To observe the distribution of Schistosoma mansoni glucose transport proteins, SGTP1 and SGTP4, in the tegument of Schistosoma japonicum.The rapidly frozen fixation technique and ultracryomicrotomy were adopted for preparing ultrathin cryosections of S. japonicum. Anti-SGTP1 and anti-SGTP4 antibodies were used to localize the corresponding antigens in the tegument of adult S. japonicum by immunocytochemical technique.SGTP1 was localized on the basal membrane of the tegument and its infoldings, SGTP4 was localized on the apical membrane of the tegument and its invaginations of S. japonicum.The same localization for SGTP 1 and SGTP4 in the tegument of S. japonicum and S. mansoni exhibited apparent homology between SGTPs of the two schistosomes.
Objective The purpose of this paper was to investigate the aberration of the E cadherin in human hepatocellular carcinomas, and to provide evidence for a better understanding of the development of human hepatocellular carcinoma(HCC).Methods Using the single strand conformation polymorphism analysis with polymerase chain reaction,aberration of the E cadherin exon 6,9 and 10 were examined in 22 HCC (including 4 well differentiated and 18 poorly differentiated HCCs),12 adjacent tissues of HCC and 5 HCC emboli.Results Structural abnormalities of E cadherin gene were observed in 4 of 18 poorly differentiated HCCs,(2 with an abnormal exon 9,2 with an aberrant exon 6).Two of 5 HCC emboli carried the mutation,(one with an abnormal exon 9 and the other with a mutation of exon 10).However,in 12 adjacent tissues of HCCs and 4 well differentiated HCCs,structural abnormalities of E cadherin exon 6,9 and 10 were not found.Conclusions The results suggest the involvement of E cadherin gene in development and metastasis of HCC.$$$$
Aluminum-doped zinc oxide (AZO) is considered as a promising candidate as transparent conductive oxide (TCO) for silicon heterojunction solar cells due to its high carrier density, nontoxic nature, and low cost. Herein, it is presented that the transparency of the AZO film can be optimized through co-sputtering of AZO and molybdenum oxide (MoOx). Furthermore, aluminum and molybdenum co-doped zinc oxide (MAZO) can be used as both the TCO layer and electron-selective contact (ESC) for silicon heterojunction solar cells. The surface morphology, cation oxidation state, and optical and electrical properties of all MAZO films are characterized. It is found that the transmittance of all MAZO films is significantly increased at a wavelength of 450-800 nm due to MAZO with a stronger Zn-O bond and a wider band gap. The conductivity of MAZO films is approximate to AZO films at a low MoOx target deposit power (50 W), and the sheet resistance of MAZO films increases significantly by increasing the deposition power up to 100 W. Finally, the optimized MAZO films are used as TCO and ESC for silicon heterojunction solar cells, showing a power conversion efficiency of 19.58%. The results show an effective stage to improve the optical properties of AZO through co-doping and the possibility of applying MAZO as a dual-functional layer for silicon solar cells.
ABSTRACT Age‐related cataracts (ARCs) are associated with increased oxidative stress and cellular senescence. Our objective is to investigate the function of Sirtuin 1 (SIRT1) within ARCs. In ARCs tissues and H 2 O 2 ‐treated lens epithelial cells (LECs), the expression levels of SIRT1 were examined. Senescence‐associated β‐galactosidase (SA‐β‐gal) staining was employed to evaluate cellular senescence. The Cell Counting Kit‐8 assay was employed to measure viability. A wound healing assay was performed to assess migratory capacity in LECs. Oxidative stress‐related indicators were determined by enzyme‐linked immunosorbent assay kits. Additionally, the Coxpresdb and GeneCards databases were utilized to identify downstream pathways of SIRT1 in ARCs. The expression levels of protein and mRNA were detected using western blot and real‐time quantitative polymerase chain reaction, respectively. The expression of SIRT1 was downregulated in ARCs tissues with an increase in reactive oxygen species. In H 2 O 2 ‐induced LECs, SIRT1 was downregulated and its overexpression inhibited oxidative stress and cellular senescence while promoting viability and migration. Furthermore, FoxO1/TLR4 pathway was screened out as the key pathway of SIRT1, which was activated in H 2 O 2 ‐induced LECs senescence. Overexpression of SIRT1 suppressed FoxO1/TLR4 pathway. Further research demonstrated that the activation of FoxO1/TLR4 pathway reversed the inhibitory role of SIRT1 in oxidative stress‐induced cellular senescence and the promotion effect of SIRT1 on viability and migration in H 2 O 2 ‐induced LECs. SIRT1 inhibits oxidative stress‐induced cellular senescence and promotes the viability and migration in H 2 O 2 ‐induced LECs via suppressing FoxO1/TLR4 pathway.
