Phencyclidine and the Dynamics of Mouse Brain Histamine

ABSTRAC

Influence of storage temperature on indomethacin release from fatty-base suppositories in vitro and in vivo.

The release of indomethacin from fatty-base suppositories, which had been stored at a low (4 degrees C) and a high (25-30 degrees C) temperature for about one month, was examined in vitro and in vivo. In the in vivo experiments, the plasma indomethacin levels after administration of suppositories stored at different temperatures were measured in conscious and anesthetized rats. In the in vitro release test using a dialysis cell method, much lower amounts of indomethacin were released from the suppositories stored at a high temperature than from those stored at a low temperature. The melting point of suppositories stored at a high temperature was higher by approximately 2 degrees C than those stored at a low temperature. In conscious rats, the plasma indomethacin levels attained after the intrarectal administration of suppositories stored at a high temperature were slightly lower than those after the animals were given suppositories stored at a low temperature, but the difference was significant only 30 min after administration. In anesthetized rats, the plasma indomethacin levels were markedly lower than those in conscious rats, and the influence of the storage temperature on the plasma indomethacin levels was clearly observed. These results suggest that in conscious rats many factors such as a locomotor hyperactivity and enhancement of gastrointestinal motility caused by the rectal administration mask the real character of suppositories. The in vitro and in vivo results show that the release of indomethacin from fatty-base suppositories stored at a high temperature is less than the release from those stored at a low temperature.</p

Effects of 6-month eicosapentaenoic acid treatment on postprandial hyperglycemia, hyperlipidemia, insulin secretion ability, and concomitant endothelial dysfunction among newly-diagnosed impaired glucose metabolism patients with coronary artery disease. An open label, single blinded, prospective randomized controlled trial

Additional file 2: Table S2. Comparison of cookie meal test data between baseline and 6 months, and comparison of absolute change from baseline among patients with baseline plasma glucose <110 mg/dL

Beta-Arrestin Functionally Regulates the Non-Bleaching Pigment Parapinopsin in Lamprey Pineal

The light response of vertebrate visual cells is achieved by light-sensing proteins such as opsin-based pigments as well as signal transduction proteins, including visual arrestin. Previous studies have indicated that the pineal pigment parapinopsin has evolutionally and physiologically important characteristics. Parapinopsin is phylogenetically related to vertebrate visual pigments. However, unlike the photoproduct of the visual pigment rhodopsin, which is unstable, dissociating from its chromophore and bleaching, the parapinopsin photoproduct is stable and does not release its chromophore. Here, we investigated arrestin, which regulates parapinopsin signaling, in the lamprey pineal organ, where parapinopsin and rhodopsin are localized to distinct photoreceptor cells. We found that beta-arrestin, which binds to stimulated G protein-coupled receptors (GPCRs) other than opsin-based pigments, was localized to parapinopsin-containing cells. This result stands in contrast to the localization of visual arrestin in rhodopsin-containing cells. Beta-arrestin bound to cultured cell membranes containing parapinopsin light-dependently and translocated to the outer segments of pineal parapinopsin-containing cells, suggesting that beta-arrestin binds to parapinopsin to arrest parapinopsin signaling. Interestingly, beta-arrestin colocalized with parapinopsin in the granules of the parapinopsin-expressing cell bodies under light illumination. Because beta-arrestin, which is a mediator of clathrin-mediated GPCR internalization, also served as a mediator of parapinopsin internalization in cultured cells, these results suggest that the granules were generated light-dependently by beta-arrestin-mediated internalization of parapinopsins from the outer segments. Therefore, our findings imply that beta-arrestin-mediated internalization is responsible for eliminating the stable photoproduct and restoring cell conditions to the original dark state. Taken together with a previous finding that the bleaching pigment evolved from a non-bleaching pigment, vertebrate visual arrestin may have evolved from a “beta-like” arrestin by losing its clathrin-binding domain and its function as an internalization mediator. Such changes would have followed the evolution of vertebrate visual pigments, which generate unstable photoproducts that independently decay by chromophore dissociation