Rabbit Anti-Human MREG (a.a. 1-214) Polyclonal antibody

Purpose: To improve the reconstruction efficiency (i.e., computational load) and stability of iterative reconstruction for non-Cartesian fMRI when using high undersampling rates and/or in the presence of strong off-resonance effects. Theory and Methods: The magnetic resonance encephalography (MREG) sequence with 3D non-Cartesian trajectory and 0.1s repetition time (TR) was applied to acquire fMRI datasets. Different from a conventional time-point-by-time-point sequential reconstruction (SR), the proposed time-domain principal component reconstruction (tPCR) performs three steps: (1) decomposing the k-t-space fMRI datasets into time-domain principal component space using singular value decomposition, (2) reconstructing each principal component with redistributed computation power according to their weights, and (3) combining the reconstructed principal components back to image-t-space. The comparison of reconstruction accuracy was performed by simulation experiments and then verified in real fMRI data. Results: The simulation experiments showed that the proposed tPCR was able to significantly reduce reconstruction errors, and subsequent functional activation errors, relative to SR at identical computational cost. Alternatively, at fixed reconstruction accuracy, computation time was greatly reduced. The improved performance was particularly obvious for L1-norm nonlinear reconstructions relative to L2-norm linear reconstructions and robust to different regularization strength, undersampling rates, and off-resonance effects intensity. By examining activation maps, tPCR was also found to give similar improvements in real fMRI experiments. Conclusion: The proposed proof-of-concept tPCR framework could improve (1) the reconstruction efficiency of iterative reconstruction, and (2) the reconstruction stability especially for nonlinear reconstructions. As a practical consideration, the improved reconstruction speed promotes the application of highly undersampled non-Cartesian fast fMRI.

Porphyromonas gingivalis often subverts host cell autophagic processes for its own survival. Our previous studies document the association of the cargo sorting protein, melanoregulin (MREG), with its binding partner, the autophagic protein, microtubule-associated protein 1 light chain 3 (LC3) in macrophages incubated with P.gingivalis (strain 33277). Differences in the lipid A moiety of lipopolysaccharide (LPS) affect the virulence of P.gingivalis; penta-acylated LPS1690 is a weak Toll-like receptor 4 agonist compared with Escherichia coli LPS, whereas tetra-acylated LPS1435/1449 acts as an LPS1690 antagonist. To determine how P.gingivalis LPS1690 affects autophagy we assessed LC3-dependent and MREG-dependent processes in green fluorescent protein (GFP)-LC3-expressing Saos-2 cells. LPS1690 stimulated the formation of very large LC3-positive vacuoles and MREG puncta. This LPS1690-mediated LC3 lipidation decreased in the presence of LPS1435/1449. When Saos-2 cells were incubated with P.gingivalis the bacteria internalized but did not traffic to GFP-LC3-positive structures. Nevertheless, increases in LC3 lipidation and MREG puncta were observed. Collectively, these results suggest that P.gingivalis internalization is not necessary for LC3 lipidation. Primary human gingival epithelial cells isolated from patients with periodontitis showed both LC3II and MREG puncta whereas cells from disease-free individuals exhibited little co-localization of these two proteins. These results suggest that the prevalence of a particular LPS moiety may modulate the degradative capacity of host cells, so influencing bacterial survival.