A5009938916- Endoplasmic Reticulum Stress and Disease
- Fungal and yeast genetics research
- RNA regulation and disease
- Toxin Mechanisms and Immunotoxins
- Pancreatic function and diabetes
- Heat shock proteins research
- Transgenic Plants and Applications
- Autophagy in Disease and Therapy
- RNA and protein synthesis mechanisms
- Thin-Film Transistor Technologies
- Silicon Nanostructures and Photoluminescence
- RNA Research and Splicing
- Viral Infectious Diseases and Gene Expression in Insects
- CRISPR and Genetic Engineering
- DNA Repair Mechanisms
- Peripheral Artery Disease Management
- RNA modifications and cancer
- Cellular transport and secretion
- Genomics and Chromatin Dynamics
- Liver physiology and pathology
- Developmental Biology and Gene Regulation
- Neurogenesis and neuroplasticity mechanisms
- Glycosylation and Glycoproteins Research
- Galectins and Cancer Biology
- Microbial Inactivation Methods
Nara Institute of Science and Technology
2014-2024
University of Hyogo
2021-2024
Initiatives (Denmark)
2019
RELX Group (United States)
2019
Odawara Municipal Hospital
2012-2016
Northwest African American Museum
2016
Bio-Medical Science (South Korea)
2015
Cell Medica (Switzerland)
2015
Tokyo Medical and Dental University
2014
Keio University
2013
Glomerular injury and proteinuria in diabetes (types 1 2) IgA nephropathy is related to the degree of podocyte depletion humans. For determining causal relationship between glomerulosclerosis, a transgenic rat strain which human diphtheria toxin receptor specifically expressed podocytes was developed. The rodent homologue does not act as (DT) receptor, thereby making rodents resistant DT. Injection DT into rats but wild-type resulted dose-dependent from glomeruli. Three stages glomerular...
Inositol requiring enzyme-1 (IRE1), a protein located on the endoplasmic reticulum (ER) membrane, is highly conserved from yeast to humans. This activated during ER stress and induces cellular adaptive responses stress. In mice, IRE1alpha inactivation results in widespread developmental defects, leading embryonic death after 12.5 days of gestation. However, cause this lethality not fully understood. Here, by using vivo imaging analysis conventional knockout respectively, we showed that was...
Upon endoplasmic reticulum (ER) stress, an endoribonuclease, inositol-requiring enzyme-1α, splices the precursor unspliced form of X-box-binding protein 1 messenger RNA (XBP1u mRNA) on ER membrane to yield active transcription factor (XBP1s), leading alleviation stress. The nascent peptide encoded by XBP1u mRNA drags mRNA-ribosome-nascent chain (R-RNC) complex for efficient cytoplasmic splicing. We found that translation was briefly paused stabilize R-RNC complex. Mutational analysis...
Chaperone protein BiP binds to Ire1 and dissociates in response endoplasmic reticulum (ER) stress. However, it remains unclear how the signal transducer senses ER stress is subsequently activated. The crystal structure of core stress-sensing region (CSSR) yeast luminal domain led controversial suggestion that molecule can bind unfolded proteins. We demonstrate that, upon stress, clusters actually interacts with mutations affect these phenomena reveal activated via two steps, both which are...
The body's capacity to restore damaged neural networks in the injured CNS is severely limited. Although various treatment regimens can partially alleviate spinal cord injury (SCI), mechanisms responsible for symptomatic improvement remain elusive. Here, using a mouse model of SCI, we have shown that transplantation stem cells (NSCs) together with administration valproic acid (VPA), known antiepileptic and histone deacetylase inhibitor, dramatically enhanced restoration hind limb function....
Eukaryotic cells activate the unfolded-protein response (UPR) upon endoplasmic reticulum (ER) stress, where stress is assumed to be accumulation of unfolded proteins in ER. Consistent with previous vitro studies ER-luminal domain mutant UPR initiator Ire1, our study show its association a model protein yeast cells. An Ire1 luminal mutation that compromises Ire1's unfolded-protein-associating ability weakens respond stimuli, likely resulting In contrast, this was activated like wild-type by...
