Death from drought in tropical forests is triggered by hydraulics not carbon starvation.

Drought threatens tropical rainforests over seasonal to decadal timescales, but the drivers of tree mortality following drought remain poorly understood. It has been suggested that reduced availability of non-structural carbohydrates (NSC) critically increases mortality risk through insufficient carbon supply to metabolism ('carbon starvation'). However, little is known about how NSC stores are affected by drought, especially over the long term, and whether they are more important than hydraulic processes in determining drought-induced mortality. Using data from the world's longest-running experimental drought study in tropical rainforest (in the Brazilian Amazon), we test whether carbon starvation or deterioration of the water-conducting pathways from soil to leaf trigger tree mortality. Biomass loss from mortality in the experimentally droughted forest increased substantially after >10 years of reduced soil moisture availability. The mortality signal was dominated by the death of large trees, which were at a much greater risk of hydraulic deterioration than smaller trees. However, we find no evidence that the droughted trees suffered carbon starvation, as their NSC concentrations were similar to those of non-droughted trees, and growth rates did not decline in either living or dying trees. Our results indicate that hydraulics, rather than carbon starvation, triggers tree death from drought in tropical rainforest.

Drought sensitivity of Amazonian carbon balance revealed by atmospheric measurements.

Feedbacks between land carbon pools and climate provide one of the largest sources of uncertainty in our predictions of global climate. Estimates of the sensitivity of the terrestrial carbon budget to climate anomalies in the tropics and the identification of the mechanisms responsible for feedback effects remain uncertain. The Amazon basin stores a vast amount of carbon, and has experienced increasingly higher temperatures and more frequent floods and droughts over the past two decades. Here we report seasonal and annual carbon balances across the Amazon basin, based on carbon dioxide and carbon monoxide measurements for the anomalously dry and wet years 2010 and 2011, respectively. We find that the Amazon basin lost 0.48 ± 0.18 petagrams of carbon per year (Pg C yr(-1)) during the dry year but was carbon neutral (0.06 ± 0.1 Pg C yr(-1)) during the wet year. Taking into account carbon losses from fire by using carbon monoxide measurements, we derived the basin net biome exchange (that is, the carbon flux between the non-burned forest and the atmosphere) revealing that during the dry year, vegetation was carbon neutral. During the wet year, vegetation was a net carbon sink of 0.25 ± 0.14 Pg C yr(-1), which is roughly consistent with the mean long-term intact-forest biomass sink of 0.39 ± 0.10 Pg C yr(-1) previously estimated from forest censuses. Observations from Amazonian forest plots suggest the suppression of photosynthesis during drought as the primary cause for the 2010 sink neutralization. Overall, our results suggest that moisture has an important role in determining the Amazonian carbon balance. If the recent trend of increasing precipitation extremes persists, the Amazon may become an increasing carbon source as a result of both emissions from fires and the suppression of net biome exchange by drought.

The sensitivity of wood production to seasonal and interannual variations in climate in a lowland Amazonian rainforest.

Understanding climatic controls on tropical forest productivity is key to developing more reliable models for predicting how tropical biomes may respond to climate change. Currently there is no consensus on which factors control seasonal changes in tropical forest tree growth. This study reports the first comprehensive plot-level description of the seasonality of growth in a Peruvian tropical forest. We test whether seasonal and interannual variations in climate are correlated with changes in biomass increment, and whether such relationships differ among trees with different functional traits. We found that biomass increments, measured every 3 months on the two plots, were reduced by between 40 and 55% in the peak dry season (July-September) relative to peak wet season (January-March). The seasonal patterns of biomass accumulation are significantly (p < 0.01) associated with seasonal patterns of rainfall and soil water content; however, this may reflect a synchrony of seasonal cycles rather than direct physiological controls on tree growth rates. The strength of the growth seasonality response among trees is significantly correlated to functional traits: consistent with a hypothesised trade-off between maximum potential growth rate and hydraulic safety, tall and fast-growing trees with broad stems had the most strongly seasonal biomass accumulation, suggesting that they are more productive in the wet season, but more vulnerable to water limitation in the dry season.

Incorporating health equity in the neurology curriculum: Our experience.

BACKGROUND: Social determinants of health (SDoH) are responsible for 80-90% of modifiable contributors to health, yet this material may not be covered in preclinical medical school neuroscience courses. OBJECTIVE: To describe how topics related to SDoH and inclusion, diversity, equity, anti-racism, and social justice (IDEAS) were incorporated into a preclinical neuroscience course. METHODS: IDEAS concepts and guided discussions were added to our existing case-based curriculum, and guest speakers were invited to discuss how these concepts are relevant in the field of neurology. RESULTS: Most students felt that content and discussions were integrated thoughtfully. Students also found it helpful to learn and observe how faculty address these topics in real-world cases. CONCLUSION: The additional content related to SDoH and IDEAS is feasible. Faculty with or without expertise in IDEAS concepts were able to utilize these cases and generate discussion without detracting from the neuroscience course material.

Isolation and characterization of aldose reductase from calf brain.

