Search PubMed⌕ Search

PubMed · 9702700

Fast 1H spectroscopic imaging using a multi-element head-coil array.

Abstract

Fast proton magnetic resonance spectroscopic imaging (MRSI) using a multi-element head-coil array is examined with respect to three aspects: the coil design, the use of an appropriate signal combination method, and the design of the MRSI pulse sequence itself. An eight-element head-coil array has been developed to increase the signal-to-noise ratio (SNR) of MRSI in the human brain. The flexible wraparound design optimally fits different head sizes and thus provides high sensitivity. The signal combination of the individual coil elements is based on the approach proposed by Roemer et al. (Magn. Reson. Med. 16, 192 (1990)). An additional short prescan is performed to provide a good estimate of the complex coil sensitivity profiles, which are used in the signal combination procedure to correct the spectroscopic imaging data for the spatially varying intensity. The use of coil arrays in MRSI has some effect on the requirements for both water and lipid suppression. These techniques and a MRSI pulse sequence that provides a high spectroscopic resolution are described and discussed. Experimental results at 1.5 T show that metabolite maps of N-acetylaspartate (NAA), choline (Cho), phosphocreatine (PCr)/creatine (Cr) can be obtained within a 5-min acquisition time.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T Schäffter, P Börnert, C Leussler, I C Carlsen, D Leibfritz. 1998. Fast 1H spectroscopic imaging using a multi-element head-coil array.. https://doi.org/10.1002/mrm.1910400204

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Insights into the role of an active site aspartate in Ty1 reverse transcriptase polymerization.

Long terminal repeat-containing retrotransposons encode reverse transcriptases (RTs) that replicate their RNA into integratable, double-stranded DNA. A mutant version of the RT from Saccharomyces cerevisiae retrotransposon Ty1, in which one of the three active site aspartates has been changed to asparagine (D211N), is still capable of in vitro polymerization, although it is blocked for in vivo transposition. We generated recombinant WT and D211N Ty1 RTs to study RT function and determine specific roles for the Asp(211) residue. Presteady-state kinetic analysis of the two enzymes shows that the D211N mutation has minimal effect on nucleotide binding but reduces the k(pol) by approximately 230-fold. The mutation reduces binding affinity for both Mn(2+) and Mg(2+), indicating that the Asp(211) side chain helps create a tight metal binding pocket. Although both enzymes are highly processive and tend to remain bound to their initial substrate, each shows distinctive patterns of pausing, attributable to interactions between metal ions and the active site residue. These results provide insights to specific roles for the Asp(211) residue during polymerization and indicate unusual enzymatic properties that bear on the Ty1 replication pathway.

Aspartic Acid↗

Potentiation of the osmosensitive release of taurine and D-aspartate from SH-SY5Y neuroblastoma cells after activation of M3 muscarinic cholinergic receptors.

The ability of muscarinic cholinergic receptors (mAChRs) to regulate the volume-sensitive efflux of two organic osmolytes, namely, taurine and d-aspartate, from human SH-SY5Y neuroblastoma cells has been examined. Incubation of the cells with hypoosmolar buffers resulted in an efflux of both osmolytes, with the threshold for release occurring at approximately 225 mOsM for taurine and d-aspartate. Inclusion of oxotremorine-M (Oxo-M), a muscarinic agonist, resulted in a marked enhancement of the volume-dependent efflux of both osmolytes and increased the threshold osmolarity for taurine and d-aspartate release to 340 (isotonic) and 320 mOsM, respectively. Maximum agonist stimulation of osmolyte release (350% of basal) was observed in the range of 225 to 250 mOsM. Oxo-M-stimulated osmolyte efflux was inhibited by muscarinic antagonists with a rank order of potency 4-diphenylacetoxy-N-methylpiperidine methiodide > pirenzepine > 11-[[2-[(diethylamino)methyl]-1-piperidinyl]acetyl]-5,11-dihydro-6H-pyrido[2,3-b][1,4]benzodiazepin-6-one, a pharmacological profile identical to that obtained for M3 mAChR-stimulated phosphoinositide hydrolysis. Agonist-stimulated efflux of both osmolytes could be inhibited by inclusion of either anion channel blockers known to inhibit the volume-sensitive organic anion channel (VSOAC) or by a tyrosine kinase inhibitor alpha-cyano-(3,4-dihydroxy)cinnamonitrile. The results indicate that the activation of M3 mAChRs on SH-SY5Y neuroblastoma facilitates the ability of these cells to respond to very limited reductions in osmolarity via a release of osmolytes. mAChR-stimulated osmolyte efflux is mediated via a VSOAC and seems to require the activity of a tyrosine kinase.

Aspartic Acid↗

Proteomic response analysis of a threonine-overproducing mutant of Escherichia coli.

The proteomic response of a threonine-overproducing mutant of Escherichia coli was quantitatively analysed by two-dimensional electrophoresis. Evidently, 12 metabolic enzymes that are involved in threonine biosynthesis showed a significant difference in intracellular protein level between the mutant and native strain. The level of malate dehydrogenase was more than 30-fold higher in the mutant strain, whereas the synthesis of citrate synthase seemed to be severely inhibited in the mutant. Therefore, in the mutant, it is probable that the conversion of oxaloacetate into citrate was severely inhibited, but the oxidation of malate to oxaloacetate was significantly up-regulated. Accumulation of oxaloacetate may direct the metabolic flow towards the biosynthetic route of aspartate, a key metabolic precursor of threonine. Synthesis of aspartase (aspartate ammonia-lyase) was significantly inhibited in the mutant strain, which might lead to the enhanced synthesis of threonine by avoiding unfavourable degradation of aspartate to fumarate and ammonia. Synthesis of threonine dehydrogenase (catalysing the degradation of threonine finally back to pyruvate) was also significantly down-regulated in the mutant. The far lower level of cystathionine beta-lyase synthesis in the mutant seems to result in the accumulation of homoserine, another key precursor of threonine. In the present study, we report that the accumulation of important threonine precursors, such as oxaloacetate, aspartate and homoserine, and the inhibition of the threonine degradation pathway played a critical role in increasing the threonine biosynthesis in the E. coli mutant.

Aspartic Acid↗