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Providing uncertainties in satellite datasets used for Earth observation can be a daunting prospect because of the many processing stages and input data required to convert raw detector counts to calibrated radiances. The Sea and Land Surface Temperature Radiometer (SLSTR) was designed to provide measurements of the Earth’s surface for operational and climate applications. In this paper the authors describe the traceability chain and derivation of uncertainty estimates for the thermal infrared channel radiometry. Starting from the instrument model, the contributing input quantities are identified to build up an uncertainty effects tree. The characterisation of each input effect is described, and uncertainty estimates provided which are used to derive the combined uncertainties as a function of scene temperature. The SLSTR Level-1 data products provide uncertainty estimates for fully random effects (noise) and systematic effects that can be mapped for each image pixel, examples of which are shown.

The first two models of the Sea and Land Surface Temperature Radiometers (SLSTR) for the European Copernicus Sentinel-3 missions were tested prior to launch at the Rutherford Appleton Laboratory space instrument calibration facility. The pre-launch tests provide an essential reference that ensures that the flight data of SLSTR are calibrated to the same standards needed for surface temperature measurements and to those used by shipborne radiometers for Fiducial Reference Measurement (FRM). The radiometric calibrations of the thermal infrared channels were validated against accurate and traceable reference BB sources under flight representative thermal vacuum environment. Measurements were performed in both earth views for source temperatures covering the main operating range, for different instrument configurations and for the full field-of-view of the instruments. The data were used to derive non-linearity curves to be used in the level-1 processing. All results showed that the measured brightness temperatures and radiometric noise agreed within the requirements for the mission. An inconsistency that particularly affected SLSTR-A was observed which has been attributed to an internal stray light error. A correction for the stray light has been proposed to reduce the error. The internal stray light error was reduced for SLSTR-B by replacing the coating on the main aperture stop. We present a description of the test methodology and the key results.

The α7 nicotinic acetylcholine receptor (α7 nAChR) is involved in several cognitive and physiologic processes; its expression levels and patterns change in neurologic and psychiatric diseases, such as schizophrenia and Alzheimer’s disease, which makes it a relevant drug target. Development of selective radioligands is important for defining binding properties and occupancy of novel molecules targeting the receptor. We tested the in vitro binding properties of [125I]Iodo-ASEM [(3-(1,4-diazabycyclo[3.2.2]nonan-4-yl)-6-(125I-iododibenzo[b,d]thiopentene 5,5-dioxide)] in the mouse, rat and pig brain using autoradiography. The in vivo binding properties of [18F]ASEM were investigated using positron emission tomography (PET) in the pig brain. [125I]Iodo-ASEM showed specific and displaceable high affinity (~1 nM) binding in mouse, rat, and pig brain. Binding pattern overlapped with [125I]α-bungarotoxin, specific binding was absent in α7 nAChR gene-deficient mice and binding was blocked by a range of α7 nAChR orthosteric modulators in an affinity-dependent order in the pig brain. Interestingly, relative to the wild-type, binding in β2 nAChR gene-deficient mice was lower for [125I]Iodo-ASEM (58% ± 2.7%) than [125I]α-bungarotoxin (23% ± 0.2%), potentially indicating different binding properties to heteromeric α7β2 nAChR. [18F]ASEM PET in the pig showed high brain uptake and reversible tracer kinetics with a similar spatial distribution as previously reported for α7 nAChR. Blocking with SSR-180,711 resulted in a significant decrease in [18F]ASEM binding. Our findings indicate that [125I]Iodo-ASEM allows sensitive and selective imaging of α7 nAChR in vitro, with better signal-to-noise ratio than previous tracers. Preliminary data of [18F]ASEM in the pig brain demonstrated principal suitable kinetic properties for in vivo quantification of α7 nAChR, comparable to previously published data.

Changes in the expression of α7 nicotinic acetylcholine receptors (α7 nAChRs) in the human brain are widely assumed to be associated with neurological and neurooncological processes. Investigation of these receptors in vivo depends on the availability of imaging agents such as radioactively labelled ligands applicable in positron emission tomography (PET). We report on a series of new ligands for α7 nAChRs designed by the combination of dibenzothiophene dioxide as a novel hydrogen bond acceptor functionality with diazabicyclononane as an established cationic center. To assess the structure-activity relationship (SAR) of this new basic structure, we further modified the cationic center systematically by introduction of three different piperazine-based scaffolds. Based on in vitro binding affinity and selectivity, assessed by radioligand displacement studies at different rat and human nAChR subtypes and at the structurally related human 5-HT3 receptor, we selected the compound 7-(1,4-diazabicyclo[3.2.2]nonan-4-yl)-2-fluorodibenzo-[b,d]thiophene 5,5-dioxide (10a) for radiolabeling and further evaluation in vivo. Radiosynthesis of [18F]10a was optimized and transferred to an automated module. Dynamic PET imaging studies with [18F]10a in piglets and a monkey demonstrated high uptake of radioactivity in the brain, followed by washout and target-region specific accumulation under baseline conditions. Kinetic analysis of [18F]10a in pig was performed using a two-tissue compartment model with arterial-derived input function. Our initial evaluation revealed that the dibenzothiophene-based PET radioligand [18F]10a ([18F]DBT-10) has high potential to provide clinically relevant information about the expression and availability of α7 nAChR in the brain.