Feasting, fasting and freezing: energetic effects of meal size and temperature on torpor expression by little brown bats Myotis lucifugus

Torpor is an adaptation for energy conservation employed by many species of small-bodied endotherms. However, surprisingly little is known regarding proximate factors influencing day-to-day variation in torpor expression in the wild. We used open-flow respirometry to quantify torpor expression in nine little brown bats (Myotis lucifugus, LeConte 1831) at two ambient temperatures (7°C and 17°C) following either sham feeding or consumption of a high-protein meal (50% or 100% of the mass required to reach satiation for each individual). Food consumption significantly increased the time spent normothermic before torpor entry but did not affect either the rate of body cooling or torpid metabolic rate. Bats did not fully exploit potential energy savings by maximising their use of torpor. Instead they varied torpor expression such that total energy expenditure over the course of each 22-h trial was balanced against gross energy intake immediately before the trial, independent of ambient temperature. This was accomplished by adjusting the timing of entry into torpor (thus altering the time spent torpid), rather than by modulating torpid metabolic rate. However, pre-trial body mass was also a significant predictor of torpor expression, which suggests that energy reserves combine with recent foraging success to influence individuals’ decisions about depth and duration of their torpor bouts. We also present evidence that little brown bats use the heat generated through digestion (i.e. the heat increment of feeding) to substitute for active thermogenesis at sub-thermoneutral temperatures, thereby reducing the energetic costs of thermoregulation prior to torpor entry."Funding was provided by Natural Sciences and Engineering Research Council (NSERC, Canada) Discovery grants to C.K.R.W. and K.L.C., and a NSERC Undergraduate Student Research Award to A.L.M. The University of Winnipeg Bat Lab and C.K.R.W. are also funded by the Canada Foundation for Innovation and the Manitoba Research and Innovation Fund."http://jeb.biologists.org/content/213/12/216

Cardiovascular disease risk factor responses to a type 2 diabetes care model including nutritional ketosis induced by sustained carbohydrate restriction at 1 year: An open label, non-randomized, controlled study

Additional file 1: Table S1. Detailed baseline characteristics for participants in the continuous care intervention (CCI) and usual care (UC) groups

An Early Look at a Time-Lapse 3D VSP

In 2007 Australian Cooperative Research Centre for Greenhouse Gas Technologies (CO2CRC) started a project to evaluate the available technology for monitoring the movement of CO2 in an underground reservoir. In stage one of this project CO2 and methane are being produced in a nearby well, then the CO2/CH4 is being injected back down a second well into a depleted gas sand. The movement of the CO2 up-dip needs to be remotely monitored. One of the technologies being evaluated to monitor the movement of the CO2 is 3D VSP. The CRC-1 injector well is instrumented with 10 3C downhole accelerometers. A baseline 3D VSP survey was shot around this well in late 2007 and was followed by a repeat survey in 2010. We hope to monitor the movement of CO2 around the CRC-1 well by observing changes in the time-lapse signature

The Globin Gene Repertoire of Lampreys: Convergent Evolution of Hemoglobin and Myoglobin in Jawed and Jawless Vertebrates

Agnathans (jawless vertebrates) occupy a key phylogenetic position for illuminating the evolution of vertebrate anatomy and physiology. Evaluation of the agnathan globin gene repertoire can thus aid efforts to reconstruct the origin and evolution of the globin genes of vertebrates, a superfamily that includes the well-known model proteins hemoglobin and myoglobin. Here, we report a comprehensive analysis of the genome of the sea lamprey (Petromyzon marinus) which revealed 23 intact globin genes and two hemoglobin pseudogenes. Analyses of the genome of the Arctic lamprey (Lethenteron camtschaticum) identified 18 full length and five partial globin gene sequences. The majority of the globin genes in both lamprey species correspond to the known agnathan hemoglobins. Both genomes harbor two copies of globin X, an ancient globin gene that has a broad phylogenetic distribution in the animal kingdom. Surprisingly, we found no evidence for an ortholog of neuroglobin in the lamprey genomes. Expression and phylogenetic analyses identified an ortholog of cytoglobin in the lampreys; in fact, our results indicate that cytoglobin is the only orthologous vertebrate-specific globin that has been retained in both gnathostomes and agnathans. Notably, we also found two globins that are highly expressed in the heart of P. marinus, thus representing functional myoglobins. Both genes have orthologs in L. camtschaticum. Phylogenetic analyses indicate that these heart-expressed globins are not orthologous to the myoglobins of jawed vertebrates (Gnathostomata), but originated independently within the agnathans. The agnathan myoglobin and hemoglobin proteins form a monophyletic group to the exclusion of functionally analogous myoglobins and hemoglobins of gnathostomes, indicating that specialized respiratory proteins for O2 transport in the blood and O2 storage in the striated muscles evolved independently in both lineages. This dual convergence of O2-transport and O2-storage proteins in agnathans and gnathostomes involved the convergent co-option of different precursor proteins in the ancestral globin repertoire of vertebrates

