Publications by authors named "Mitsuzawa H"

Plant tendrils are specialized organs that can twine around other structures to facilitate climbing. They occur in a variety of plant families and have diverse ontogenic origins. In cucurbits, tendrils originate from lateral shoots.

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The fission yeast Schizosaccharomyces pombe undergoes a switch from yeast to filamentous invasive growth in response to certain environmental stimuli. Among them is ammonium limitation. Amt1, one of the three ammonium transporters in this yeast, is required for the ammonium limitation-induced morphological transition; however, the underlying molecular mechanism remains to be understood.

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Objectives: To investigate the outcome of pediatric tracheostomy and identify predictive factors for successful decannulation.

Methods: We performed a retrospective chart review of a series of 42 consecutive patients of less than 24 months of age who underwent a tracheostomy between 2012 and 2015.

Results: Successful decannulation was achieved in 11 patients (26%).

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Conclusions: Tracheoesophageal diversion (TED) and laryngotracheal separation (LTS) can prevent aspiration pneumonia and improve the morbidity of patients with severe motor and intellectual disability (SMID). By improving hospitalization rates and care needs, the quality-of-life can be improved for the patients and their parents.

Objectives: This study evaluated the clinical outcomes of TED and LTS in patients with intractable aspiration and SMID.

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Objective: Tracheo-innominate artery fistula (TIF) is a rare but life-threatening complication following tracheostomy or tracheoesophageal diversion (TED). Although successful surgical intervention for TIF has been reported, few studies have been performed in patients with severe motor and intellectual disability (SMID). Therefore, we aimed to analyze TIF in patients with SMID to clarify the clinical variables predicting the occurrence and adequate management for lifesaving of TIF.

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Pulmonary collectins, surfactant proteins A (SP-A) and D (SP-D), play important roles in innate immunity of the lung. Legionella pneumophila is a bacterial respiratory pathogen that can replicate within macrophages and causes opportunistic infections. L.

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Background: We have previously shown that lung collectins, surfactant protein A (SP-A) and surfactant protein D, interact with Toll-like receptor (TLR) 2, TLR4, or MD-2. Bindings of lung collectins to TLR2 and TLR4/MD-2 result in the alterations of signaling through these receptors, suggesting the immunomodulatory functions of lung collectins. Mannose binding lectin (MBL) is another collectin molecule which has structural homology to SP-A.

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Lipopolysaccharide (LPS), derived from Gram-negative bacteria, is a major cause of acute lung injury and respiratory distress syndrome. Pulmonary surfactant is secreted as a complex mixture of lipids and proteins onto the alveolar surface of the lung. Surfactant phospholipids are essential in reducing surface tension at the air-liquid interface and preventing alveolar collapse at the end of the respiratory cycle.

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The role of MD-2 in cell surface expression of Toll-like receptor (TLR) 4 has been controversial. The purposes of this study were to characterize the N-glycan of TLR4 and to investigate the roles of MD-2 in N-linked glycosylation and cell surface expression of TLR4. Lectin blot and cell surface biotinylation revealed that TLR4 exhibited the 110 kDa protein with high mannose type N-glycans and the 130 kDa protein with complex type N-glycans and that only the 130 kDa TLR4 with complex type N-glycans was expressed on the cell surface.

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Objective: To determine the frequency of hearing impairment in children with congenital anomalies of the central nervous system (CNS) by using detailed audiological evaluation methods.

Methods: The patients were 78 children with congenital anomalies of the CNS with a mean age of 29.5 months.

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Pulmonary surfactant protein D (SP-D) is a member of the collectin family and plays crucial roles in the innate immunity of the lung. We have previously shown that surfactant protein A (SP-A), a homologous collectin, interacts with MD-2 and alters lipopolysaccharide signaling. In this study, we examined and characterized the binding of SP-D to MD-2 using a soluble form of recombinant MD-2 (sMD-2).

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Pulmonary surfactant protein D (SP-D) is a member of the collectin family that plays an important role in regulating innate immunity of the lung. We examined the mechanisms by which SP-D modulates lipopolysaccharide (LPS)-elicited inflammatory cell responses. SP-D bound to a complex of recombinant soluble forms of Toll-like receptor 4 (TLR4) and MD-2 with high affinity and down-regulated tumor necrosis factor-alpha secretion and NF-kappaB activation elicited by rough and smooth LPS, in alveolar macrophages and TLR4/MD-2-transfected HEK293 cells.

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Mycoplasma pneumoniae is an extracellular pathogen, residing on mucosal surfaces of the respiratory and genital tracts. The lack of cell walls in mycoplasmas facilitates the direct contact of the bacterial membrane with the host cell. The cell membrane of mycoplasma is the major inducer of the host pathogenic response.

