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)

Phorbol 12-myristate 13-acetate, 1-20 nM, induced the synthesis in HeLa cells of a 65 200 Mr tissue-type plasminogen activator, and of prostaglandin E2. Omission of Ca2+ from the incubation medium inhibited the induction of plasminogen activator synthesis by 40-60% and abolished the induction of prostaglandin E2 synthesis. Maximal plasminogen activator synthesis could be maintained at extracellular Ca2+ concentrations of approx. 0.1 mM, while maximal prostaglandin synthesis required at least 0.45-0.9 mM Ca2+. The induction of each factor was inhibited by 10-100 microM 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate (TMB-8), an inhibitor of intracellular C2+ mobilization. Prostaglandin synthesis, but not plasminogen activator synthesis, was also inhibited by 10-100 microM verapamil and nifedipine, which inhibit intracellular Ca2+ uptake via the so-called 'slow-channels' and by 0.5-10 microM trifluoperazine, an inhibitor of calmodulin. Neither plasminogen activator synthesis nor prostaglandin synthesis were stimulated by 5-50 microM 1-oleoyl-2-acetylglycerol or 1-250 microM 1,2-dioctanoylglycerol, alone and in combination with 50 nM-1 microM ionophore A23187. These results indicate that the synthesis of plasminogen activator and prostaglandins in HeLa cells is Ca2+-dependent, and that the Ca2+ requirements for each process are not identical. Thus, Ca2+ regulation of the production of tissue plasminogen activator and prostaglandin E2 occurs at multiple points in their biosynthetic pathways.
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PMID:Calcium regulation of tissue plasminogen activator and prostaglandin biosynthesis in HeLa cells. 308 71

The purification and properties of an estradiol-sensitive hydrolytic activity from mouse uterus which fits several criteria for being an induced protein are described. The activity in the uteri of immature animals can be stimulated 2--4-fold by estradiol to that approaching the adult level. Stimulation is blocked by puromycin. The enzyme which we have designated hydrolase II, was purified approx. 400-fold to apparent homogeneity by chromatography on Affigel Blue, DEAE-cellulose and octyl-Sepharose. Hydrolase II is a single chain polypeptide with an estimated mol. wt = 65,000 daltons and has an N-terminal serine residue. A variety of N-blocked L-amino acid nitrophenyl esters are cleaved by the enzyme. Km's at pH 7.2 were all approx. 40 microns. Of substrates tested, phenylalanine nitrophenyl ester had the highest Vmax. Cbz-beta-alanine nitrophenyl ester, which is not a normal protease substrate was cleaved with a Km of 145 microM. The enzyme had no detectable activity against peptide nitroanilide substrates for trypsin-, chymotrypsin- or elastase-like enzymes. It is inhibited by ZPCK and DIFP but not by TLCK and Ala-Ala-Pro-Ala chloromethyl ketone, a potent inhibitor of elastase-like enzymes. Mouse plasma protein protease inhibitors were without effect as was SBTI. Our results rule out hydrolase II being a carnosinase, non-serine esterase, plasminogen activator, collagenase or collagenase activator and suggest that it is a chymotrypsin-like protease.
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PMID:Properties of an estrogen-induced hydrolytic enzyme from mouse uterus. 635 Jul 23

New formulation strategies have to be developed to limit the skin penetration of UV-filter. Nanoparticles (NP) are very suitable for that purpose. In this study, the skin distribution, at different times (1, 2 and 3 h), of octyl-methoxycinnamate (OMC) from loaded PLA-nanoparticles was compared to a classical formulation containing non-encapsulated OMC, using the Franz cell method. The results showed that the OMC penetration was clearly impeded by stratum corneum and that the major part of the OMC-NP was accumulated at the skin surface (> 80%). A significant lower OMC amount was quantified in viable skin with NP compared to the OMC emulgel. To accurately determine the real OMC amount in close contact with viable skin layers two solvents were used to extract OMC from the skin compartments. Acetone (ACET) allowed quantifying both OMC in NP and OMC released from the particles, while isopropylmyristate (IPM), a non-solvent of the NP polymer (PLA), allowed quantifying only OMC released from the particles. Using IPM as an extraction solvent, it appeared that the OMC released from NP, in contact with viable skin, was 3-fold lower than free OMC diffused from the emulgel. Lastly, a sustained release was observed when nanoparticles were used.
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PMID:Skin absorption studies of octyl-methoxycinnamate loaded poly(D,L-lactide) nanoparticles: estimation of the UV filter distribution and release behaviour in skin layers. 2040 95

Films of poly(l-lactide) (PLA) plasticized with varying levels of N-octyl lactate (NOL) were prepared by extrusion. The thermal and functional properties of the blends were investigated by SEM, DSC, TGA, tensile, opacity, water vapor permeability, and water contact angle tests. The compatibility of the plasticizer with PLA was confirmed by DSC and SEM analysis. A higher plasticizing effect on the thermal properties of PLA was generally observed with the increase in NOL content. Additionally, the mechanical properties were improved with the increase in NOL content. The mechanical resistance of the films could be related to their glass transition temperature. The effect of the concentration of plasticizer on the opacity of the films was negligible. The water vapor permeability of the PLA/NOL composite films increased with the increase in the concentration of NOL; however, the values observed were still lower than the water vapor permeability of commercial LDPE films. In conclusion, the extruded PLA-based films with NOL plasticizers could be used as food-packaging materials.
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PMID:Effects of N-octyl lactate as plasticizer on the thermal and functional properties of extruded PLA-based films. 2459 2