Biodiversity and ecosystem functioning: It is time for dispersal experiments

The experimental study of the relationship between biodiversity and ecosystem function has mainly addressed the effect of species and number of functional groups. In theory, this approach has mainly focused on how extinction affects function, whereas dispersal limitation of ecosystem function has been rarely discussed. A handful of seed introduction experiments, as well as numerous observations of the effects of long‐distance dispersal of alien species, indicate that ecosystem function may be strongly determined by dispersal limitation at the local, regional and/or global scales. We suggest that it is time to replace biodiversity manipulation experiments, based on random draw of species, with those addressing realistic scenarios of either extinction or dispersal. Experiments disentangling the dispersal limitation of ecosystem function should have to take into account the probability of arrival. The latter is defined as the probability that a propagule of a particular species will arrive at a particular community. Arrival probability depends on the dispersal ability and the number of propagules of a species, the distance a species needs to travel, and the permeability of the matrix landscape. Current databases, in particular those in northwestern and central Europe now enable robust estimation of arrival probability in plant communities. We suggest a general hypothesis claiming that dispersal limitation according to arrival probability will have ecosystem‐level effects different from those arising due to random arrival. This hypothesis may be rendered more region‐, landscape‐ or ecosystem‐specific by estimating arrival probabilities for different background conditions.     

Functional Effects of Adiponectin on Endothelial Progenitor Cells

Adiponectin is an adipokine whose plasma levels are inversely correlated to metabolic syndrome components. Adiponectin protects against atherosclerosis and decreases risks in myocardial infarction. Endothelial progenitor cells (EPCs) are a heterogeneous population of circulating cells involved in vascular repair and neovascularization. EPCs number is reduced in patients with cardiovascular disease. We hypothesize that the positive effects of adiponectin against atherosclerosis are explained in part by its interactions with EPCs. Cells were obtained from healthy volunteers' blood by mononuclear cell isolation and plating on collagen‐coated dishes. Three sub‐populations of EPCs were identified and characterized using flow cytometry. EPCs' expression of adiponectin receptors, AdipoR1, and AdipoR2 was evaluated by quantitative PCR. The effects of recombinant adiponectin on EPCs' susceptibility to apoptosis were assessed. Finally, expression of neutrophil elastase by EPCs and activity of this enzyme on adiponectin processing were assessed. Quantitative PCR analysis of EPCs mRNAs showed that AdipoR1 mRNA is expressed at higher levels than AdipoR2. Expression of AdipoR1 protein was confirmed by western blot. Adiponectin significantly increased survival of two sub‐populations of EPCs in conditions of serum deprivation. Such effect could not be demonstrated in the third EPCs sub‐population. We also demonstrated that EPCs, particularly one sub‐population, express neutrophil elastase. Neutrophil elastase activity was confirmed in EPCs' conditioned media. Adiponectin protects some EPCs sub‐populations against apoptosis and therefore could modulate EPCs ability to induce repair of vascular damage. Neutrophil elastase activity of EPCs could locally modulate adiponectin activity by its involvement in the generation of the globular form of adiponectin.     

LEFKOVITCH'S ERROR

Abstract — Lefkovitch's formula for the probability of incompatibility between two binary characters can give incorrect results because it redundantly counts some possible compatibilities. The inaccuracy occurs when the characters have the same number of terminals showing the apomorphic state.     

Induction of porphobilinogen oxygenase and porphobilinogen deaminase in rat blood under conditions of erythropoietic stress

Porphobilinogen is the substrate of two enzymes: porphobilinogen deaminase and porphobilinogen-oxygenase. The first one transforms it into the metabolic precursors of heme and the second diverts it from this metabolic pathway by oxidizing porphobilinogen to 5-oxopyrrolinones. Rat blood is devoid of porphobilinogen-oxygenase under normal conditions while it carries porphobilinogen-deaminase activity. When the rats were submitted to hypoxia (p_O2 = 0.42 atm) for 18 days, the activity of porphobilinogen-oxygenase appeared at the tenth day of hypoxia and reached the maximum at the 14–16th day. It decreased to a half after 2 days (half-life of the enzyme) and disappeared after 4 days of return to normal oxygen pressure. Porphobilinogen-deaminase activity increased after the first day of hypoxia, reached a maximum at the 14–16th day and did not decrease to normal values until the 15th day after return to normal oxygen pressure. The activities of both prophobilinogen-oxygenase and porphobilinogen-deaminase were induced by administration of erythropoietin. When rats were made anaemic with phenylhydrazine, porphobilinogen-oxygenase activity also appeared in the blood cells. Although the reticulocyte concentration was higher when compared to that obtained under hypoxia, the activities of the oxygenase obtained under both conditions were comparable. Porphobilinogen-deaminase activity was always closely related to the reticulocyte content. The appearance of porphobilinogen-oxygenase under the described erythropoietic conditions was due to a de novo induction of the enzyme, as shown by its inhibition with actinomycin D and cycloheximide. Porphobilinogen-oxygenase as well as porphobilinogen-deaminase were present in the rat bone marrow under normal conditions. Their activities increased in phenylhydrazine treated rats. The properties and kinetics of porphobilinogen-oxygenase from the rat blood and bone marrow were determined and found to differ in several aspects.     

