15 research outputs found
Gated myocardial perfusion SPECT underestimates left ventricular volumes and shows high variability compared to cardiac magnetic resonance imaging -- a comparison of four different commercial automated software packages
Abstract Background We sought to compare quantification of left ventricular volumes and ejection fraction by different gated myocardial perfusion SPECT (MPS) programs with each other and to magnetic resonance (MR) imaging. Methods N = 100 patients with known or suspected coronary artery disease were examined at rest with 99 mTc-tetrofosmin gated MPS and cardiac MR imaging. Left ventricular end-diastolic volume (EDV), end-systolic volume (ESV), stroke volume (SV) and ejection fraction (EF) were obtained by analysing gated MPS data with four different programs: Quantitative Gated SPECT (QGS), GE MyoMetrix, Emory Cardiac Toolbox (ECTb) and Exini heart. Results All programs showed a mean bias compared to MR imaging of approximately -30% for EDV (-22 to -34%, p Conclusions Gated MPS, systematically underestimates left ventricular volumes by approximately 30% and shows a high variability, especially for ESV. For EF, accuracy was better, with a mean bias between -15 and 6% of EF. It may be of value to take this into consideration when determining absolute values of LV volumes and EF in a clinical setting.</p
Evaluation of inter-departmental variability of ejection fraction and cardiac volumes in myocardial perfusion scintigraphy using simulated data
The consequences of a new software package for the quantification of gated-SPECT myocardial perfusion studies
Semiquantitative analysis of myocardial perfusion scintigraphy (MPS) has reduced inter- and intraobserver variability, and enables researchers to compare parameters in the same patient over time, or between groups of patients. There are several software packages available that are designed to process MPS data and quantify parameters. In this study the performances of two systems, quantitative gated SPECT (QGS) and 4D-MSPECT, in the processing of clinical patient data and phantom data were compared. The clinical MPS data of 148 consecutive patients were analysed using QGS and 4D-MSPECT to determine the end-diastolic volume, end-systolic volume and left ventricular ejection fraction. Patients were divided into groups based on gender, body mass index, heart size, stressor type and defect type. The AGATE dynamic heart phantom was used to provide reference values for the left ventricular ejection fraction. Although the correlations were excellent (correlation coefficients 0.886 to 0.980) for all parameters, significant differences (p < 0.001) were found between the systems. Bland-Altman plots indicated that 4D-MSPECT provided overall higher values of all parameters than QGS. These differences between the systems were not significant in patients with a small heart (end-diastolic volume < 70 ml). Other clinical factors had no direct influence on the relationship. Additionally, the phantom data indicated good linear responses of both systems. The discrepancies between these software packages were clinically relevant, and influenced by heart size. The possibility of such discrepancies should be taken into account when a new quantitative software system is introduced, or when multiple software systems are used in the same institution.Vascular Biology and Interventio
Creation and characterization of Japanese standards for myocardial perfusion SPECT: database from the Japanese Society of Nuclear Medicine Working Group
A new era for understanding amyloid structures and disease
The aggregation of proteins into amyloid fibrils and their deposition into plaques and intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition of amyloid fibrils, collectively known as amyloidosis, is associated with many pathological conditions that can be associated with ageing, such as Alzheimer disease, Parkinson disease, type II diabetes and dialysis-related amyloidosis. However, elucidation of the atomic structure of amyloid fibrils formed from their intact protein precursors and how fibril formation relates to disease has remained elusive. Recent advances in structural biology techniques, including cryo-electron microscopy and solid-state NMR spectroscopy, have finally broken this impasse. The first near-atomic-resolution structures of amyloid fibrils formed in vitro, seeded from plaque material and analysed directly ex vivo are now available. The results reveal cross-β structures that are far more intricate than anticipated. Here, we describe these structures, highlighting their similarities and differences, and the basis for their toxicity. We discuss how amyloid structure may affect the ability of fibrils to spread to different sites in the cell and between organisms in a prion-like manner, along with their roles in disease. These molecular insights will aid in understanding the development and spread of amyloid diseases and are inspiring new strategies for therapeutic intervention