ABSTRACT
OBJECTIVE: Long noncoding RNA (lncRNA) was found to play crucial roles in regulating cancer progression. HOXA11 antisense RNA (HOXA11-AS) was reported to serve an oncogenic lncRNA in cancers but its role in prostate cancer (PCa) remains to be explored. MATERIALS AND METHODS: Expression levels of HOXA11-AS in PCa tissues and cells were analyzed with quantitative Real-Time PCR method. MTT assay, colony formation assay, transwell invasion assay, and flow cytometry assay were conducted to explore the biological roles of HOXA11-AS in PCa. Rescue experiments were conducted to investigate mechanisms of HOXA11-AS in regulating PCa progression. RESULTS: We revealed that HOXA11-AS was upregulated in PCa. Silencing of HOXA11-AS significantly inhibited PCa cell proliferation, colony formation, invasion, and promoted apoptosis in vitro. On the contrary, forcing of HOXA11-AS expression caused opposite effects on cancer cell behaviors. Furthermore, we showed that HOXA11-AS1 serves as a competing endogenous RNA (ceRNA) to regulate Jupiter microtubule associated homolog 1 (JPT1) via sponging microRNA-24-3p (miR-24-3p). Functionally, the overexpression of miR-24-3p or knockdown of JPT1 could partially reverse the effects of HOXA11-AS overexpression on PCa cell behaviors. CONCLUSIONS: This newly identified HOXA11-AS/miR-24-3p/JPT1 axis may provide novel angle for the better control of PCa.
Subject(s)
Cell Cycle Proteins/metabolism , MicroRNAs/metabolism , Microtubule-Associated Proteins/metabolism , Prostatic Neoplasms/metabolism , RNA, Long Noncoding/metabolism , Cell Cycle Proteins/genetics , Cell Proliferation , Cells, Cultured , Humans , Male , MicroRNAs/genetics , Microtubule-Associated Proteins/genetics , Prostatic Neoplasms/pathology , RNA, Long Noncoding/geneticsABSTRACT
Crossbreeding is an efficient means to increase production and quality in plants; however, hybridization is seldom reported in bamboo. We crossbred two bamboo species Phyllostachys kwangsiensis (female parent) and Phyllostachys bambusoides (male parent) for the first time, and obtained suspected bamboo hybrids. We identified two bamboo hybrids from the above parents using PCR/ISSR. We concluded that ISSR markers are useful to identify bamboo hybrids, and that breeding between bamboo species is possible and useful.
Subject(s)
Hybridization, Genetic , Inbreeding , Minisatellite Repeats/genetics , Poaceae/genetics , Chromosome Mapping , Genetic Markers , PhylogenyABSTRACT
Electron transfer during the reaction of fully reduced bovine heart cytochrome oxidase with dioxygen has been studied at 24 degrees C in the near-infrared region following photolysis of the fully reduced CO-bound complex. The transient spectral changes and kinetics were followed on microsecond to millisecond time scales at nine different wavelengths between 597 and 935 nm and were analyzed using singular value decomposition and global exponential fitting. Four apparent lifetimes, 14 micros, 40 micros, 86 micros, and 1.1 ms, were resolved. The near-infrared spectra of the intermediates are extracted on the basis of a previously proposed mechanism [Sucheta et al. (1998) Biochemistry 37, 17905-17914] and compared to model spectra of the postulated intermediates. The data provide a comprehensive picture of the spectral contributions of the different redox centers in their respective oxidation or ligation states in the near-infrared region and strongly support that Cu(A) is partially (2/3), but not fully, oxidized in the 3-electron-reduced ferryl intermediate.
Subject(s)
Electron Transport Complex IV/chemistry , Oxygen/chemistry , Animals , Binding Sites , Cattle , Copper/metabolism , Electron Transport Complex IV/metabolism , Heme/analogs & derivatives , Heme/metabolism , Kinetics , Ligands , Models, Chemical , Myocardium/enzymology , Oxidation-Reduction , Oxygen/metabolism , Reproducibility of Results , Spectrophotometry, Infrared/methods , TemperatureABSTRACT
Diazene reacts rapidly with cytochrome c oxidase to reduce cytochrome a and CuA and to form a charge-transfer complex with ferric cytochrome a3; the diazene may serve to bridge the heme iron of this cytochrome and CuB. The complex is characterized by an intense, optically active absorbance located at 847 nm. A similar band had been observed previously upon reduction of cytochrome oxidase with hydrazine [Markossian, K. A., Paitian, N. A., and Nalbandyan, R. M. (1983) FEBS Lett. 156, 235-238], but it appears that this band is actually due to the diazene produced as a result of the oxidation of the hydrazine that occurs in this process. A similar diazene to iron charge-transfer band is found following the reaction of diazene with ferric horseradish peroxidase and with hemin chloride but not with met-myoglobin.
Subject(s)
Electron Transport Complex IV/chemistry , Imides/chemistry , Animals , Cattle , Electron Spin Resonance Spectroscopy , Electron Transport Complex IV/metabolism , Heme/chemistry , Horseradish Peroxidase/chemistry , Hydrazines/chemistry , Imides/metabolism , Ligands , Models, Molecular , Myoglobin/chemistry , Oxidation-Reduction , Oxygen , Potassium Cyanide/chemistry , SpectrophotometryABSTRACT
We have re-investigated the reduced minus oxidized difference spectra of the two heme centers of cytochrome oxidase, cytochromes a and a3. In contrast to data obtained in an earlier study (Vanneste, W.H. (1966) Biochemistry 5, 838-848), we find that the spectrum for cytochrome a3 agrees with that found with a 5-coordinate high-spin heme A model compound. Small but significant additional differences are noted for both heme centers.
