Brassica napus is an important oilseed crop worldwide. Although seed weight is the main determinant of seed yield, few studies have focused on the molecular mechanisms that regulate seed weight in B . napus . In this study, the immature seeds of G-42 and 7–9, two B . napus doubled haploid (DH) lines with extremely different thousand-seed weight (TSW), were selected for a transcriptome analysis to determine the regulatory mechanisms underlying seed weight at the whole gene expression level and to identify candidate genes related to seed weight. A total of 2,251 new genes and 2,205 differentially expressed genes (DEGs) were obtained via RNA-seq (RNA sequencing). Among these genes, 1,747 (77.61%) new genes and 2020 (91.61%) DEGs were successfully annotated. Of these DEGs, 1,118 were up-regulated and 1,087 were down-regulated in the large-seed line. The Kyoto Encyclopedia of Genes and Genomes (KEGG) database analysis indicated that 15 DEGs were involved in ubiquitin-mediated proteolysis and proteasome pathways, which might participate in regulating seed weight. The Gene Ontology (GO) database indicated that 222 DEGs were associated with the biological process or molecular function categories related to seed weight, such as cell division, cell size and cell cycle regulation, seed development, nutrient reservoir activity, and proteasome-mediated ubiquitin-dependent protein catabolic processes. Moreover, 50 DEGs encoding key enzymes or proteins were identified that likely participate in regulating seed weight. A DEG ( GSBRNA2T00037121001 ) identified by the transcriptome analysis was also previously identified in a quantitative trait locus (QTL) region for seed weight via SLAF-seq (Specific Locus Amplified Fragment sequencing). Finally, the expression of 10 DEGs with putative roles in seed weight and the expression of the DEG GSBRNA2T00037121001 were confirmed by a quantitative real-time reverse transcription PCR (qRT-PCR) analysis, and the results were consistent with the RNA sequencing data. This work has provided new insights on the molecular mechanisms underlying seed weight-related biosynthesis and has laid a solid foundation for further improvements to the seed yield of oil crops.
No abstract
Although the exact pathogenesis of Alzheimer's disease (AD) remains to be fully defined, several pharmacological strategies for preventing and treating AD are under active investigation. More recently, drug design has targeted molecular events involved in the pathogenesis of AD including b-amyloid (Ab) and neurofibrillary tangle formation. [1][2][3] In in vitro studies, Leveugle 1,4) has shown that heparin oligosaccharides (known as a type of glycosaminoglycans (GAGs)) pass through a blood-brain barrier (BBB) model in a molecular weight-dependent manner and inhibit amyloid b precursor protein processing, suggesting their potential effects against AD.As an analogue of low molecular weight GAGs, acidic oligosaccharide sugar chain (AOSC), an anti-Alzheimer's disease drug candidate, is currently undergoing preclinical evaluation. AOSC bearing rich mannuronate blocks is an acidic marine-derived oligosaccharide extracted from the brown algae Echlonia Kurome Okam by enzymatic depolymerization and has an average molecular weight of about 1300 Da. We have demonstrated that AOSC can alleviate Alzheimer-type behavioral symptoms induced by scopolamine and Ab1-40 in rodent models. The mechanisms of action underlying the cognition-improving activities of AOSC have been illustrated to be attributed to the inhibition of apoptosis, and thus, neurotoxicity via binding to Ab peptide. 5,6) Given that AOSC has a promising therapeutic value for AD, the ability of AOSC to pass through the BBB becomes crucial for understanding its direct central nerve system (CNS) effects.The detection of oligosaccharides has traditionally been performed on TLC, GC, HPLC, and capillary electrophoresis. However, there exist limitations due to the polydisperse and diversiform nature of oligosaccharides, and particularly the interference of endogenous GAGs. Moreover, these analytical methods require many clean up steps and are often time-consuming. Antibody-based methods have been developed as a favorable alternative for either the identification or quantification of oligosaccharides.7) Antibodies are often used in the detection of oligosaccharides in immunoassays for these compounds, 8,9) and enzyme-linked immunosorbent assay (ELISA) is the most commonly used.Recently, the surface plasmon resonance (SPR) biosensor assay has become increasingly recognized to be an accurate method for identifying the interaction between antibody and antigen.10,11) Compared with conventional methods such as ELISA and fluorescence enzyme immunoassay, 12,13) it possesses several inherent advantages. A particular advantage of SPR assay is there is no need to label reactants, allowing 'real-time' detection of biomolecular interactions, which has attracted considerable attention due to its easy and specific recognition of antigen-antibody (antigen-antibody interaction). Other advantages are easy sample preparation, fully automated operation, short-time analysis, and small amount of sample consumption, which are of particular relevance when the interested components are difficult...
Two conjugates of marine polysaccharide (MPS) and bovine serum albumin (BSA) were prepared using two methods, periodate oxidation and reductive amination, with the intent of enhancing its immunogenicity. Sera samples from Balb/c mice immunized with the products named MPS-BSAp and MPS-BSAr respectively were evaluated by enzyme-linked-immunosorbent assay (ELISA). The results showed that mice immunized with MPS-BSAp produced antibodies not against MPS but rather against MPS-BSAp, while the mice immunized with MPS-BSAr produced high titer antibodies only specific for MPS. The difference was attributed to the fact that the epitopes of MPS had been changed in the coupling process by periodate oxidation. A mouse immunized with MPS-BSAr was chosen to prepare monoclonal antibodies (mAbs) specific for polysaccharide MPS. A hybridoma cell line that secreted monoclonal antibody recognizing specifically polysaccharide MPS was established.
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