Wheat (T. aestivum L.) is the second most important staple food crop consumed in the form of various end-use products across the world. However, it contains lower concentrations of Fe and Zn leading to micronutrient deficiency in human beings where wheat is the sole diet. Therefore, increasing grain Fe/Zn content in wheat has become priority in wheat breeding programmes across the world. Understanding the molecular mechanism of Fe/Zn transport and accumulation in grains is required to expedite the breeding process. For this purpose, whole seedling transcriptome analysis was conducted in four wheat genotypes (CRP 1660, Sonora 64, Vinata, : high, and DBW17: low) differing in grain Fe/Zn content under controlled and Fe/Zn deficient conditions. Twenty eight key transcripts involved in phytosiderophore biosynthesis, Fe/Zn uptake and transport were identified. Expression analysis of 12 of the transcripts using qPCR was conducted in seedling stage and flag leaf which exhibited greater differential accumulation in CRP 1660 followed by Vinata, Sonora 64 and DBW 17 in both flag leaf and seedling. However, there was significantly higher differential accumulation of the transcripts in flag leaf as compared to seedling. In CRP 1660, transcripts pertaining to phytosiderophore biosynthesis like DMAS1-B, NRAMP2 and NAAT2-D showed greater accumulation. Additionally, corresponding miRNAs were also identified for these 28 transcripts. The findings will help in better understanding of molecular basis of Fe/Zn transport and accumulation in grain and subsequent utilization in breeding to improve Fe/Zn content in wheat grain.
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http://dx.doi.org/10.1016/j.jbiotec.2020.03.015 | DOI Listing |
NPJ Sci Food
December 2024
Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School of Kyushu University, Fukuoka, Japan.
In a series of studies on blood-brain barrier transportable peptides, a soybean dipeptide, Tyr-Pro, penetrated the mouse brain parenchyma after oral intake and improved short and long memory impairment in acute Alzheimer's model mice. Here, we aimed to clarify the anti-dementia effects of this peptide administered to SAMP8 mice prior to dementia onset. At the end of the 25-week protocol in 16-week-old SAMP8 mice, Tyr-Pro (10 mg/kg/day) significantly improved the reduced spatial learning ability compared with that in the control and amino acid (Tyr + Pro) groups as indicated by the results of Morris water maze tests conducted for five consecutive days.
View Article and Find Full Text PDFGenetics
December 2024
Department of Genetics and Biochemistry and Center for Human Genetics, Clemson University, 114 Gregor Mendel Circle, Greenwood, SC 29646, USA.
Mucopolysaccharidosis type IIIB (MPS IIIB) is a rare lysosomal storage disorder caused by defects in alpha-N-acetylglucosaminidase (NAGLU) and characterized by severe effects in the central nervous system. Mutations in NAGLU cause accumulation of partially degraded heparan sulfate in lysosomes. The consequences of these mutations on whole genome gene expression and their causal relationships to neural degeneration remain unknown.
View Article and Find Full Text PDFBioessays
December 2024
Department of Biochemistry and Molecular Biology, Louisiana Cancer Research Center, Tulane University School of Medicine, New Orleans, Louisiana, USA.
Epithelial tissues serve as critical barriers in metazoan organisms, maintaining structural integrity and facilitating essential physiological functions. Epithelial cell polarity regulates mechanical properties, signaling, and transport, ensuring tissue organization and homeostasis. However, the barrier function is challenged by cell turnover during development and maintenance.
View Article and Find Full Text PDFFront Pharmacol
December 2024
Department of Biochemistry, Quaid-i-Azam University, Islamabad, Pakistan.
Background: The global prevalence of diabetes among adults over 18 years of age is expected to increase from 10.5% to 12.2% (between 2021 and 2045).
View Article and Find Full Text PDFMol Neurodegener
December 2024
German Center for Neurodegenerative Diseases (LMU), Klinikum, Germany.
Background: The prion-like spreading of Tau pathology is the leading cause of disease progression in various tauopathies. A critical step in propagating pathologic Tau in the brain is the transport from the extracellular environment and accumulation inside naïve neurons. Current research indicates that human neurons internalize both the physiological extracellular Tau (eTau) monomers and the pathological eTau aggregates.
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