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Alison M Campbell

Publications and source records attributed to Alison M Campbell.

5 recordsLinked to original sources

Comparison of multislice and single-slice acquisitions for pulsed arterial spin labeling measurements of cerebral perfusion.

Multislice Q2TIPS is a widely used pulsed arterial spin labeling (PASL) technique for efficient and accurate quantification of cerebral blood flow (CBF). Slices are typically acquired inferior to superior from a tagging plane. Superior slices show signal loss greater than the loss expected from blood T1 decay. In order to assess the reasons for this additional signal loss, three single-slice acquisition studies were compared to multislice acquisition (six slices) in healthy volunteers. In Study 1 (n=8), the tagging plane was fixed in location, and the inversion time (TI2) was 1500 ms for each slice. For Study 2 (n=12), the tagging plane was fixed as in Study 1; however, TI2 increased as slices were acquired further from the tagging plane. In Study 3 (n=9), the tagging plane was kept adjacent to the imaging slice, and TI2 was 1500 ms for every slice. Gray matter (GM) and white matter (WM) signal-to-noise ratio (SNR) and CBF were measured per slice. GM SNR from single-slice acquisitions was significantly higher at slices 4-6 in Study 2 and at slices 2-6 in Study 3 compared to multislice acquisitions. Signal loss in distal slices of multislice acquisitions can be attributed to the destruction of tagged bolus in addition to blood T1 decay. If limited brain coverage is acceptable, perfusion images with greater SNR are achievable with limited slices and placement of the tagging region immediately adjacent to the site of interest.

Adult↗

Pulsed arterial spin labeling parameter optimization for an elderly population.

PURPOSE: To optimize pulsed arterial spin labeling (PASL) parameters for the elderly to take into account possible perfusion changes that occur in the brain with age. MATERIALS AND METHODS: Healthy young (N = 14, age range = 21-27 years) and elderly (N = 12, age range = 61-67 years) subjects were scanned using Q2TIPS (QUIPSS II with thin-slice TI, periodic saturation) with varying inversion times (TI(2)) at 1.5T. The difference signal (DeltaM), transit time (deltat), and cerebral blood flow (CBF) were calculated in segmented gray matter (GM). RESULTS: The young displayed more perfusion-weighted signal difference than the elderly at all TI(2)'s. The peak DeltaM occurred at TI(2) approximately 1300 msec and 1500 msec in the young and elderly groups, respectively. Qualitatively, intravascular signal was minimal in the younger group by TI(2) = 1500 msec, whereas a longer TI(2) of 1800 msec was needed to minimize this signal in the elderly. The transit time was approximately 100 msec longer in the elderly, and CBF was in the range of literature values. CONCLUSION: For acquiring perfusion-weighted images with minimal intravascular signal and adequate tissue signal for PASL studies of cerebral perfusion in the elderly, a longer inversion time is advantageous.

Adult↗

Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.

The crystal structure of GST Nu2-2 (HpolGSTN2-2) from the model hookworm nematode Heligmosomoides polygyrus has been solved by the molecular replacement method and refined to a resolution of 1.71 A, providing the first structural data from a class of nematode-specific GSTs. By structural alignment with two Sigma class GSTs, glutathione could be rationally docked into the G-site of the enzyme. By comparing with all mammalian GST classes, a novel, long, and deep cleft was identified at the H-site, providing a potential site for ligand binding. This new GST class may support the establishment of infection parasitic nematodes by passively neutralizing chemical toxins derived from host environment. The structure serves as a starting point for structure-based drug/inhibitor design that would aim to selectively disrupt nematode chemical defenses.

Animals↗

Evidence of glutathione transferase complexing and signaling in the model nematode Caenorhabditis elegans using a pull-down proteomic assay.

Phage display techniques using random peptide interactions have supported the role of mammalian glutathione transferase (GST) as part of a signalling pathway for both oxidative stress and an apoptosis pathway. Little is known about the interaction of nonmammalian GST with other proteins. GSTs have been implicated in the development of chronic nematode infections by neutralising cytotoxic products arising from host immune initiated reactive oxygen species (ROS) assault. In this study we attached one of the key GSTs expressed in the model nematode Caenorhabditis elegans to an affinity support matrix and directly identified major interacting proteins by two-dimensional electrophoresis and peptide mass fingerprinting before and following oxidative stress. Nematode GST does not appear to be a stand-alone enzyme and interacts with many types of proteins in both normal and ROS stress conditions. Pull-down proteomic presents a flexible, label free, rapid and economical assay without specialised ligand fishing equipment to identify protein binding partners.

Amino Acid Sequence↗