BackgroundThe right ventricle (RV) is not designed to sustain high pressure leading to failure. There are no current medications to help RV contraction, so further information is required on adaption of the RV to such hypertension.MethodsThe Right Ventricle in Children (RVENCH) study assessed infants with congenital heart disease undergoing cardiac surgery with hypertensive RV. Clinical and echocardiographic data were recorded, and samples of RV were taken from matched infants, analysed for proteomics and compared between pathologies and with clinical and echocardiographic outcome data.ResultsThose with tetralogy of Fallot (TOF) were significantly more cyanosed than those with ventricular septal defect (median oxygen saturation 83% vs 98%, P=0.0038), had significantly stiffer RV (tricuspid E wave/A wave ratio 1.95 vs 0.84, P=0.009) and had most had restrictive physiology. Gene ontology in TOF, with enrichment analysis, demonstrated significant increase in proteins of contractile mechanisms and those of calmodulin, actin binding and others associated with contractility than inventricular septal defect. Structural proteins were also found to be higher in association with sarcomeric function: Z-disc, M-Band and thin-filament proteins. Remaining proteins associated with actin binding, calcium signalling and myocyte cytoskeletal development. Phosphopeptide enrichment led to higher levels of calcium signalling proteins in TOF.ConclusionThis is the first demonstration that those with an RV, which is stiff and hypertensive in TOF, have a range of altered proteins, often in calcium signalling pathways. Information about these alterations might guide treatment options both in terms of individualised therapy or inotropic support for the Right ventricle when hypertensive due to pulmoanry hypertension or congenital heart disease.
The motility of bovine and ovine spermatozoa has been studied under aerobic and anaerobic conditions, using a dual beam laser velocimeter. Cells swimming under aerobic conditions were found to be characterized by a translational swimming speed and a rotation rate that were approximately double those of cells swimming in an anaerobic environment. Both types of spermatozoa have been found to exhibit a sudden coordinated transition between fast and slow swimming states when the available oxygen is exhausted. This transition from aerobic to anaerobic swimming states has also been shown to be reversible. Studies of the duration of aerobic motility using the same apparatus have shown that the cells have a constant motile efficiency over the temperature range 32 degrees-42 degrees C.
Previous laser light-scattering studies of spermatozoon motility have been hampered by the large, asymmetric shape of spermatozoa, which causes difficulties in the interpretation of intensity fluctuations in the light scattered from a single laser beam. This paper describes an experimental arrangement for measuring the distribution of transit times for swimming spermatozoa using two slightly separated, focused laser beams. The theory of operation of the instrument is developed to enable the analysis of the experimentally obtained cross-correlation functions. The effects of the pronounced spermatozoon asymmetry and associated intensity modulation in the scattered light are also investigated and shown to be negligible for the twin beam experimental arrangement, provided that the swimming speed distribution has a coefficient of variation (sigma/upsilon greater than 0.1. Results obtained using this apparatus are presented for the velocity distribution of spermatozoa from a variety of bulls.
Tethered bilayers are formed on solid supports by the interaction of lipid vesicles with mixed self-assembled monolayers (SAMs). The mixed monolayer assembles on a gold support in a solution of hydrophilic and hydrophobic thiols producing an amphipathic surface of the two components. The hydrophobic molecules are composed of an ethoxythiol tether and a cholesterol head group. Lipid vesicles spontaneously unroll on the mixed surface forming a tethered bilayer ; the hydrophobic head group anchoring it to the support and the hydrophilic spacer molecule maintaining a water layer underneath. In this poster, monolayers of different molecular compositions are characterised in terms of the physical, kinetic and electrical properties of the bilayer. SAMs with different cholesterol content, ethoxythiol tether length and phospholipid head groups are shown. The tethered bilayer system is used to study rhodopsin photoactivation. Activation of rhodopsin causes the protein, transducin, to leave the membrane. Rhodopsin-containing membranes are isolated from retinal tissue, and used to form a tethered bilayer in the dark. A flash of light activates the protein, causing the exit of transducin from the membrane, which can be observed by surface plasmon resonance, demonstrating the extent to which a tethered bilayer resembles a biological membrane. 52 Confirmation of the interaction between the monocarboxylate transporter MCTl and its ancillary protein CD147 using fluorescence resonance energy transferWe have shown previously that the monocarboxylate transporter (MCT1) is tightly associated with the monotopic membrane glycoprotein CD147. This protein is required for the proper expression of both MCTl and MCT4 at the plasma membrane.Here we describe the expression in COS cells of constructs of MCTl and CD147 in which cyan-and yellow-fluorescent protein (CFP and YFP respectively) have been attached to either the Cor N-terminal ends of both proteins. These constructs, like the native proteins, were properly targeted to the plasma membrane only when co-expressed and then enhanced lactic acid transport into the cells 3-4 fold. Fluorescence energy transfer (FRET) between the two proteins was strong only when both fluorophores were present on the cytosolic face of the proteins. A range of controls including photobleaching experiments were used to confirm that the FRET signal was not due to either excitation of the YFP by the CFP excitation light or by overcrowding. 53The genomic structure of the human lactate transporters
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