Is a euryhaline fugu species very close to and suitable for studying osmoregulation-1

<p><b>Copyright information:</b></p><p>Taken from "is a euryhaline fugu species very close to and suitable for studying osmoregulation"</p><p>BMC Physiology 2005;5():18-18.</p><p>Published online 20 Dec 2005</p><p>PMCID:PMC1351200.</p><p>Copyright © 2005 Kato et al; licensee BioMed Central Ltd.</p>n = 18 for FW; , n = 35 for FW and n = 36 for BW; , n = 10 for FW and n = 6 for BW; , n = 32 for FW and n = 10 for BW; , n = 26 for FW and n = 11 for BW; and , n = 6 for FW

Is a euryhaline fugu species very close to and suitable for studying osmoregulation-4

<p><b>Copyright information:</b></p><p>Taken from "is a euryhaline fugu species very close to and suitable for studying osmoregulation"</p><p>BMC Physiology 2005;5():18-18.</p><p>Published online 20 Dec 2005</p><p>PMCID:PMC1351200.</p><p>Copyright © 2005 Kato et al; licensee BioMed Central Ltd.</p>ies were used for the analyses. Bootstrap values from 2,000 times replications are indicated at major nodes. Bars indicate 5% replacement of a nucleotide per site. Accession numbers were as follows: , AB199318; , AB199319; , AB199320; , AB199321; , AB199322; , AB199323; , CR688806; , NC_004387; , NC_001717; , J01415; , J01420; and , X14848

Is a euryhaline fugu species very close to and suitable for studying osmoregulation-3

<p><b>Copyright information:</b></p><p>Taken from "is a euryhaline fugu species very close to and suitable for studying osmoregulation"</p><p>BMC Physiology 2005;5():18-18.</p><p>Published online 20 Dec 2005</p><p>PMCID:PMC1351200.</p><p>Copyright © 2005 Kato et al; licensee BioMed Central Ltd.</p>ematoxylin and eosin and examined for abundance of glomeruli. All the other species, , , , and , also have glomerulous nephron (data not shown). . Higher magnification view of the glomeruli of FW-acclimated indicated by a box in A. . Higher magnification views of the glomeruli of SW-acclimated indicated by boxes in B. . Paraffin-embedded sections of the kidneys of indicated species were stained with anti-Na-K-ATPase (NKA) antibody (green) and Hoechst 33342 (red). NKA antibody strongly stained basolateral surface of proximal segment (p) and entire cell of distal segment (d). , , and showed similar result to (data not shown). . Frozen sections of the kidneys of were stained with anti-NKA antibody (red) and Alaxa Fluor 488-labeled phalloidin (green). Phalloidin binds to actin filaments, and strongly stains a well-developed apical brush border of proximal segments. . Proximal segment of the nephron of . . Distal segment of the nephron of . All scale bars represent 50 μm

Is a euryhaline fugu species very close to and suitable for studying osmoregulation-0

<p><b>Copyright information:</b></p><p>Taken from "is a euryhaline fugu species very close to and suitable for studying osmoregulation"</p><p>BMC Physiology 2005;5():18-18.</p><p>Published online 20 Dec 2005</p><p>PMCID:PMC1351200.</p><p>Copyright © 2005 Kato et al; licensee BioMed Central Ltd.</p

Development of a Novel Ligand, [¹¹C]TGN-020, for Aquaporin 4 Positron Emission Tomography Imaging

Aquaporin 4 (AQP4), the most abundant isozyme of the water specific membrane transporter aquaporin family, has now been implicated to play a significant role in the pathogenesis of various disease processes of the nervous system from epilepsy to Alzheimer’s disease. Considering its clinical relevance, it is highly desirable to develop a noninvasive method for the quantitative analysis of AQP distribution in humans under clinical settings. Currently, the method of choice for such diagnostic examinations continues to be positron emission tomography (PET). Here, we report the successful development of a PET ligand for AQP4 imaging based on TGN-020, a potent AQP4 inhibitor developed previously in our laboratory. Utilizing [¹¹C]-TGN-020, PET images were successfully generated in wild type and AQP4 null mice, providing a basis for future evaluation regarding its suitability for clinical studies

Changes in Ang1-positive vessels due to focal cerebral ischemia.

<p>(A) Immunohistochemical staining with an anti-Ang1 antibody. Representative findings are shown of the peri-infarct and infarct areas of the control, tPA-1h, tPA-4h, and PMCAO groups. High magnification (1,000×) is shown in the upper right of the low magnification (200×) photograph. Ang1-positive vessels were shown by asterisk. tPA, tissue plasminogen activator; PMCAO, permanent middle cerebral artery occlusion; Ang1, angiopoietin-1. The black scale bar is 10 µm, and the red scale bar is 100 µm. (B) Mean number of Ang1-positive vessels. Three locations were chosen randomly in the control cerebral cortex and in each infarct area and peri-infarct area. The figures are the mean number of Ang1-positive vessels from 3 random fields of view of an optical microscope at 200× magnification. Each group N = 5.</p

COMP-Ang1 protein localization in the tPA-4h group visualized with a confocal laser microscope.