Thermal Imaging and Physiological Analysis of Cold-Climate Caribou-Skin Clothing

Protective clothing is essential for human existence in the Arctic, and caribou-skin clothing has played a pivotal role for millennia. Although people with northern experience often extol caribou-skin clothing, few scientific studies have investigated its properties. We used infrared thermal imaging in a pilot study to compare authentic caribou-skin clothing sewn by traditional Inuit seamstresses with two other types of cold-weather clothing: a standard-issue, Canadian army, winter uniform and an ensemble of modern retail clothing designed for extreme cold (a down anorak and snowmobile pants). To make the comparison, two subjects sequentially wore the three types of clothing—caribou skin, army uniform, and modern retail—in a still air, uniform thermal environment (where radiant temperatures of all environmental surfaces were equal to air temperature) at −21°C to −23°C (−6°F to −10°F). Thermal imaging quantifies the temperature of the outer surface of clothing, thereby providing key, functionally relevant information on the interface where clothing and environment meet. Under otherwise similar conditions, a low clothing surface temperature indicates superior clothing performance and a reduced rate of heat loss from the body to the environment. Caribou-skin clothing was similar to modern extreme-cold retail clothing: the whole-body composite surface temperature of our subjects wearing caribou-skin clothing was −22.1°C to −22.7°C, compared with −21.6°C in both subjects wearing the modern retail clothing. The army winter uniform (−18.9°C to −20.0°C) was inferior. These quantitative results were mirrored by the subjects’ subjective impressions. A particular advantage of thermal imaging is that it pinpoints locations in clothing where heat leaks occur. Although the two types of modern clothing exhibited heat leaks at zippered structures (even though fully closed), the caribou-skin clothing evaded such heat leaks by lacking such structures, because it is donned over the head. The integral hood characteristic of a caribou-skin parka was also superior in comparison to the detachable hood of the army uniform.Les vêtements de protection sont essentiels à l’existence humaine dans l’Arctique, et les vêtements en peau de caribou y jouent un rôle vital depuis des millénaires. Même si les gens qui ont évolué dans le Nord vantent souvent les mérites des vêtements en peau de caribou, peu d’études scientifiques ont été réalisées au sujet de leurs propriétés. Nous nous sommes servi d’imagerie thermique infrarouge dans le cadre d’une étude pilote visant à comparer les vêtements en peau de caribou authentique cousus par des couturières inuites traditionnelles à deux autres types de vêtements pour temps froid : un uniforme d’hiver standard de l’Armée canadienne et un ensemble de vêtements modernes du détail conçus pour des froids extrêmes (un anorak en duvet et des pantalons de motoneige). À des fins de comparaison, deux sujets ont porté, dans l’ordre séquentiel, les trois types de vêtements — vêtement en peau de caribou, uniforme de l’armée et vêtements modernes du détail — dans des conditions de vent nul thermique uniforme (où les températures radiatives de toutes les surfaces environnementales sont égales à la température de l’air) moyennant des températures allant de −21 °C à −23 °C (de −6 °F à −10 °F). L’imagerie thermique quantifie la température de la surface extérieure du vêtement, ce qui permet d’obtenir de l’information fonctionnellement pertinente et essentielle sur le point de rencontre du vêtement et de l’environnement. Dans des conditions par ailleurs semblables, la faible température du vêtement en surface indique un rendement supérieur pour ce vêtement et un taux réduit de perte de chaleur du corps à l’environnement. Les vêtements en peau de caribou ont donné des résultats semblables aux vêtements pour froid extrême modernes du détail : la température composite du corps entier de nos sujets portant les vêtements en peau de caribou variait de −22,1 °C à −22,7 °C, comparativement à −21,6 °C chez les deux sujets portant les vêtements modernes du détail. Les températures de l’uniforme d’hiver de l’armée étaient inférieures (de −18,9 °C à −20,0 °C). Ces résultats quantitatifs cadraient avec les impressions subjectives des sujets. Un des avantages particuliers de l’imagerie thermique, c’est qu’elle permet de repérer là où les pertes de chaleur se produisent dans les vêtements. Bien que les deux types de vêtements modernes perdaient de la chaleur à l’endroit des fermetures éclair (même si elles étaient fermées complètement), les vêtements en peau de caribou n’affichaient pas de telles pertes de chaleur en raison de l’absence de structures de ce genre parce que ces vêtements s’enfilent par la tête. Par ailleurs, il y a lieu de noter que la caractéristique intégrale du capuchon du parka en peau de caribou était également supérieure à celle du capuchon amovible de l’uniforme militaire

