Application of 7T MRS to High-Grade Gliomas.

MRS, including single-voxel spectroscopy and MR spectroscopic imaging, captures metabolites in high-grade gliomas. Emerging evidence indicates that 7T MRS may be more sensitive to aberrant metabolic activity than lower-field strength MRS. However, the literature on the use of 7T MRS to visualize high-grade gliomas has not been summarized. We aimed to identify metabolic information provided by 7T MRS, optimal spectroscopic sequences, and areas for improvement in and new applications for 7T MRS. Literature was found on PubMed using "high-grade glioma," "malignant glioma," "glioblastoma," "anaplastic astrocytoma," "7T," "MR spectroscopy," and "MR spectroscopic imaging." 7T MRS offers higher SNR, modestly improved spatial resolution, and better resolution of overlapping resonances. 7T MRS also yields reduced Cramér-Rao lower bound values. These features help to quantify D-2-hydroxyglutarate in isocitrate dehydrogenase 1 and 2 gliomas and to isolate variable glutamate, increased glutamine, and increased glycine with higher sensitivity and specificity. 7T MRS may better characterize tumor infiltration and treatment effect in high-grade gliomas, though further study is necessary. 7T MRS will benefit from increased sample size; reductions in field inhomogeneity, specific absorption rate, and acquisition time; and advanced editing techniques. These findings suggest that 7T MRS may advance understanding of high-grade glioma metabolism, with reduced Cramér-Rao lower bound values and better measurement of smaller metabolite signals. Nevertheless, 7T is not widely used clinically, and technical improvements are necessary. 7T MRS isolates metabolites that may be valuable therapeutic targets in high-grade gliomas, potentially resulting in wider ranging neuro-oncologic applications.

In vivo 31P spectroscopy by fully adiabatic extended image selected in vivo spectroscopy: a comparison between 3 T and 7 T.

An improved image selected in vivo spectroscopy (ISIS) sequence for localized (31)P magnetic resonance spectroscopy at 7 T was developed. To reduce errors in localization accuracy, adiabatic excitation, gradient offset independent adiabatic inversion pulses, and a special extended ISIS ordering scheme were used. The localization accuracy of extended ISIS was investigated in phantoms. The possible spectral quality and reproducibility in vivo was explored in a volunteer (brain, muscle, and liver). A comparison between 3 T and 7 T was performed in five volunteers. Adiabatic extended ISIS provided high spectral quality and accurate localization. The contamination in phantom experiments was only ∼5%, even if a pulse repetition time ∼ 1.2·T(1) was chosen to maximize the signal-to-noise ratio per unit time. High reproducibility was found in the calf muscle for 2.5 cm isotropic voxels at 7 T. When compared with 3 T, localized (31)P magnetic resonance spectroscopy in the human calf muscle at 7 T provided ∼3.2 times higher signal-to-noise ratio (as judged from phosphocreatine peak amplitude in frequency domain after matched filtering). At 7 T, extended ISIS allowed the performance of high-quality localized (31)P magnetic resonance spectroscopy in a short measurement time (∼3 to 4 min) and isotropic voxel sizes of ∼2.5 to 3 cm. With such short measurement times, localized (31)P magnetic resonance spectroscopy has the potential to be applied not only for clinical research but also for routine clinical practice.

Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.

One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides under Magic Angle Spinning. The functional dependence of a series of anisotropic recoupling schemes is analyzed using theoretical and numerical methods. These studies lead to the construction of a set of polarization dephasing or transfer units that probe local backbone conformation and overall molecular orientation within the same NMR experiment. Experimental results are shown for a randomly oriented peptide and for two model membrane-peptides reconstituted into lipid bilayers and oriented on polymer films according to a method proposed by Bechinger et al.