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The crystal structures of four cyclo­alkane­spiro-4′-imidazolidine-2′,5′-dithiones, namely cyclo­pentane­spiro-4′-imidazolidine-2′,5′-dithione {systematic name: 1,3-diaza­spiro­[4.4]­nonane-2,4-dithione}, C7H10N2S2, cyclo­hexane­spiro-4′-imidazolidine-2′,5′-dithione {systematic name: 1,3-diaza­spiro­[4.5]decane-2,4-dithione}, C8H12N2S2, cyclo­heptane­spiro-4′-imidazolidine-2′,5′-dithione {systematic name: 1,3-diaza­spiro­[4.6]undecane-2,4-dithione}, C9H14N2S2, and cyclo­octane­spiro-4′-imidazolidine-2′,5′-dithione {systematic name: 1,3-di­aza­spiro­[4.7]dodecane-2,4-dithione}, C10H16N2S2, have been determined. The three-dimensional packing in all of the structures is based on closely similar chains, in which hydantoin moieties are linked through N—H⋯S hydrogen bonding. The size of the cyclo­alkane moiety influences the degree of its deformation. In the cyclo­octane compound, the cyclo­octane ring assumes both boat–chair and boat–boat conformations. [ABSTRACT FROM AUTHOR]

The title compound [systematic name: 1′-amino­cyclo­hexane­spiro-4′-imidazole-2′,5′(3′ H,4′ H)-dione], C8H13N3O2, has been synthesized and was found to crystallize in two different structures, both monoclinic and both with the same P21/ c space group. In the first structure, there are two mol­ecules in the asymmetric unit, one of which uses all of its hydrogen-bond donors and acceptors and forms undulating layers, while the other forms chains propagating perpendicular to the layers. In the second structure, there is only one independent mol­ecule and the packing is based on a chain structure mediated by hydrogen bonding between the hydantoin moieties and further grouped into hydro­philic layers separated by layers of the hydro­phobic cyclo­hex­yl groups. [ABSTRACT FROM AUTHOR]

The article presents information on the structure of codeinone. Codeinone has been found to possess antitumor potential, with high cytotoxic activity against human promyelocytic leukaemic cell lines and is known that codeinone in the living cell is produced from the reaction of codeine with nicotinamide adenine dinucleotide phosphate. The molecular structure exhibits features typical for morphine derivatives, with a T-shaped configuration. The crystal packing was found to be stabilized by weak intermolecular C-H&3x22EF;O interactions.

The title compound (systematic name: 6α-acet­oxy-4,5α-ep­oxy-3-meth­oxy-17-meth­yl-morphin-7-ene), C20H23NO4, crystallizes with one mol­ecule in the asymmetric unit. The mol­ecular structure exhibits features typical of morphine derivatives with a T configuration. The three-dimensional packing is stabilized by inter­molecular C—H⋯N and C—H⋯π inter­actions. [ABSTRACT FROM AUTHOR]

The mol­ecule of the title compound, C21H22N2O2, is nearly planar, except for the C(CH3)2 group on the cyclo­hexene ring. Molecules are connected via electrostatic C⋯O contacts, forming zigzag pseudo-chains along the c axis. [ABSTRACT FROM AUTHOR]

In the title compound, sodium 2-hydr­oxy-3,4-dioxocyclo­but-1-en-1-olate monohydrate, Na+·C4HO4−·H2O, the Na atom is six-coordinated by the O atoms from four hydrogensquarate anions and two water mol­ecules. The three-dimensional packing is stabilized by a system of hydrogen bonds. [ABSTRACT FROM AUTHOR]

The optical properties of the bovine lens have been shown to be actively maintained by an internal microcirculation system. In the mouse lens, this water transport through gap junction channels generates an intracellular hydrostatic pressure gradient, which is subjected to a dual feedback regulation that is mediated by the reciprocal modulation of the transient receptor potential vanilloid channels TRPV1 and TRPV4. Here we test whether a similar feedback regulation of pressure exists in the bovine lens and whether it regulates overall lens optics. Lens pressure was measured using a microelectrode/pico-injector-based pressure measurement system, and lens optics were monitored in organ cultured lenses using a laser ray tracing system. Like the mouse, the bovine lenses exhibited a similar pressure gradient (0 to 340 mmHg). Activation of TRPV1 with capsaicin caused a biphasic increase in surface pressure, while activation of TRPV4 with GSK1016790A caused a biphasic decrease in pressure. These biphasic responses were abolished if lenses were preincubated with either the TRPV1 inhibitor A-889425 or the TRPV4 inhibitor HC-067047. While modulation of lens pressure by TRPV1 and TRPV4 had minimal effects on lens power and overall vision quality, the changes in lens pressure did induce opposing changes to lens geometry and its gradient of refractive index that effectively kept lens power constant. Hence, our results suggest that the TRPV1/4-mediated feedback control of lens hydrostatic pressure operates to ensure that any fluctuations in lens water transport, and consequently water content, do not result in changes in lens power and therefore overall vision quality.

Although the functionality of the lens water channels aquaporin 1 (AQP1; epithelium) and AQP0 (fiber cells) is well established, less is known about the role of AQP5 in the lens. Since in other tissues AQP5 functions as a regulated water channel with a water permeability (P H2O ) some 20 times higher than AQP0, AQP5 could function to modulate P H2O in lens fiber cells. To test this possibility, a fluorescence dye dilution assay was used to calculate the relative P H2O of epithelial cells and fiber membrane vesicles isolated from either the mouse or rat lens, in the absence and presence of HgCl 2 , an inhibitor of AQP1 and AQP5. Immunolabeling of lens sections and fiber membrane vesicles from mouse and rat lenses revealed differences in the subcellular distributions of AQP5 in the outer cortex between species, with AQP5 being predominantly membranous in the mouse but predominantly cytoplasmic in the rat. In contrast, AQP0 labeling was always membranous in both species. This species-specific heterogeneity in AQP5 membrane localization was mirrored in measurements of P H2O , with only fiber membrane vesicles isolated from the mouse lens, exhibiting a significant Hg 2+ -sensitive contribution to P H2O . When rat lenses were first organ cultured, immunolabeling revealed an insertion of AQP5 into cortical fiber cells, and a significant increase in Hg 2+ -sensitive P H2O was detected in membrane vesicles. Our results show that AQP5 forms functional water channels in the rodent lens, and they suggest that dynamic membrane insertion of AQP5 may regulate water fluxes in the lens by modulating P H2O in the outer cortex.