MR spectroscopy quantitation: a review of frequency domain methods

There has been a vast increase in applications of magnetic resonance spectroscopy (MRS) in biomedical research during the last few years. This is not surprising since MRS provides both in vivo and in vitro a non‐invasive tool for various biochemical and biomedical studies. There are also expectations that clinical MRS will have an important role as a diagnostic tool. An essential prerequisite for the future success of MRS for applicability in biomedical sciences will be accurate and biochemically relevant data analysis (at as high a level of automation as possible). This review briefly describes principles of the methodology available for advanced quantitative data analysis in the frequency domain. Various biomedical applications are discussed in order to illustrate the practical aspects of the analyses and to show the applicability and power of biochemical prior knowledge‐based lineshape fitting analysis. Copyright © 2001 John Wiley & Sons, Ltd. