Anti-oxidant and free radical scavenging capacity of the samples were assessed using 2,2-diphenyl-1-picrylhydrazyl [DPPH] and Ferric Reducing Antioxidant Power [FRAP] methods. Their AAPH-induced hemolysis prevention was also analyzed. The total phenolic content of the samples was assessed using Folin-Ciocalteau method


Results: Maximum phenolic content was obtained from Quaen Jujube [1317+/-4.3 equal to mol Gallic acid]


The highest antioxidant capacity by FRAP [1390.1 +/- 65.5mol/L] also belonged to Quaen jujube. The ability of Arish Jujube extracts in scavenging and neutralizing free radical, tested by DPPH, was always higher compared to the other extracts. Results obtained from the effects of different dilutions of Jujube extracts [0- 25 - 5 mg/ml] on hemolysis showed a dose dependent relationship. All the extracts showed dose dependent reducing hemolysis in a specific range of concentrations, induced by 2,2'-azobis [2-amidinopropane] dihydrochloride [AAPH]. There was no significant statistical difference between jujube ecotypes in preventing hemolysis


Conclusion: According to total phenolic content of the Jujobe extracts, its significant antioxidant properties and radical scavenging activities, which was tested through different methods, it can be a potential booster for anti-oxidant capacities


Subject(s)
Antioxidants , Plant Extracts , Phytotherapy , Plants, Medicinal , Hemolysis , Free Radical Scavengers , Amidines
2.
Cell Journal [Yakhteh]. 2015; 16 (4): 466-475
in English | IMEMR | ID: emr-154849

ABSTRACT

Many studies have focused on the epigenetic characteristics of donor cells to improve somatic cell nuclear transfer [SCNT]. We hypothesized that the epigenetic status and chromatin structure of undifferentiated bovine adipose tissue-derived stem cells [BADSCs] would not remain constant during different passages. The objective of this study was to determine the mRNA expression patterns of DNA methyltransferases [DNMT1, DNMT3a, DNMT3b] and histone deacetyltransferses [HDAC1, HDAC2, HDAC3] in BADSCs. In addition, we compared the measured levels of octamer binding protein-4 expression [OCT4] and acetylation of H3K9 [H3K9ac] in BADSCs cultures and different passages in vitro. In this experimental study, subcutaneous fat was obtained from adult cows immediately post-mortem. Relative level of DNMTs and HDACs was examined using quantitative real time polymerase chain reaction [q-PCR], and the level of OCT4 and H3K9ac was analyzed by flow cytometry at passages 3 [P3], 5 [P5] and 7 [P7]. The OCT4 protein level was similar at P3 and P5 but a significant decrease in its level was seen at P7. The highest and lowest levels of H3K9ac were observed at P5 and P7, respectively. At P5, the expression of HDACs and DNMTs was significantly decreased. In contrast, a remarkable increase in the expression of DNMTs was observed at P7. Our data demonstrated that the epigenetic status of BADSCs was variable during culture. The P5 cells showed the highest level of stemness and multipotency and the lowest level of chromatin compaction. Therefore, we suggest that P5 cells may be more efficient for SCNT compared with other passages


Subject(s)
Animals , DNA Methylation , Histones , RNA, Messenger , Adipose Tissue , Histone Deacetylase 1 , Histone Deacetylase 2 , Histone Deacetylases , Cattle
SELECTION OF CITATIONS
SEARCH DETAIL