AKI increases the risk of developing CKD, but mechanisms linking to CKD remain unclear. Because proximal tubule injury is mainstay AKI, we postulated that triggers features CKD. We generated a novel mouse model induce tubule–specific adjustable by inducing expression diphtheria toxin (DT) receptor with variable prevalence in tubules. Administration high-dose DT mice expressing consistently caused severe associated interstitial fibrosis and reduction erythropoietin production. Mild from...
Ribosome movement is not always smooth and rather often impeded. For ribosome pauses, fundamental issues remain to be addressed, including where ribosomes pause on mRNAs, what kind of RNA/amino acid sequence causes this pause, the physiological significance attenuation protein synthesis. Here, we survey positions collisions caused by pauses in humans zebrafish using modified profiling. Collided ribosomes, i.e., disomes, emerge at various sites: Pro-Pro/Gly/Asp motifs; Arg-X-Lys stop codons;...
The immunosuppressant rapamycin (RAP) has been demonstrated to specifically inhibit the activity of p70 S6 kinase (p70s6k) and subsequent phosphorylation ribosomal protein in mammalian cells. Addition RAP proliferating lymphoid cells resulted inhibition synthesis before any changes rate cell proliferation. When cellular composition proteins was examined by gel electrophoresis, dramatically inhibited selective proteins, particularly elongation factor 2 (eEF-2). eEF-2 at translational level....
The endoplasmic reticulum (ER) of eukaryotic cells contains an abundant 78,000-Da protein (BiP) that is involved in the translocation, folding, and assembly secretory transmembrane proteins. In yeast Saccharomyces cerevisiae, as mammalian cells, BiP mRNA synthesized at a high basal rate further induced by presence increased amounts unfolded proteins ER. However, unlike BiP, also severalfold heat shock, albeit transient fashion. To identify regulatory sequences respond to these stimuli KAR2...
In the unfolded protein response, type I transmembrane Ire1 transmits an endoplasmic reticulum (ER) stress signal to cytoplasm. We previously reported that under nonstressed conditions, ER chaperone BiP binds and represses Ire1. It is still unclear how this event contributes overall regulation of The present mutation study shows luminal domain possesses two subregions seem indispensable for activity. BiP-binding site was assigned not these subregions, but a region neighboring domain....
The endoplasmic reticulum (ER) of eukaryotic cells contains an abundant 78,000-Da protein (BiP) that is involved in the translocation, folding, and assembly secretory transmembrane proteins. In yeast Saccharomyces cerevisiae, as mammalian cells, BiP mRNA synthesized at a high basal rate further induced by presence increased amounts unfolded proteins ER. However, unlike BiP, also severalfold heat shock, albeit transient fashion. To identify regulatory sequences respond to these stimuli KAR2...
Abstract A major response of eukaryotic cells to the presence unfolded proteins in lumen endoplasmic reticulum (ER) is activate genes that encode ER-located molecular chaperones, such as binding protein. This response, called protein requires transduction a signal from ER nucleus. In yeast (Saccharomyces cerevisiae) and mammalian cells, an transmembrane receptor kinase/ribonuclease Ire1, with sensor domain ER, first component this pathway. Here, we report cloning derived amino acid sequences...
Journal Article Inhibition of Biosynthesis Polyisoprenol Sugars in Chick Embryo Microsomes by Tunicamycin Get access Akira Takatsuki, Takatsuki Laboratory Microbiology, Department Agricultural Chemistry, The University Tokyo, Bunkyo-ku, Tokyo 113, Japan Search for other works this author on: Oxford Academic Google Scholar Kenji Kohno, Kohno Gakuzo Tamura and Biological Volume 39, Issue 10, 1 October 1975, Pages 2089–2091, https://doi.org/10.1080/00021369.1975.10861914 Published: 01 1975...