Monitoring Primary Response to Chilling Stress in Etiolated Vigna radiata and V. mungo Seedlings Using Thermal Hysteresis of Water Proton NMR Relaxation Times

Thermal hysteresis of longitudinal relaxation times (T₁) ofwater protons in hypocotyls of etiolated Vigna radiata and V.mungo seedlings was investigated by pulse nuclear magnetic resonance(NMR) spectroscopy. Various lengths of chilling exposures duringa cool-warm cycle between 20 and 0?C (below 10?C, about 4 h)for the T₁ hysteresis measurement did not cause any visibleinjury symptoms in hypocotyls. However, the profiles of T₁ hysteresisvaried as a result of different chilling exposures. The sumsof the T₁ ratio (for detail see Introduction) reflecting T₁prolongation or shortening upon the warming process were a goodquantitative index for the extent of T₁ hysteresis, and thewide dispersion of this value ranging on the "minus" side (T₁prolongation upon warming) suggested the occurrence of a primaryresponse of cells to chilling stress before obvious visiblesymptoms occur while the T₁ ratio sums on the "plus" side (T₁shortening upon warming) corresponded to a response of seriousvisible injury. Therefore, the sums of the T₁ ratio can be usedas a non-destructive diagnostic tool for monitoring the primaryevent of chilling injury when lacking any visible injury symptoms.The data indicate that the critical temperature for the occurrenceof primary response for chilling stress was around 7.5?C forV. radiata and 12.5?C for V. mungo. (Received February 1, 1988; Accepted June 1, 1988)     

Characterization of 69- and 100-kDa forms of 2-5A-synthetase from interferon-treated human cells

The existence of distinct 69- and 100-kDa forms of 2-5A-synthetase in addition to the smaller (40 and 46 kDa) forms has recently been established. Using specific monoclonal antibodies we investigated the induction, synthesis, and activity of 69- and 100-kDa 2',5'-oligoadenylate (2-5A) synthetases in interferon-treated human Daudi cells. Although induction of these synthetases is detectable in cells treated with as little as 1-5 units/ml of human alpha-interferon, higher concentrations are required for maximum synthesis of the 100 kDa than the 69-kDa protein. At 5 units/ml of interferon, enhanced synthesis of both proteins is detectable at 4 h with maximum synthesis occurring between 8 to 12 and 12 to 16 h for 69- and 100-kDa 2-5A-synthetases, respectively. At 24 h after addition of interferon, synthesis of these synthetases declines due to a decrease of active interferon in the culture medium. The synthesis of both synthetases is blocked by actinomycin D, and the half-life of these proteins is estimated to be 8 h. The activities of immunoaffinity purified 69- and 100-kDa synthetases are dependent on double-stranded (ds)RNA but show different requirements for optimum concentration of dsRNA and pH of the reaction. The apparent Km of 69- and 100-kDa synthetases for ATP is 1.7 X 10(-3) M and 3.6 X 10(-3) M, respectively. At optimum conditions for the activity of these enzymes, the pattern of 2',5'-linked oligoadenylates synthesized are different, the 69-kDa protein synthesizing higher oligomers than the 100-kDa species. Taken together, these results indicate that the 69- and 100-kDa 2-5A-synthetases are distinct proteins each with specific characteristics of induction and enzymatic activity.     

Quantitative aspects of the uptake and degradation of lysozyme in the rat kidney in vivo

Uptake and degradation of lysozyme in the rat kidney were studied in vivo. The protein was labeled with 125I by way of a moiety (tyramine-cellobiose or 'TC') which remained trapped inside the cells even after proteolysis of the peptide chain (in contrast, the label from conventionally labeled proteins escapes after degradation). Following the injection of 'trapped-label' lysozyme, the radioactivity in the kidneys represented the total amount of lysozyme that was taken up during the experiment. Proteolysis could be followed by determining the amount of acid-soluble degradation products. By adding the radioactivity in the urine to that in the kidneys, a measure of the total filtered load was obtained. When only a trace dose of 125I-labeled TC lysozyme was injected into rats, the amount of radioactivity in the kidneys increased on average by 0.09% per min, after the concentration in the blood had become nearly stable. After 100 min, 30% of the injected dose was recovered in the kidneys. The labeled protein was degraded to acid-soluble molecules of Mr less than 1000. There was apparently a 'lag period' between the endocytosis in the kidneys and the start of degradation. 40 min after the injection of a trace dose, about 0.6% of the 'trapped-label' lysozyme in the kidneys was degraded per min.; subsequently, there was a decline in the fraction which was degraded per min. The amount of lysozyme in the urine increased after the injection of increasing amounts of lysozyme, showing that the capacity of the uptake mechanism was being exceeded, but truly saturating levels of lysozyme could not be reached in vivo.