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Your search keyword '"Iwamura, H."' showing total 49 results
Start Over Author "Iwamura, H." Publisher wiley-blackwell
49 results on '"Iwamura, H."'

1. Endogenous protein and enzyme fragments induce immunoglobulin E‐independent activation of mast cells via a G protein‐coupled receptor, MRGPRX2.

Author

Tatemoto, K., Nozaki, Y., Tsuda, R., Kaneko, S., Tomura, K., Furuno, M., Ogasawara, H., Edamura, K., Takagi, H., Iwamura, H., Noguchi, M., and Naito, T.

Subjects
MAST cell immunology, G protein coupled receptors, GHRELIN receptors, IMMUNOGLOBULINS, IMMUNOLOGY of inflammation
Abstract

Abstract: Mast cells play a central role in inflammatory and allergic reactions by releasing inflammatory mediators through 2 main pathways, immunoglobulin E‐dependent and E‐independent activation. In the latter pathway, mast cells are activated by a diverse range of basic molecules (collectively known as basic secretagogues) through Mas‐related G protein‐coupled receptors (MRGPRs). In addition to the known basic secretagogues, here, we discovered several endogenous protein and enzyme fragments (such as chaperonin‐10 fragment) that act as bioactive peptides and induce immunoglobulin E‐independent mast cell activation via MRGPRX2 (previously known as MrgX2), leading to the degranulation of mast cells. We discuss the possibility that MRGPRX2 responds various as‐yet‐unidentified endogenous ligands that have specific characteristics, and propose that MRGPRX2 plays an important role in regulating inflammatory responses to endogenous harmful stimuli, such as protein breakdown products released from damaged or dying cells. [ABSTRACT FROM AUTHOR]

Published
2018
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48. IMPDH inhibition activates TLR-VCAM1 pathway and suppresses the development of MLL-fusion leukemia.

Author

Liu X, Sato N, Yabushita T, Li J, Jia Y, Tamura M, Asada S, Fujino T, Fukushima T, Yonezawa T, Tanaka Y, Fukuyama T, Tsuchiya A, Shikata S, Iwamura H, Kinouchi C, Komatsu K, Yamasaki S, Shibata T, Sasaki AT, Schibler J, Wunderlich M, O'Brien E, Mizukawa B, Mulloy JC, Sugiura Y, Takizawa H, Shibata T, Miyake K, Kitamura T, and Goyama S

Subjects
Humans, Enzyme Inhibitors pharmacology, NF-kappa B, Immunosuppressive Agents therapeutic use, Myeloid-Lymphoid Leukemia Protein metabolism, Leukemia, Myeloid, Acute drug therapy, Leukemia, Myeloid, Acute pathology
Abstract

Inosine monophosphate dehydrogenase (IMPDH) is a rate-limiting enzyme in de novo guanine nucleotide synthesis pathway. Although IMPDH inhibitors are widely used as effective immunosuppressants, their antitumor effects have not been proven in the clinical setting. Here, we found that acute myeloid leukemias (AMLs) with MLL-fusions are susceptible to IMPDH inhibitors in vitro. We also showed that alternate-day administration of IMPDH inhibitors suppressed the development of MLL-AF9-driven AML in vivo without having a devastating effect on immune function. Mechanistically, IMPDH inhibition induced overactivation of Toll-like receptor (TLR)-TRAF6-NF-κB signaling and upregulation of an adhesion molecule VCAM1, which contribute to the antileukemia effect of IMPDH inhibitors. Consequently, combined treatment with IMPDH inhibitors and the TLR1/2 agonist effectively inhibited the development of MLL-fusion AML. These findings provide a rational basis for clinical testing of IMPDH inhibitors against MLL-fusion AMLs and potentially other aggressive tumors with active TLR signaling., (© 2022 The Authors. Published under the terms of the CC BY 4.0 license.)

Published
2023
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49. Purification, crystallization and preliminary X-ray analysis of a hexameric beta-glucosidase from wheat.

Author

Sue M, Yamazaki K, Kouyama J, Sasaki Y, Ohsawa K, Miyamoto T, Iwamura H, and Yajima S

Subjects
Crystallization, Crystallography, X-Ray, Protein Structure, Quaternary, Triticum chemistry, beta-Glucosidase chemistry
Abstract

The wheat beta-glucosidase TaGlu1b, which is only active in a hexameric form, was tagged with 6xHis at the N-terminus, overexpressed in Escherichia coli and purified in two steps. The protein complexed with a substrate aglycone was crystallized at 293 K from a solution containing 10 mM HEPES pH 7.2, 1 M LiSO4 and 150 mM NaCl using the hanging-drop vapour-diffusion method. Diffraction data were collected to 1.7 A at the Photon Factory. The crystal belongs to space group P4(1)32, with unit-cell parameters a = b = c = 194.65 A, alpha = beta = gamma = 90 degrees. The asymmetric unit was confirmed by molecular-replacement solution to contain one monomer, giving a solvent content of 72.1%.

Published
2005
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