We studied diaphragm function in a total of 64 normal subjects, who had no past or present respiratory or neuromuscular impairment. We measured transdiaphragmatic pressure (Pdi) during maximal sniffs and compared these values with Pdi during maximal static inspiratory efforts (PImax.). The range of Pdi during maximal sniffs (82-204 cm H2O) had better defined lower limits than Pdi during PImax. ...

Protein disulphide isomerase (PDI) shows chaperone and anti-chaperone activities in assisting refolding of denatured and reduced lysozyme in redox Hepes buffer, but only chaperone activity in phosphate buffer and redox Hepes buffer containing 0.1 M NaCl. In non-redox Hepes buffer its anti-chaperone activity is very weak. PDI displays its anti-chaperone activity only for those substrates showing...

e19651 Background: Cancer patients (CP) are frequently exposed to polypharmacy, which may increase their risk for drug interactions. Our study aims were to 1) determine and compare the prevalence and clinical significance of potential drug interactions (PDI) in CP vs. non-cancer patients (NCP) and 2) identify clinical risk factors associated with PDI in CP. METHODS Self-reported prescription ...

Herein, balanced intermixed and pure crystalline phases in N,N'-bis(1-ethylpropyl)-perylene-3,4,9,10-tetracarboxylic diimide (EP-PDI)-based non-fullerene organic solar cells (OSCs) were achieved via selective solvent additives (SAs). Poly[[4,8-bis[(2-ethylhexyl)oxy]benzo[1,2-b:4,5-b']dithiophene-2,6-diyl][3-fluoro-2-[(2-ethylhexyl)carbonyl]thieno[3,4-b]thiophenediyl]] (PTB7) and 7,7'-(4,4-bis(2...

BACKGROUND: Protein disulfide isomerase (PDI) is required for thrombus formation. We previously demonstrated that glycosylated quercetin flavonoids such as isoquercetin inhibit PDI activity and thrombus formation in animal models, but whether extracellular PDI represents a viable anticoagulant target in humans and how its inhibition affects blood coagulation remain unknown. METHODS: We evaluate...

The activation of initiator protein tissue factor (TF) is likely to be a crucial step in the blood coagulation process, which leads to fibrin formation. The stimuli responsible for inducing TF activation are largely undefined. Here we show that the oxidoreductase protein disulfide isomerase (PDI) directly promotes TF-dependent fibrin production during thrombus formation in vivo. After endotheli...

ERcalcistorin/protein-disulfide isomerase (ECaSt/PDI), a high capacity low affinity Ca2+-binding protein in the endoplasmic reticulum of sea urchin eggs (Lebeche, D., and Kaminer, B. (1992) Biochem. J. 287, 741-747), shares 55% sequence identity with mammalian PDI and has PDI activity (Lucero, H., Lebeche, D., and Kaminer, B. (1994) J. Biol. Chem. 269, 23112-23119). We report on ECaSt/PDI funct...

Protein Disulfide Isomerase (PDI) was originally discovered fifty years ago as the first protein folding catalyst and isolated from rat liver [1]. It was demonstrated early on that PDI acts as a dithiol–disulfide oxidoreductase capable of reducing, oxidizing and isomerizing disulfide bonds. Independently of its redox activity, PDI can also act as a vital cellular defense against the intracellul...

Protein disulfide isomerase (PDI) is a 55 kDa multifunctional protein of the endoplasmic reticulum (ER) involved in protein folding and isomerization. In addition to the chaperone and catalytic functions, PDI is a major calcium-binding protein of the ER. Although the active site of PDI has a similar motif CXXC to the Cu-binding motif in Wilson and Menkes proteins and in other copper chaperones,...

Protein disulfide isomerase (PDI) is an abundant reticulum endoplasmic protein but also acts as an important functional regulator of some extracellular surface proteins. Recent studies suggest that PDI plays a role in integrin activation and thrombus formation. The aim of this study was to examine whether activation of integrin is the first stage leading to release of PDI from the subcellular c...