Ultrasound inflammation imaging in rats with myocardial ischemia-reperfusion: Evaluation by non-specific targeted contrast microbubbles

Background: Reports on ultrasound inflammation imaging with non-specific targeted microbubbles in the heart have been scarce. We investigated whether inflammation induced by myocardial ischemia-reperfusion in rats could be evaluated by ultrasound inflammation imaging with non-specific targeted microbubbles. Methods: Six rats subjected to 30 min of occlusion of the left anterior descending artery (LAD) followed by 4 h of reperfusion (ischemia group) and 4 rats subjected to the sham operation (sham group) were used. Ultrasound inflammation imaging was performed 4 h after reperfusion, and non-circulating signal intensity (SI), which reflects the signal derived from microbubbles phagocytosed by neutrophils in inflamed tissue, was calculated by the SI difference between the initial and subsequent imaging both in the LAD and non-LAD areas. The accumulation of neutrophils was confirmed by myeloperoxidase (MPO) staining. Results: Non-circulating SI in the LAD area was significantly greater for the ischemia group than the sham group [5.19 ± 2.19 (ischemia) vs. 0.31 ± 0.13 (sham) dB, p < 0.01]. Non-circulating SI in the LAD area was significantly higher than that in the non-LAD area when compared in the same rat of the ischemia group [5.19 ± 2.19 (LAD) vs. 0.18 ± 0.64 (non-LAD) dB, p < 0.01]. MPO-positive cells were confirmed in the LAD area of the ischemia group. Conclusion: Inflammation induced by myocardial ischemia-reperfusion in rats could be quantitatively assessed by ultrasound inflammation imaging with non-specific targeted microbubbles.This version of the article has been accepted for publication, after peer review (when applicable) and is subject to Springer Nature’s AM terms of use, but is not the Version of Record and does not reflect post-acceptance improvements, or any corrections. The Version of Record is available online at: https://doi.org/10.1007/s12574-010-0051-z

Goal-orientation mechanism in a fractal manufacturing system

Decomposition of tasks in ordinary manufacturing systems is usually based on the predefined goal of the system. To achieve the high-level goals (e.g. factory goal or company goal), several subgoals should be achieved in advance. However, goals can dynamically change along with the current status of the system and the external environmental situations. Thus, a manufacturing system should support the goal formations, which can bear these changes for efficient and effective operations. Therefore, it is necessary to develop a systematic methodology for goal formations in a manufacturing system. In particular, the formation and/or change of goals in real-time should be possible for distributed and dynamic systems including a fractal manufacturing system (FrMS). However, most researchers have started their study from an assumption that every goal in the system is naturally well defined. This paper proposes a methodology for the goal-formation process (GFP), which embodies one of the characteristics of a fractal (i.e. goal orientation) in the FrMS. In order to generate fuzzy goals and propagate them in the system, fuzzification/defuzzification and goal-generation procedures are presented in detail. For easy understanding of the procedure, an exemplary goal generation is also illustrated within the proposed GFP frame-work. By applying the GFP, we expect that the manufacturing system would become autonomous and flexible by generating and evolving goals without human intervention.close142

CLLD8/KMT1F Is a Lysine Methyltransferase That Is Important for Chromosome Segregation*

Proteins bearing a SET domain have been shown to methylate lysine residues in histones and contribute to chromatin architecture. Methylation of histone H3 at lysine 9 (H3K9) has emerged as an important player in the formation of heterochromatin, chromatin condensation, and transcriptional repression. Here, we have characterized a previously undescribed member of the histone H3K9 methyltransferase family named CLLD8 (or SETDB2 or KMT1F). This protein contributes to the trimethylation of both interspersed repetitive elements and centromere-associated repeats and participates in the recruitment of heterochromatin protein 1 to centromeres. Consistently, depletion in CLLD8/KMT1F coincides with a loss of CENP proteins and delayed mitosis, suggesting that this protein participates in chromosome condensation and segregation. Altogether, our results provide evidence that CLLD8/KMT1F is recruited to heterochromatin regions and contributes in vivo to the deposition of trimethyl marks in concert with SUV39H1/KMT1A