ABSTRACT
The bioactive compounds and antioxidant activities of propolis extracts were investigated using subcritical water extraction (SWE). SWE was performed by varying temperature (110-200 °C) and time (10-30 min). SWE using only water as solvent successfully to extracted bioactive compounds from propolis using high-purity glass thimbles. The concentrations of galangin (16.37 ± 0.61 mg/g), and chrysin (7.66 ± 0.64 mg/g) were maximal at 200 °C for 20 min, and 170 °C for 20 min, respectively. The antioxidative properties from propolis increased with the increasing extraction temperature and extraction time on SWE. The maximum yields of the total phenolics (226.37 ± 4.37 mg/g), flavonoids (70.28 ± 1.33 mg/g), and antioxidant activities (88.73 ± 0.58%, 98.86 ± 0.69%, and 858.89 ± 11.48 mg/g) were obtained at 200 °C for 20 min. Compared with using ethanol extraction (at 25 °C for 24 h, total phenolics = 176.28 ± 0.35, flavonoids = 56.41 ± 0.65, antioxidant activities = 72.74 ± 0.41%, 95.18 ± 0.11%, 619.51 ± 8.17 mg/g), all yields of SWE extracts obtained at 200 °C for 20 min were higher. SWE is suitable for a much faster and more efficient method extracting bioactive compounds from propolis compared to traditional extraction method.
Subject(s)
Ascomycota , Propolis , Bees , Animals , Water , Antioxidants , Flavonoids , Phenols , Plant ExtractsABSTRACT
The tripartite motif containing (TRIM) proteins are a large family of proteins that have been implicated in many biological processes including cell differentiation, apoptosis, transcriptional regulation, and signaling pathways. Here, we show that TRIM15 co-localized to focal adhesions through homo-dimerization and significantly suppressed cell migration. Domain mapping analysis indicated that B-box2 and PRY domains were essential for TRIM15 localization to focal adhesions and inhibition of cell migration. Our protein-protein interaction screen of TRIM15 with the integrin adhesome identified several TRIM15 interacting proteins including coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. TRIM15 expression was tissue-restricted and downregulated in colon cancer. Level of TRIM15 expression was associated with colon cancer cell migration, as well as both in vitro and in vivo tumor growth. These data provide novel insights into the role of TRIM15 as an additional component of the integrin adhesome, regulating cell migration, and suggest that TRIM15 may function as a tumor suppressor of colon cancer.
Subject(s)
Carcinogenesis/genetics , Carcinogenesis/pathology , Colonic Neoplasms/genetics , Colonic Neoplasms/pathology , DNA-Binding Proteins/metabolism , Focal Adhesions/metabolism , Actins/metabolism , Adenocarcinoma/genetics , Adenocarcinoma/pathology , Animals , Cell Adhesion , Cell Line, Tumor , Cell Movement , Cell Proliferation , Cortactin/metabolism , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/genetics , Down-Regulation , Epithelial Cells/metabolism , Extracellular Matrix/metabolism , Female , Gene Expression Profiling , Gene Expression Regulation, Neoplastic , Humans , Mice, Nude , Phosphorylation , Protein Binding , Protein Multimerization , Protein Structure, Tertiary , Protein Transport , Structure-Activity RelationshipABSTRACT
We report the successful application of interphase fluorescent in situ hybridization (FISH) using extracted nuclei from snap frozen buffy coat stored for the purpose of molecular analysis. Included in this study were 30 frozen buffy coat specimens, ranging from <1 day to 3 yr old. Thawing of the buffy coat at 37 degrees C was followed by lysing erythrocytes with lysing solution (LYSE S III DIFF, Coulter Corp.). Cells were fixed and slides were prepared according to manufacturer's FISH protocol. All specimens from the 30 frozen-thawed buffy coats were suitable for FISH evaluation, and signal intensities were not significantly related to the age of specimens. In conclusion, interphase FISH is feasible using frozen-thawed buffy coat; the technique will be useful for retrospective molecular cytogenetic analysis of hematologic malignancies.
Subject(s)
Blood Cells/cytology , Blood Preservation/methods , Cell Nucleus/genetics , In Situ Hybridization, Fluorescence/methods , Cryopreservation/methods , Evaluation Studies as Topic , Humans , Interphase/geneticsABSTRACT
OBJECTIVE: To investigate the relationships among longitudinal weight status, body dissatisfaction, and attitude to weight loss among Korean children from the age of 7-8 to 13-14 years old. RESEARCH METHODS AND PROCEDURES: 351 Korean school children's heights and weights were measured at the ages of 7-8 and 13-14 years old; at the age of 13-14, they completed a questionnaire about body dissatisfaction and weight loss efforts. RESULTS: At the age of 7-8, 15.7% of children were overweight by International Obesity Task Force standards, as compared with 26.2% at the age of 13-14. Of the 55 7- to 8-year-old overweight children, 85.5% were still overweight at the age of 13-14 years old. Greater concerns about body image and stronger desires to be thinner were observed among stable overweight children and among those in whom there had been a rapid increase in BMI over the 6-year study period. Girls favored thinner shapes than did boys, regardless of their weight status or BMI changes. In girls, the level of body dissatisfaction was related only to weight loss desire, regardless of weight status or changes in BMI. In boys, however, weight loss desire was related only to weight loss attempts and was independent of weight status, BMI changes, and level of body dissatisfaction. DISCUSSION: Regardless of weight status, changes in BMI should be considered when dealing with body dissatisfaction and attitudes to weight loss in children.
