Proteinase-activated receptors are a recently described, novel family of seven-transmembrane G-protein-coupled receptors. Rather then being stimulated through ligand receptor occupancy, activation is initiated by cleavage of the N terminus of the receptor by a serine protease resulting in the generation of a new tethered ligand that interacts with the receptor within extracellular loop-2. To date, four proteinase-activated receptors (PARs) have been identified, with distinct N-terminal cleavage sites and tethered ligand pharmacology. In addition to the progress in the generation of PAR-1 antagonists, we describe the role of thrombin in such processes as wound healing and the evidence implicating PAR-1 in vascular disorders and cancer. We also identify advances in the understanding of PAR-1-mediated intracellular signaling and receptor desensitization. The cellular functions, signaling events, and desensitization processes involved in PAR-2 activation are also assessed. However, other major aspects of PAR-2 are highlighted, in particular the ability of several serine protease enzymes, in addition to trypsin, to function as activators of PAR-2. The likely physiological and pathophysiological roles for PAR-2 in skin, intestine, blood vessels, and the peripheral nervous system are considered in the context of PAR-2 activation by multiple serine proteases. The recent discovery of PAR-3 and PAR-4 as additional thrombin-sensitive PARs further highlights the complexity in assessing the effects of thrombin in several different systems, an issue that remains to be fully addressed. These discoveries have also highlighted possible PAR–PAR interactions at both functional and molecular levels. The future identification of other PARs and their modes of activation are an important future direction for this expanding field of study.

Proteinase-Activated Receptors

Selective Targeting of a Redox-active Ubiquinone to Mitochondria within Cells: ANTIOXIDANT AND ANTIAPOPTOTIC PROPERTIES *

https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1538-7836.2005.01377.x

Protease-activated receptors in hemostasis, thrombosis and vascular biology.

Proteinase-activated receptors

A battery management system (BMS) includes at least one sub-BMS and a main BMS. The at least one sub-BMS measures information about a battery, and generates an activation signal according to operating state. The main BMS receives the activation signal and determines the operating state of the at least two sub-BMSs. If the at least two sub-BMSs normally operate, the main BMS generates a synchronization signal and transfers the same to the sub-BMSs. The at least one sub-BMS measures the information about the battery according to the synchronization signal.

Battery management system and driving method thereof

Publisher Summary Quantitative analyses of individual ubiquinones (Q) homologs in biological samples have been performed by high-performance liquid chromatography (HPLC) combined with an ultraviolet spectrometric detector (UVD) or by mass spectrometry (MS). An electrochemical detector (ECD) for HPLC was confirmed to be simple and sensitive for the determination of Q. However, only Q was determined by these methods. For the determination of QH 2 (ubiquinol) and Q in mitochondria, submitochondrial particle and cell-free bacterial homogenates, the dual-wavelength spectrometric method has been generally used. The method, however, cannot simultaneously measure the amounts of QH 2 and Q in whole tissues owing to the presence of vitamin A and other interfering compounds, which have an absorbance in the same spectral region as Q and undergo an absorption change by chemical reduction. The dual-wavelength spectrometric method cannot separately determine individual Q homologs. The analytical procedure described was developed to provide a rapid, sensitive, and direct assay method for QH 2 and Q in biological samples. This method is based on extraction from tissues, mitochondria, microsomal fractions, or plasma with organic solvents, followed by quantitation by means of reversed-phase chromatography with UVD and ECD.

Simultaneous determination of reduced and oxidized ubiquinones.

Increased lung uptake of liposomes coated with polysaccharides

Studies on reduced and oxidized coenzyme Q (ubiquinones). II. The determination of oxidation-reduction levels of coenzyme Q in mitochondria, microsomes and plasma by high-performance liquid chromatography

Studies on reduced and oxidized ubiquinones. I. Simultaneous determination of reduced and oxidized ubiquinones in tissues and mitochondria by high performance liquid chromatography.

Masahiro Takada

Papers

Simultaneous determination of reduced and oxidized ubiquinones.

Increased lung uptake of liposomes coated with polysaccharides

Studies on reduced and oxidized coenzyme Q (ubiquinones). II. The determination of oxidation-reduction levels of coenzyme Q in mitochondria, microsomes and plasma by high-performance liquid chromatography

Studies on reduced and oxidized ubiquinones. I. Simultaneous determination of reduced and oxidized ubiquinones in tissues and mitochondria by high performance liquid chromatography.

Simultaneous determination of ubiquinone-10 and ubiquinol-10 in tissues and mitochondria by high performance liquid chromatography