Genome-Wide Identification and Expression Profiling Analysis of the Trihelix Gene Family Under Abiotic Stresses in Medicago truncatula
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Genome-Wide Identification and Expression Profiling Analysis of the Trihelix Gene Family Under Abiotic Stresses in Medicago truncatula
The TRIHELIX Transcription FACTOR (GT) family is widely involved in the regulation of growth and plant development, especially, responding to various abiotic stresses. Our study first reported the identification and analysis of the genome of the GT family genes in Medicago Trucuma. Overall, 38 trihelix genes have been identified in the genome of Mr. Truncutatula and have been classified into five sub-reflection (GT-1, GT-2, SH4, GTγ and SIP1). We systematically analyze the phylogenetic relationship, chromosomal distribution, tandem and segmental duplication events, genes structures and stored motives of MTGT.
The syten analysis revealed that the genes of the trihelix family of Mr. Truncutule had the most collinearity relationship with soybeans, followed by alfalfa, but very little collinearity with those of corn and rice. In addition, an expression analysis specific to a fabric of the trihelix family genes suggested playing various roles in the growth and development of specific tissues of Mr. Truncutule. In addition, the expression of certain MTGT genes, such as MTGT19, MTGT20, MTGT22 and MTGT33, has been considerably induced by treatments of drought, salt and ABA, illustrating their vital roles in response to abiotic constraints. . These conclusions are useful for improving the overall understanding of the TRIHELIX family; In addition, the study provides candidate genes for achieving the genetic improvement of stress resistance in legumes.
Global gene expression profiling reveals that isorhamnetin induces a specific differentiation of hepatic lineage in human amniotic epithelial cells
Human amnion epithelial cells (HAECs), derived from an abandoned term placenta, are anticipated as a new stem cell resource due to their advantages over embryonic stem cells (CES) and induced pluripotent stem cells (IPSCS ), such as the risk of tumorigenicity and minimal ethical problem. It has been reported that HEECs are distinguished in hepatic cells (HLC) with variable functionalities adapted to liver cell disease cell therapy in the end phase, drug screening and drug toxicity testing. On the other hand, a new search stream evolves to use natural compounds such as stimulants in the differentiation of stem cells due to their high availability and minimum side effects.
Isorhamnetin is a natural flavonoid commonly found in fruits and vegetables and has been reported to improve hepatic fibrosis and steatosis. In this current study, we have screed the potential for differentiation of isorhamnetin in the Hats. The cells were grown on a 3D cell culture and were treated with 20 μm of isorhamnetin synthesized for 10 days without adding additional growth factors. The analysis of the global gene gene expression of the DNA has been carried out for genes expressed differentially between the control cells treated with isorhamnetin and untreated, the validation of gene expression was carried out using the help of The RT-QPCR method, and finally, several liver functions have been evaluated.
The analysis of the PCERRAY has shown that isorhamnetin could activate essential biological processes, molecular functions and signaling pathways for liver differentiation. Hepatic offspring markers, EPCAM and DLK1 were regulated in the HECs treated with isorhamnetin. AFP has been regulated, while ALB has been regulated on day 10. In addition, isorhamnetin-treated cells can show an increase in CYP enzyme mRNA levels, absorption and liberation of GCG, a glycogen storage activity and a secretion of urea. In addition, Isorhamnetin’s treated cells showed no trace of transferentiation obvious by significant regulation of several colon and cholangiocyte-specific markers. However, longer treatment with isorhamnetin has not favored hepatic maturation. In total, our results indicate that Isorhamnetin has a promising effect on the direction of specific differentiation of the hepatic line of HECs.
Genome-Wide Identification and Expression Profiling Analysis of the Trihelix Gene Family Under Abiotic Stresses in Medicago truncatula
Histological assessment and gene expression Profile of genes related to autophagy for cartilage of young and sevenciers
Autophagy is a cellular mechanism that protects stress cells by digesting non-functional cellular components. In cartilage, chondrocytes depend on autophagy as the main mechanism for maintaining cell homeostasis. This protective role decreases before the structural damage that occurs normally during aging.
Considering that aging is the main risk factor for osteoarthritis, evaluating the expression of genes associated with autophagy in senescent cartilage could allow the identification of potential therapeutic targets for treatment. Thus, we studied two groups of young and session rats. A histological analysis of cartilage and the quantification of gene expression of autophagy genes have been carried out. In aged cartilage, morphological changes have been observed, such as an increase in cartilage degeneration measured by the modified Mankin score, a decrease in the number of chondrocytes and collagen II (COLL2A1) and an increase in metalloproteinase 13 (MMP13). In addition, 84 genes associated with autophagy were evaluated by a PCR network analysis and 15 of them were significantly considered with aging.
Description: A competitive ELISA for quantitative measurement of Canine Pancreas Specific Transcription Factor 1a in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Dog Pancreas Specific Transcription Factor 1a ELISA kit
Description: A competitive ELISA for quantitative measurement of Canine Pancreas Specific Transcription Factor 1a in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Dog Pancreas Specific Transcription Factor 1a ELISA kit
Description: A competitive ELISA for quantitative measurement of Canine Pancreas Specific Transcription Factor 1a in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: Pancreas tissue array with pancreas cancer tissue, including TNM, clinical stage and pathology grade, 80 cases/80 cores, replaced by PAN801a
Multiple tumor of pancreas and pancreas tissue array
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.
Description: Pancreas tumor tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.
Description: Human pancreas tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human pancreas tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the pancreas tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The pancreas tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human pancreas tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human pancreas tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated pancreas tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated pancreas tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human pancreas tissue cytoplasmic protein lysate was prepared by isolating the cytoplasmic protein from whole tissue homogenates using a proprietary technique. The human pancreas tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The cytoplasmic protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, glycerol, and a cocktail of protease inhibitors. For quality control purposes, the isolated pancreas tissue cytoplasmic protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated pancreas tissue cytoplasmic protein is then Western analyzed by GAPDH antibody, and the expression level is consistent with each lot.
Description: DNase I (EC 3.1.21.1) is an enzyme that degrade DNA, it plays a key role in the cleavage of extracellular DNA is crucial for limiting the inflammatory response and maintaining homeostasis. Exogenous deoxyribonuclease shows beneficial effects in inflammatory diseases and cancer[1].
Description: Ribonuclease A (EC 3.1.27.5) cleaves RNA 3′ to pyrimidines and actively cleaves RNA at every pyrimidine residue. Ribonuclease A catalyzes the hydrolysis of single stranded RNA in the absence of metal ions or cofactors[1][2][3].
Description: A competitive ELISA for quantitative measurement of Canine Pancreastatin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Pancreastatin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Pancreastatin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: Pancreas tumor tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% β-mercaptoethanol.
Description: Pancreas tumor tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% β-mercaptoethanol.
Description: Pancreas tumor tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% β-mercaptoethanol.
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% β-mercaptoethanol.
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 5% β-mercaptoethanol.
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In addition, a silico analysis based on two different bioinformatic software has revealed that several processes, including cell homeostases, the automatic set of autophagosome and several biological lanes such as autophagy, the factor of Insulin-type growth 1 (IGF-1) signaling, PI3K (phosphoinositide 3-kinase) / AKT (Serine / Threonine Kinase) signaling and mammal target of the signaling of rapamycin (MOR) – have been enriched. In conclusion, the analysis identified potential targets for the treatment of osteoarthritis that would develop new therapeutic strategies for this chronic disease.