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The class A scavenger receptor (SR-A) is a multifunctional transmembrane glycoprotein that is implicated in atherogenesis, innate immunity, and cell adhesion. Despite extensive structure-function studies of the receptor, intracellular molecules that directly interact with SR-A and regulate the receptor trafficking have not been determined. In the current study, we have identified a microtubule-binding protein, Hook3, as a novel interacting partner of SR-A.

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Pulmonary surfactant protein A (SP-A) belongs to the collectin subgroup of the C-type lectin superfamily. SP-A oligomerizes as an octadecamer, which forms a flower bouquet-like structure. A collagen-like domain of human SP-A consists of 23 Gly-X-Y repeats with an interruption near the midpoint of this domain.

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In this study, we sought the possibility of a new therapeutic strategy for dampening endotoxin-induced inflammation using soluble form of extracellular rTLR4 domain (sTLR4) and soluble form of rMD-2 (sMD-2). Addition of sTLR4 plus sMD-2 was significantly effective in inhibiting LPS-elicited IL-8 release from U937 cells and NF-kappaB activation in the cells transfected with TLR4 and MD-2 when compared with a single treatment with sTLR4 or sMD-2. Thus, we investigated the role of the extracellular TLR4 domain in interaction of lipid A with MD-2.

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Toll-like receptor 4 (TLR4) is a signaling receptor for lipopolysaccharide (LPS), but its interaction with MD-2 is required for efficient responses to LPS. Previous studies with deletion mutants indicate a critical role of the amino-terminal TLR4 region in interaction with MD-2. However, it is uncertain which region in the TLR4 molecule directly binds to MD-2.

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Article Synopsis
  • Fluoroquinolones, specifically gatifloxacin (GFLX), not only kill bacteria but also influence immune responses in monocytes and macrophages, particularly related to chronic prostatitis/chronic pelvic pain syndrome.
  • In experiments with the prostate cell line PC-3, GFLX was shown to reduce interleukin-8 (IL-8) production, suggesting it has anti-inflammatory properties against various stimulants like TNF-alpha.
  • GFLX achieved this by decreasing IL-8 mRNA expression and reducing the activity of the IL-8 gene promoter, indicating potential mechanisms for its effects in the prostate tissue.
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We investigated roles of scavenger receptor A (SR-A) and mannose-binding lectin (MBL) in the uptake of endotoxin and bacteria by Kupffer cells. When [3H]lipid A was injected into retro-orbital plexus of mice, significantly less accumulation of lipid A in the liver was observed in SR-A-deficient mice and wild-type mice coinjected with fucoidan or acetylated low-density lipoprotein, which are known ligands for SR-A. Isolated Kupffer cells were able to take up [3H]lipid A in a time-dependent manner.

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Ammonium is an important source of nitrogen for many microorganisms, including yeast, and its availability also has substantial effects on the nitrogen metabolism and development of yeast cells. Three ammonium transporter genes of the fission yeast Schizosaccharomyces pombe, named amt1, amt2, and amt3, were identified on the basis of amino acid sequence similarity to members of the ammonium transporter/methylammonium permease (Amt/Mep) family. A series of strains were constructed that carry all combinations of amt deletion (amt delta) mutations, and tested for growth on low ammonium and resistance to the toxic ammonium analog methylammonium.

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Article Synopsis
  • Pulmonary surfactant protein D (SP-D) is an innate immune protein that recognizes lipopolysaccharide (LPS) and interacts with Toll-like receptors (TLRs), specifically TLR2 and TLR4.
  • The study demonstrates that SP-D binds to soluble forms of TLR2 and TLR4 in a concentration- and calcium-dependent manner, with specific binding sites identified through monoclonal antibodies.
  • The findings suggest that the mechanism of SP-D binding to TLRs differs from its interaction with its major ligands, phosphatidylinositol (PI) and LPS, indicating a complex role in immune signaling.
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The purpose of the current study was to examine the binding of pulmonary surfactant protein A (SP-A) to TLR4 and MD-2, which are critical signaling receptors for lipopolysaccharides (LPSs). The direct binding of SP-A to the recombinant soluble form of extracellular TLR4 domain (sTLR4) and MD-2 was detected using solid-phase binding, immunoprecipitation, and BIAcore. SP-A bound to sTLR4 and MD-2 in a Ca2+-dependent manner, and an anti-SP-A monoclonal antibody whose epitope lies in the region Thr184-Gly194 blocked the SP-A binding to sTLR4 and MD-2, indicating the involvement of the carbohydrate recognition domain (CRD) in the binding.

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Alloiococcus otitidis has been found to be associated with otitis media with effusion. In this study we investigated whether TLR2 and collectins, surfactant protein A (SP-A) and mannose-binding lectin (MBL), interacted with A. otitidis.

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Pulmonary surfactant proteins (SP) A and D play important roles in the innate immune system of the lung. These proteins belong to the collectin subgroup in which lectin domains are associated with collagenous structures. To obtain a better understanding of how lung collectins modulate cellular responses, the authors investigated whether SP-A interacts with the toll-like receptor 2 (TLR2).

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