Measuring Channel Planform Change From Image Time Series: A Generalizable, Spatially Distributed, Probabilistic Method for Quantifying Uncertainty

Abstract Channels change in response to natural or anthropogenic fluctuations in streamflow and/or sediment supply and measurements of channel change are critical to many river management applications. Whereas repeated field surveys are costly and time‐consuming, remote sensing can be used to detect channel change at multiple temporal and spatial scales. Repeat images have been widely used to measure long‐term channel change, but these measurements are only significant if the magnitude of change exceeds the uncertainty. Existing methods for characterizing uncertainty have two important limitations. First, while the use of a spatially variable image co‐registration error avoids the assumption that errors are spatially uniform, this type of error, as originally formulated, can only be applied to linear channel adjustments, which provide less information on channel change than polygons of erosion and deposition. Second, previous methods use a level‐of‐detection (LoD) threshold to remove non‐significant measurements, which is problematic because real changes that occurred but were smaller than the LoD threshold would be removed. In this study, we present a new method of quantifying uncertainty associated with channel change based on probabilistic, spatially varying estimates of co‐registration error and digitization uncertainty that obviates a LoD threshold. The spatially distributed probabilistic (SDP) method can be applied to both linear channel adjustments and polygons of erosion and deposition, making this the first uncertainty method generalizable to all metrics of channel change. Using a case study from the Yampa River, Colorado, we show that the SDP method reduced the magnitude of uncertainty and enabled us to detect smaller channel changes as significant. Additionally, the distributional information provided by the SDP method allowed us to report the magnitude of channel change with an appropriate level of confidence in cases where a simple LoD approach yielded an indeterminate result

Mapping the bathymetry of supraglacial lakes and streams on the Greenland Ice Sheet using field measurements and high resolution satellite images

Recent melt events on the Greenland ice sheet (GrIS) accentuate the need to constrain estimates of sea level rise through improved characterization of meltwater pathways. This effort will require more precise estimates of the volume of water stored on the surface of the GrIS. We assessed the potential to obtain such information by mapping the bathymetry of supraglacial lakes and streams from WorldView2 (WV2) satellite images. Simultaneous in situ observations of depth and reflectance from two streams and a lake with measured depths up to 10.45 m were used to test a spectrally based depth retrieval algorithm. We performed optimal band ratio analysis (OBRA) of continuous field spectra and spectra convolved to the bands of the WV2, Landsat 7 (ETM+), MODIS, and ASTER sensors. The field spectra yielded a strong relationship with depth (R² = 0.94), and OBRA R² values were nearly as high (0.87–0.92) for convolved spectra, suggesting that these sensors' broader bands would be sufficient for depth retrieval. Our field measurements thus indicated that remote sensing of supraglacial bathymetry is not only feasible but potentially highly accurate. OBRA of spectra from 2 m-pixel WV2 images acquired within 3–72 h of our field observations produced an optimal R² value of 0.92 and unbiased, precise depth estimates, with mean and root mean square errors < 1% and 10–25% of the mean depth. Bathymetric maps produced by applying OBRA relations revealed subtle features of lake and channel morphology. In addition to providing refined storage volume estimates for lakes of various sizes, this approach can help provide estimates of the transient flux of meltwater through stream

Point Mutations in Aβ Result in the Formation of Distinct Polymorphic Aggregates in the Presence of Lipid Bilayers

