Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00750 (PLA)
 16,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

FSAP (Factor VII-activating protease) is a new plasma-derived serine protease with putative dual functions in haemostasis, including activation of coagulation Factor VII and generation of urinary-type plasminogen activator (urokinase). The (auto-)activation of FSAP is facilitated by polyanionic glycosaminoglycans, such as heparin or dextran sulphate, whereas calcium ions stabilize the active form of FSAP. In the present study, extracellular RNA was identified and characterized as a novel FSAP cofactor. The conditioned medium derived from various cell types such as smooth muscle cells, endothelial cells, osteosarcoma cells or CHO (Chinese-hamster ovary) cells contained an acidic factor that initiated (auto-)activation of FSAP. RNase A, but not other hydrolytic enzymes (proteases, glycanases and DNase), abolished the FSAP cofactor activity, which was subsequently isolated by anion-exchange chromatography and unequivocally identified as RNA. In purified systems, as well as in plasma, different forms of natural RNA (rRNA, tRNA, viral RNA and artificial RNA) were able to (auto-)activate FSAP into the two-chain enzyme form. The specific binding of FSAP to RNA (but not to DNA) was shown by mobility-shift assays and UV crosslinking, thereby identifying FSAP as a new extracellular RNA-binding protein, the K(D) estimated to be 170-350 nM. Activation of FSAP occurred through an RNA-dependent template mechanism involving a nucleic acid size of at least 100 nt. In a purified system, natural RNA augmented the FSAP-dependent Factor VII activation several-fold (as shown by subsequent Factor Xa generation), as well as the FSAP-mediated generation of urokinase. Our results provide evidence for the first time that extracellular RNA, present at sites of cell damage or vascular injury, can serve an important as yet unrecognized cofactor function in haemostasis by inducing (auto-)activation of FSAP through a novel surface-dependent mechanism.
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PMID:Extracellular RNA is a natural cofactor for the (auto-)activation of Factor VII-activating protease (FSAP). 1565 66

Poly(lactic) acid (PLA) is one of the most promising biobased materials, but its inherent flammability limits its applications. A novel flame retardant hexa-(DOPO-hydroxymethylphenoxy-dihydroxybiphenyl)-cyclotriphosphazene (HABP-DOPO) for PLA was prepared by bonding 9,10-dihydro-9-oxy-10-phosphaphenanthrene-10-oxide (DOPO) to cyclotriphosphazene. The morphologies, mechanical properties, thermal stability and burning behaviors of PLA/HABP-DOPO blends were investigated using a scanning electron microscope (SEM), a universal mechanical testing machine, thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), limiting oxygen index (LOI), vertical burning (UL-94) and a cone calorimeter test (CCT). The LOI value reached 28.5% and UL-94 could pass V-0 for the PLA blend containing 25 wt% HABP-DOPO. A significant improvement in fire retardant performance was observed for PLA/HABP-DOPO blends. PLA/HABP-DOPO blends exhibited balanced mechanical properties. The flame retardant mechanism of PLA/HABP-DOPO blends was evaluated.
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PMID:Effect of a Novel Flame Retardant on the Mechanical, Thermal and Combustion Properties of Poly(Lactic Acid). 3308 26