53 research outputs found
Modulation of left ventricular diastolic distensibility by collateral flow recruitment during balloon coronary occlusion
AbstractOBJECTIVESThe goals of this study were to elucidate the scaffolding effect of blood-filled coronary vasculature and to determine the functional role of recruited collateral flow in modulating left ventricular (LV) distensibility during balloon coronary occlusion (BCO).BACKGROUNDAlthough LV distensibility is an important factor affecting acute dilation after myocardial infarction, the response of LV diastolic pressure–volume (P-V) relations to coronary occlusion is inconsistent in humans.METHODSMicromanometer and conductance derived LV P-V loops were serially obtained from 16 patients undergoing percutaneous transluminal coronary angioplasty. Coronary collateral flow recruitment was angiographically evaluated by contralateral and ipsilateral contrast injection during BCO.RESULTSIn the group with poor collateral flow (grades 0–I; n = 8), BCO resulted in a downward and rightward shift of the diastolic P-V relations, where end-diastolic volume (EDV) increased by 13% (p < 0.05) without appreciable change in end-diastolic pressure (EDP; 18 ± 6 to 18 ± 8 mm Hg). In contrast, BCO in the group with good collateral flow (grades II–III; n = 8) shifted the diastolic P-V relations upward to the right with a concomitant increase in minimal pressure (min-P; 6 ± 4 to 10 ± 5 mm Hg, p < 0.05), EDP (15 ± 7 to 21 ± 9 mm Hg, p < 0.05) and EDV (+10%, p < 0.05). Reactive hyperemia after balloon deflation caused a rapid and parallel upward shift of the diastolic P-V relations with a marked increase in min-P and EDP, especially in the group with poor collateral flow, before any improvement in LV contraction or relaxation abnormalities.CONCLUSIONSGrades of coronary filling, either retrograde or anterograde, abruptly modulate LV distensibility through the rapid scaffolding effect of coronary vascular turgor
Mapping of a Melting Zone near Mt.Nikko-Shirane in Northern Kanto, Japan, as inferred from SxP and SxS Reflections
Bmi-1 regulates mucin levels and mucin O-glycosylation in the submandibular gland of mice.
Mucins, the major components of salivary mucus, are large glycoproteins abundantly modified with O-glycans. Mucins present on the surface of oral tissues contribute greatly to the maintenance of oral hygiene by selectively adhering to the surfaces of microbes via mucin O-glycans. However, due to the complex physicochemical properties of mucins, there have been relatively few detailed analyses of the mechanisms controlling the expression of mucin genes and the glycosyltransferase genes involved in glycosylation. Analysis performed using supported molecular matrix electrophoresis, a methodology developed for mucin analysis, and knockout mice without the polycomb group protein Bmi-1 revealed that Bmi-1 regulates mucin levels in the submandibular gland by suppressing the expression of the mucin Smgc gene, and that Bmi-1 also regulates mucin O-glycosylation via suppression of the glycosyltransferase Gcnt3 gene in the submandibular gland
Synthesis of New Photoresponsive Polyesters Containing Donor−Acceptor Norbornadiene (D−A NBD) Residues by the Polyaddition of D−A NBD Dicarboxylic Acids with Bis(epoxide)s and Their Photochemical Properties
Fine-Needle Aspiration Cytology for Diagnosing Thyroid Nodules Based on a New Reporting System
A Procedure for Alcian Blue Staining of Mucins on Polyvinylidene Difluoride Membranes
The isolation and characterization of mucins are critically
important
for obtaining insight into the molecular pathology of various diseases,
including cancers and cystic fibrosis. Recently, we developed a novel
membrane electrophoretic method, <i>supported molecular matrix
electrophoresis </i>(SMME), which separates mucins on a polyvinylidene
difluoride (PVDF) membrane impregnated with a hydrophilic polymer.
Alcian blue staining is widely used to visualize mucopolysaccharides
and acidic mucins on both blotted membranes and SMME membranes; however,
this method cannot be used to stain mucins with a low acidic glycan
content. Meanwhile, periodic acid–Schiff staining can selectively
visualize glycoproteins, including mucins, but is incompatible with
glycan analysis, which is indispensable for mucin characterizations.
Here we describe a novel staining method, designated succinylation-Alcian
blue staining, for visualizing mucins on a PVDF membrane. This method
can visualize mucins regardless of the acidic residue content and
shows a sensitivity 2-fold higher than that of Pro-Q Emerald 488,
a fluorescent periodate Schiff-base stain. Furthermore, we demonstrate
the compatibility of this novel staining procedure with glycan analysis
using porcine gastric mucin as a model mucin
Direct On-Membrane Glycoproteomic Approach Using MALDI-TOF Mass Spectrometry Coupled with Microdispensing of Multiple Enzymes
Three cases of pulmonary resection for new lesions in the contralateral lung following pneumonectomy
Rapid chemical de-N-glycosylation and derivatization for liquid chromatography of immunoglobulin N-linked glycans
<div><p>Glycan analysis may result in exploitation of glycan biomarkers and evaluation of heterogeneity of glycosylation of biopharmaceuticals. For N-linked glycan analysis, we investigated alkaline hydrolysis of the asparagine glycosyl carboxamide of glycoproteins as a deglycosylation reaction. By adding hydroxylamine into alkaline de-N-glycosylation, we suppressed the degradation of released glycans and obtained a mixture of oximes, free glycans, and glycosylamines. The reaction was completed within 1 h, and the mixture containing oximes was easily tagged with 2-aminobenzamide by reductive amination. Here, we demonstrated N-linked glycan analysis using this method for a monoclonal antibody, and examined whether this method could liberate glycans without degradation from apo-transferrin containing NeuAc and NeuGc and horseradish peroxidase containing Fuc α1–3 GlcNAc at the reducing end. Furthermore, we compared glycan recoveries between conventional enzymatic glycan release and this method. Increasing the reaction temperature and reaction duration led to degradation, whereas decreasing these parameters resulted in lower release. Considering this balance, we proposed to carry out the reaction at 80°C for 1 h for asialo glycoproteins from mammals and at 50°C for 1 h for sialoglycoproteins.</p></div
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