A hallmark of Alzheimer's disease (AD) is the rearrangement of the β-amyloid (Aβ) peptide to a non-native conformation that promotes the formation of toxic, nanoscale aggregates. Recent studies have pointed to the role of sample preparation in creating polymorphic fibrillar species. One of many potential pathways for Aβ toxicity may be modulation of lipid membrane function on cellular surfaces. There are several mutations clustered around the central hydrophobic core of Aβ near the α-secretase cleavage site (E22G Arctic mutation, E22K Italian mutation, D23N Iowa mutation, and A21G Flemish mutation). These point mutations are associated with hereditary diseases ranging from almost pure cerebral amyloid angiopathy (CAA) to typical Alzheimer's disease pathology with plaques and tangles. We investigated how these point mutations alter Aβ aggregation in the presence of supported lipid membranes comprised of total brain lipid extract. Brain lipid extract bilayers were used as a physiologically relevant model of a neuronal cell surface. Intact lipid bilayers were exposed to predominantly monomeric preparations of Wild Type or different mutant forms of Aβ, and atomic force microscopy was used to monitor aggregate formation and morphology as well as bilayer integrity over a 12 hour period. The goal of this study was to determine how point mutations in Aβ, which alter peptide charge and hydrophobic character, influence interactions between Aβ and the lipid surface. While fibril morphology did not appear to be significantly altered when mutants were prepped similarly and incubated under free solution conditions, aggregation in the lipid membranes resulted in a variety of polymorphic aggregates in a mutation dependent manner. The mutant peptides also had a variable ability to disrupt bilayer integrity

Corn Tiller Yield Contributions are Dependent on Environment: A 17 Site-Year Kansas Study

Historic breeding efforts in corn (Zea mays L.) have resulted in uniform, single-stalked phenotypes with limited potential for environmental plasticity. Therefore, plant density is a critical yield component for corn, as corn is unable to successfully compensate for a deficit of plants. Other grass crop species can overcome plant density deficits via vegetative branching (tillering), but this trait is historically undesirable in corn. Improving corn flexibility across plant densities has potential benefits, particularly considering diverse yield environments and seasonal weather uncertainties due to climate change. The present study evaluated tiller presence with two hybrids in a range of plant densities across the state of Kansas to identify yield impacts and potential usefulness of this plasticity trait in corn. Tiller presence was identified as neutral or additive to final yields, but fine-tuning plant density was confirmed as key to maximizing grain yields. Tillers have potential to stabilize yields across plant densities in productive environments. This capability may offer a source of production stability for growers when deficits develop in plant density after planting

A Major Role for Side-Chain Polyglutamine Hydrogen Bonding in Irreversible Ataxin-3 Aggregation

The protein ataxin-3 consists of an N-terminal globular Josephin domain (JD) and an unstructured C-terminal region containing a stretch of consecutive glutamines that triggers the neurodegenerative disorder spinocerebellar ataxia type 3, when it is expanded beyond a critical threshold. The disease results from misfolding and aggregation, although the pathway and structure of the aggregation intermediates are not fully understood. In order to provide insight into the mechanism of the process, we monitored the aggregation of a normal (AT3Q24) ataxin-3, an expanded (AT3Q55) ataxin-3, and the JD in isolation. We observed that all of them aggregated, although the latter did so at a much slower rate. Furthermore, the expanded AT3Q55 displayed a substantially different behavior with respect to the two other variants in that at the latest stages of the process it was the only one that did the following: i) lost its reactivity towards an anti-oligomer antibody, ii) generated SDS-insoluble aggregates, iii) gave rise to bundles of elongated fibrils, and iv) displayed two additional bands at 1604 and 1656 cm−1 in FTIR spectroscopy. Although these were previously observed in other aggregated polyglutamine proteins, no one has assigned them unambiguously, yet. By H/D exchange experiments we show for the first time that they can be ascribed to glutamine side-chain hydrogen bonding, which is therefore the hallmark of irreversibly SDS-insoluble aggregated protein. FTIR spectra also showed that main-chain intermolecular hydrogen bonding preceded that of glutamine side-chains, which suggests that the former favors the latter by reorganizing backbone geometry

A Major Role for Side-Chain Polyglutamine Hydrogen Bonding in Irreversible Ataxin-3 Aggregation