The nucleotide sequence of the plastid-encoded operon containing genes for the alpha (cpcA) and beta (cpcB) subunits of phycocyanin in the unicellular red alga Cyanidium caldarium is described. cpcB is located 5' to cpcA and the two genes are separated by a 102-bp spacer region. The transcription start site of cpcBA was mapped to 80 bp upstream of the ATG initiation codon of cpcB. Promoter-like elements similar to the -10 (TATAAT) and -35 (TTGACA) consensus promoters in bacteria were found 6 and 31 bp upstream of the transcription initiation site. Northern blotting revealed an abundant 1.3-kb cpcBA transcript in illuminated cells, but this transcript was undetectable in dark-grown cells. Expression levels of cpcBA in cells incubated with 10(-6) M heme in the dark were similar to those in cells illuminated for 24 h. Cells illuminated with 150 microM gabaculine (an inhibitor of delta-aminolevulinate synthesis) or 10 mM levulinic acid (an inhibitor of delta-aminolevulinate dehydrase) lacked detectable cpcBA transcripts. In cells illuminated with 200 microM N-methyl-mesoporphyrin IX (an inhibitor of ferrocheletase), inhibition of cpcBA expression and phycocyanin synthesis was similar. These results provide strong evidence that light induction of the cpcBA operon is dependent on synthesis of heme.
Cataract, a painless and progressive disorder is manifested as the opacification of the lens that represents the most significant cause of blindness worldwide. The objective of this study is to unveil the function of Kirsten rat sarcoma (KRAS) and potential action mechanisms against cataract. The ferroptosis-associated differentially expressed genes (DEGs) and pivot genes were extracted through the comprehensive bioinformatics methods. Erastin was applied for inducing ferroptosis in hydrogen peroxide (H2O2)-treated SRA01/04 cells, and validated by detecting content of intracellular iron, glutathione (GSH), malondialdehyde (MDA). Additionally, the effects of KRAS deficiency on ferroptosis were determined by functional assays. The proteins expression related to ferroptosis and Hippo pathway were determined by Western blotting. A total of 73 ferroptosis-related DEGs were discovered, and 6 critical core genes were confirmed upregulation in cataract cell model. The H2O2-treated SRA01/04 cells exhibited decrease of cell viability and proliferation, iron accumulation, MDA increase, GSH consumption, rise of COX2 and decline of GPX4, with further aggravated under erastin treatment, while the phenomena were improved by KRAS knockdown. Additionally, KRAS deficiency was involved in the Hippo signalling pathway activation. Downregulation of KRAS might restrain ferroptosis and affect Hippo pathway in cataract.
RAS is a well-known oncogene contributing to significant proportion of cancer incidences, yet it remains as an undruggable target to majority of therapeutic modalities. Here, we explored the potential of extracellular vesicles (EVs) for therapeutic targeting of KRAS mutation-driven tumorigenesis. EVs loaded with small interfering RNA (siRNA) against KRAS successfully inhibited tumor xenograft growth when injected intratumorally in mice models. Intriguingly, when injected intravenously, EVs were still able to accumulate in tumors and deliver KRAS targeting siRNA payload in sufficient amount to show tumor growth inhibition. Therefore, EV-siRNA platform show great promises for therapeutic targeting of KRAS mutations and other undruggable targets.
The rapid overall characterization of quality changes in complex food systems is considered extremely challenging. Herein, a multi-molecular infrared spectroscopy (MM-IR) methodology in combination with low-field nuclear magnetic resonance and chemometrics, to in-situ reveal the quality changes of surimi (protein) products as a whole was developed. Surimi with cryoprotectant (SWC) and without cryoprotectant (SWO) were used as a typical demonstration. Specifically, secondary structures in proteins could transform into each other and the structural variation of SWC was smaller than that of SWO. Cryoprotectant could slow down the water conversion from non-moveable to free, thereby slow down the rate of protein degradation. principal component analysis results of massive samples verified the differences in quality between SWC and SWO at different storage stages. Therefore, the addition of cryoprotectant led to the frozen surimi having less protein secondary structure conversion and water migration. In sum, the developed MM-IR could be applicable for the quality tracking of frozen surimi. Practical applications Low-temperature storage is currently the most mainstream storage method for surimi, and the preservation time of surimi can be extended by adding cryoprotectants. In this study, the overall quality of frozen surimi could be characterized in situ and simultaneous multi-component analysis could be realized, and the changes in the secondary structure of surimi protein and the migration of water could be tracked in situ. The results of this work had the potential to track the quality changes of complex frozen aquatic products as a whole and predicted the frozen storage time.
'/%3e%3cuse xlink:href='%23a' transform='rotate(23.036 .093 25.536)'/%3e%3cuse xlink:href='%23a' transform='rotate(45.87 1.273 16.18)'/%3e%3cuse xlink:href='%23a' transform='rotate(69.945 .996 12.078)'/%3e%3cuse xlink:href='%23a' transform='rotate(20.66 -19.689 31.932)'/%3e%3c/svg%3e)