Aldose reductase activity (alditol: NADP+ 1-oxidoreductase, EC 1.1.1.21) from calf brain was separated into two protein fractions by DEAE chromatography. Further purifcation by molecular sieve chromotography and electrofocusing yielding two distinctive enzymes, which were designated AR I and AR II. AR I was purified 646-fold and found to have an isoelectric point of 6.18. AR I was most active as a monomer with a molecular weight of 29 000 and appeared to be in equilibrium with a less active dimer. AR II was purified 425-fold and found to have an isoelectric point of 4.88. The molecular weight of this enzyme was 30 000. Although both enzymes had specificity for aldoses as substrates, AR I had two to three times larger turnover numbers with aromatic aldehydes and hexonates than did AR II. AR I was activated by sulfhydryl compounds and exhibited biphasic double reciprocal plots. AR I was more sensitive to inhibition by high substrate and phenobarbital concentrations than was AR II. AR I and AR II did not have antigenic similarity as tested by Ouchterlony immunodiffusion and counter immunoelectrophoresis. An immunochemical cross-reaction was observed between AR II and lens aldose reductase.

Comparative studies on aldose reductase from bovine, rat and human lens.

A purification scheme for aldose reductase (alditol: NADP+ 1-oxidoreductase, EC 1.1.1.21) developed using bovine lens tissue including an affinity chromatographic step is presented which is particularly suited for small quantities of lenses. Using the affinity chromatographic method as a key step also makes it possible to obtain preparations of rat lens aldose reductase which are homogeneous. The behavior of crude preparations of aldose reductase from human lens on both ion-exchange and affinity chromatography was similar to the chromatographic behavior of the enzyme from rat and bovine lens. Comparative studies of aldose reductase obtained from the lenses of the three species demonstrate the similarity of the enzymes. These comparisons were based on molecular weights, isoelectric points, chromatographic behavior and kinetic data. Homotropic cooperativity for both NADPH and glyceraldehyde, as evidenced by a downward curvature in the Lineweaver-Burk double-reciprocal plots, had been demonstrated for aldose reductase obtained from bovine lens (Sheaff, C.M. and Doughty, C.C. (1976) J. Biol. Chem. 251, 2696-2702). Similarly, cooperativity was observed with the enzyme from both rat and human lenses and the apparent Km values at both high and low concentrations of substrate are comparable for the lens aldose reductases from all three species for both substrates.

A reaction mechanism for aldose reductase from lens.

Sheys and Doughty, (Sheys, G.H. and Doughty, C.C. (1979) Biochim. Biophys. Acta 242, 523-531) suggested a model for Rhodotorula (yeast) aldose reductase (alditol:NADP+ 1-oxidoreductase, EC 1.1.1.21) which offered a unified explanation for changes in reversibility, reaction mechanism, and effects of multivalent anions as well as substrate activation. The present paper extends this model to lens aldose reductase, explaining its similarities to the reverse reaction in Rhodotorula in regard to its reaction mechanism, as well as multivalent anion effects of sulfate, pyrophosphate and NADPH (above 20 micro M) and also substrate activation with glyceraldehyde involving formation of an abortive complex (above 50 micro M). Activation of lens aldose reductase resulted with multivalent anions, due to increased V max and apparent Km values with increasing concentration of multivalent anions. The lens enzyme mechanism is similar to the reverse reaction mechanism for the Rhodotorula enzyme, being partially random in character, based on NADP+ inhibitor studies presented here. The binding of NADPH appears to occur at a basic center containing arginine and possibly histidine. Evidence of the participation of these residues at the active center is based on time-course inactivation protection studies using reagents specific for these residues.

Aldose reductase, NADPH and NADP+ in normal, galactose-fed and diabetic rat lens.

NADPH and NADP+ levels were measured in rat lens from normal controls, from galactose-fed and diabetic rats during the first week of cataract formation. The level of NADPH in normal rat lens was determined to be 12.3 +/- 0.4 nmol/g wet weight, and that of NADP+ 4.6 +/- 0.2 nmol/g wet weight. In early cataract formation NADPH levels decreased rapidly during the first 2 days and then remained stable at 76% of control for galactose-fed and 84% for diabetic rats. NADP+ levels increased by 38% of control for galactose-fed and 54% for diabetic rats. Calculated NADPH/NADP+ ratios dropped from 3.36 +/- 0.21 to 1.86 +/- 0.16 in galactose fed rats, and from 2.81 +/- 0.15 to 1.61 +/- 0.16 in diabetic rats (P less than 0.001 for both experimental groups). These data are consistent with rapid NADPH oxidation during onset of lens cataracts. No significant changes in aldose reductase enzymatic activity levels were observed in either the galactosemic or the diabetic rats during the times measured.

Effects of oestradiol-17beta, oestradiol benzoate and the synthetic oestrogen RU 2858 on sexual differentiation in the neonatal female rat.

Groups of neonatal female rats were treated for the first 5 days of life with oestradiol-17beta, oestradiol benzoate or a synthetic oestrogen, 11beta-methoxy-17-ethynyl-1,3,5(10)-oestratriene-3,17beta-diol (RU 2858), in daily doses ranging from 0-5 to 1000 ng. Oestradiol-17beta had no effect on adult ovarian cyclicity or sexual receptivity after ovariectomy and oestrogen+ progesterone treatment. Ovarian cyclicity was prevented by 100 ng or more oestradiol benzoate/day, and by all doses of RU 2858. Only rats receiving 50 ng oestradiol benzoate/day or 0-5 ng RU 2858/day showed normal receptivity. The defeminizing action of RU 2858 was at least 100 times greater than that of oestradiol benzoate; it is suggested that this greater potency is due to the low affinity of RU 2858 for the oestradiol-binding protein in the plasma of neonatal rats. These results indicate that defeminization of the neonatal rat brain can be induced by physiological amounts of oestrogen, and are discussed with reference to the action of testosterone.