The protein ataxin-3 consists of an N-terminal globular Josephin domain (JD) and an unstructured C-terminal region containing a stretch of consecutive glutamines that triggers the neurodegenerative disorder spinocerebellar ataxia type 3, when it is expanded beyond a critical threshold. The disease results from misfolding and aggregation, although the pathway and structure of the aggregation intermediates are not fully understood. In order to provide insight into the mechanism of the process, we monitored the aggregation of a normal (AT3Q24) ataxin-3, an expanded (AT3Q55) ataxin-3, and the JD in isolation. We observed that all of them aggregated, although the latter did so at a much slower rate. Furthermore, the expanded AT3Q55 displayed a substantially different behavior with respect to the two other variants in that at the latest stages of the process it was the only one that did the following: i) lost its reactivity towards an anti-oligomer antibody, ii) generated SDS-insoluble aggregates, iii) gave rise to bundles of elongated fibrils, and iv) displayed two additional bands at 1604 and 1656 cm−1 in FTIR spectroscopy. Although these were previously observed in other aggregated polyglutamine proteins, no one has assigned them unambiguously, yet. By H/D exchange experiments we show for the first time that they can be ascribed to glutamine side-chain hydrogen bonding, which is therefore the hallmark of irreversibly SDS-insoluble aggregated protein. FTIR spectra also showed that main-chain intermolecular hydrogen bonding preceded that of glutamine side-chains, which suggests that the former favors the latter by reorganizing backbone geometry

Formation and Toxicity of Soluble Polyglutamine Oligomers in Living Cells

Aggregation and cytotoxicity of mutant proteins containing an expanded number of polyglutamine (polyQ) repeats is a hallmark of several diseases, including Huntington's disease (HD). Within cells, mutant Huntingtin (mHtt) and other polyglutamine expansion mutant proteins exist as monomers, soluble oligomers, and insoluble inclusion bodies (IBs). Determining which of these forms constitute a toxic species has proven difficult. Recent studies support a role for IBs as a cellular coping mechanism to sequester levels of potentially toxic soluble monomeric and oligomeric species of mHtt.When fused to a fluorescent reporter (GFP) and expressed in cells, the soluble monomeric and oligomeric polyglutamine species are visually indistinguishable. Here, we describe two complementary biophysical fluorescence microscopy techniques to directly detect soluble polyglutamine oligomers (using Htt exon 1 or Htt(ex1)) and monitor their fates in live cells. Photobleaching analyses revealed a significant reduction in the mobilities of mHtt(ex1) variants consistent with their incorporation into soluble microcomplexes. Similarly, when fused to split-GFP constructs, both wildtype and mHtt(ex1) formed oligomers, as evidenced by the formation of a fluorescent reporter. Only the mHtt(ex1) split-GFP oligomers assembled into IBs. Both FRAP and split-GFP approaches confirmed the ability of mHtt(ex1) to bind and incorporate wildtype Htt into soluble oligomers. We exploited the irreversible binding of split-GFP fragments to forcibly increase levels of soluble oligomeric mHtt(ex1). A corresponding increase in the rate of IBs formation and the number formed was observed. Importantly, higher levels of soluble mHtt(ex1) oligomers significantly correlated with increased mutant cytotoxicity, independent of the presence of IBs.Our study describes powerful and sensitive tools for investigating soluble oligomeric forms of expanded polyglutamine proteins, and their impact on cell viability. Moreover, these methods should be applicable for the detection of soluble oligomers of a wide variety of aggregation prone proteins

Sediment supply as a driver of river meandering and floodplain evolution in the Amazon Basin

The role of externally imposed sediment supplies on the evolution of meandering rivers and their floodplains is poorly understood, despite analytical advances in our physical understanding of river meandering. The Amazon river basin hosts tributaries that are largely unaffected by engineering controls and hold a range of sediment loads, allowing us to explore the influence that sediment supply has on river evolution. Here we calculate average annual rates of meander migration within 20 reaches in the Amazon Basin from Landsat imagery spanning 1985-2013. We find that rivers with high sediment loads experience annual migration rates that are higher than those of rivers with lower sediment loads. Meander cutoff also occurs more frequently along rivers with higher sediment loads. Differences in meander migration and cutoff rates between the study reaches are not explained by differences in channel slope or river discharge. Because faster meander migration and higher cutoff rates lead to increased sediment-storage space in the resulting oxbows, we suggest that sediment supply modulates the reshaping of floodplain environments by meandering rivers. We conclude that imposed sediment loads influence planform changes in lowland rivers across the Amazon