Monomerization of Far-Red Fluorescent Proteins

Anthozoa-class red fluorescent proteins (RFPs) are frequently used as biological markers, with far-red (λ_(em) ∼ 600–700 nm) emitting variants sought for whole-animal imaging because biological tissues are more permeable to light in this range. A barrier to the use of naturally occurring RFP variants as molecular markers is that all are tetrameric, which is not ideal for cell biological applications. Efforts to engineer monomeric RFPs have typically produced dimmer and blue-shifted variants because the chromophore is sensitive to small structural perturbations. In fact, despite much effort, only four native RFPs have been successfully monomerized, leaving the majority of RFP biodiversity untapped in biomarker development. Here we report the generation of monomeric variants of HcRed and mCardinal, both far-red dimers, and describe a comprehensive methodology for the monomerization of red-shifted oligomeric RFPs. Among the resultant variants is mKelly1 (emission maximum, λ_(em) = 656 nm), which, along with the recently reported mGarnet2 [Matela G, et al. (2017) Chem Commun (Camb) 53:979–982], forms a class of bright, monomeric, far-red FPs

Molecular basis of a novel adaptation to hypoxic-hypercapnia in a strictly fossorial mole

<p>Abstract</p> <p>Background</p> <p>Elevated blood O₂affinity enhances survival at low O₂pressures, and is perhaps the best known and most broadly accepted evolutionary adjustment of terrestrial vertebrates to environmental hypoxia. This phenotype arises by increasing the intrinsic O₂affinity of the hemoglobin (Hb) molecule, by decreasing the intracellular concentration of allosteric effectors (e.g., 2,3-diphosphoglycerate; DPG), or by suppressing the sensitivity of Hb to these physiological cofactors.</p> <p>Results</p> <p>Here we report that strictly fossorial eastern moles (<it>Scalopus aquaticus</it>) have evolved a low O₂affinity, DPG-insensitive Hb - contrary to expectations for a mammalian species that is adapted to the chronic hypoxia and hypercapnia of subterranean burrow systems. Molecular modelling indicates that this functional shift is principally attributable to a single charge altering amino acid substitution in the β-type δ-globin chain (δ136Gly→Glu) of this species that perturbs electrostatic interactions between the dimer subunits via formation of an intra-chain salt-bridge with δ82Lys. However, this replacement also abolishes key binding sites for the red blood cell effectors Cl^-, lactate and DPG (the latter of which is virtually absent from the red cells of this species) at δ82Lys, thereby markedly reducing competition for carbamate formation (CO₂binding) at the δ-chain N-termini.</p> <p>Conclusions</p> <p>We propose this Hb phenotype illustrates a novel mechanism for adaptively elevating the CO₂carrying capacity of eastern mole blood during burst tunnelling activities associated with subterranean habitation.</p

Molecular basis of a novel adaptation to hypoxic-hypercapnia in a strictly fossorial mole

Background: Elevated blood O2 affinity enhances survival at low O2 pressures, and is perhaps the best known and most broadly accepted evolutionary adjustment of terrestrial vertebrates to environmental hypoxia. This phenotype arises by increasing the intrinsic O2 affinity of the hemoglobin (Hb) molecule, by decreasing the intracellular concentration of allosteric effectors (e.g., 2,3-diphosphoglycerate; DPG), or by suppressing the sensitivity of Hb to these physiological cofactors. Results: Here we report that strictly fossorial eastern moles (Scalopus aquaticus) have evolved a low O2 affinity, DPG-insensitive Hb - contrary to expectations for a mammalian species that is adapted to the chronic hypoxia and hypercapnia of subterranean burrow systems. Molecular modelling indicates that this functional shift is principally attributable to a single charge altering amino acid substitution in the β-type δ-globin chain (δ136Gly→Glu) of this species that perturbs electrostatic interactions between the dimer subunits via formation of an intra-chain salt-bridge with δ82Lys. However, this replacement also abolishes key binding sites for the red blood cell effectors Cl-, lactate and DPG (the latter of which is virtually absent from the red cells of this species) at δ82Lys, thereby markedly reducing competition for carbamate formation (CO2 binding) at the δ-chain N-termini. Conclusions: We propose this Hb phenotype illustrates a novel mechanism for adaptively elevating the CO2 carrying capacity of eastern mole blood during burst tunnelling activities associated with subterranean habitation