<p>From left to right: markers of cells that make up the blood brain barrier (a, e, i; red), neuronal cell (m; red), COMP-Ang1 protein (b, f, j, n; green), DAPI stain (c, g, k, o; blue), and a merged image (d, h, l, p). Immunostaining with an anti-FLAG antibody was performed on COMP-Ang1 proteins in order to differentiate them from endogenous Ang1. RECA1 is an endothelial cell marker protein; PDGFRβ is a pericyte marker; GFAP is an astrocyte marker; and MAP2 is a neuronal cell marker. RECA1, rat endothelial cell antigen; PDGFRβ, platelet-derived growth factor receptor; GFAP, glial fibrillary acidic protein; Ang1, angiopoietin-1. The scale bars are 10 µm.</p

Effects of COMP-Ang1 protein administration on the tPA-4h group.

<p>These panels show the amount of cerebral hemorrhage (A), cerebral edema volume (B), cerebral infarct volume (C), and the prognosis with a 6-point neurological scale score (D) 24 h after ischemia. A-C were performed on the COMP-Ang1 group (N = 5) and the COMP group (N = 5). D was performed on the COMP-Ang1 group (N = 11) and the COMP group (N = 9). Cerebral edema and infarct volumes are expressed as proportions on the ischemic side of the cerebral hemisphere. The amount of cerebral hemorrhage is expressed as hemoglobin concentration in a whole cerebral homogenate. COMP; cartilage oligomeric protein, COMP-Ang1; cartilage oligomeric protein-angiopoietin-1.</p

Effects of Alda-1, an Aldehyde Dehydrogenase-2 Agonist, on Hypoglycemic Neuronal Death

<div><p>Hypoglycemic encephalopathy (HE) is caused by a lack of glucose availability to neuronal cells, and no neuroprotective drugs have been developed as yet. Studies on the pathogenesis of HE and the development of new neuroprotective drugs have been conducted using animal models such as the hypoglycemic coma model and non-coma hypoglycemia model. However, both models have inherent problems, and establishment of animal models that mimic clinical situations is desirable. In this study, we first developed a short-term hypoglycemic coma model in which rats could be maintained in an isoelectric electroencephalogram (EEG) state for 2 min and subsequent hyperglycemia without requiring anti-seizure drugs and an artificial ventilation. This condition caused the production of 4-hydroxy-2-nonenal (4-HNE), a cytotoxic aldehyde, in neurons of the hippocampus and cerebral cortex, and a marked increase in neuronal death as evaluated by Fluoro-Jade B (FJB) staining. We also investigated whether <i>N</i>-(1,3-benzodioxole-5-ylmethyl)-2,6-dichlorobenzamide (Alda-1), a small-molecule agonist of aldehyde dehydrogenase-2, could attenuate 4-HNE levels and reduce hypoglycemic neuronal death. After confirming that EEG recordings remained isoelectric for 2 min, Alda-1 (8.5 mg/kg) or vehicle (dimethyl sulfoxide; DMSO) was administered intravenously with glucose to maintain a blood glucose level of 250 to 270 mg/dL. Fewer 4-HNE and FJB-positive cells were observed in the cerebral cortex of Alda-1-treated rats than in DMSO-treated rats 24 h after glucose administration (<i>P</i> = 0.002 and <i>P</i> = 0.020). Thus, activation of the ALDH2 pathway could be a molecular target for HE treatment, and Alda-1 is a potentially neuroprotective agent that exerts a beneficial effect on neurons when intravenously administered simultaneously with glucose.</p></div

Reduced CSF Water Influx in Alzheimer’s Disease Supporting the β-Amyloid Clearance Hypothesis

<div><p>Objective</p><p>To investigate whether water influx into cerebrospinal fluid (CSF) space is reduced in Alzheimer’s patients as previously shown in the transgenic mouse model for Alzheimer’s disease.</p><p>Methods</p><p>Ten normal young volunteers (young control, 21-30 years old), ten normal senior volunteers (senior control, 60-78 years old, MMSE ≥ 29), and ten Alzheimer’s disease (AD) patients (study group, 59-84 years old, MMSE: 13-19) participated in this study. All AD patients were diagnosed by neurologists specializing in dementia based on DSM-IV criteria. CSF dynamics were analyzed using positron emission tomography (PET) following an intravenous injection of 1,000 MBq [¹⁵O]H₂O synthesized on-line.</p><p>Results</p><p>Water influx into CSF space in AD patients, expressed as influx ratio, (0.755 ± 0.089) was significantly reduced compared to young controls (1.357 ± 0.185; p < 0.001) and also compared to normal senior controls (0.981 ± 0.253, p < 0.05). Influx ratio in normal senior controls was significantly reduced compared to young controls (p < 0.01).</p><p>Conclusion</p><p>Water influx into the CSF is significantly reduced in AD patients. β-amyloid clearance has been shown to be dependent on interstitial flow and CSF production. The current study indicates that reduction in water influx into the CSF may disturb the clearance rate of β-amyloid, and therefore be linked to the pathogenesis of AD.</p><p>Trial Registration</p><p>UMIN Clinical Trials Registry <a href="https://upload.umin.ac.jp/cgi-open-bin/ctr/ctr.cgi?function=brows&action=brows&recptno=R000013940&type=summary&language=E" target="_blank">UMIN000011939</a></p></div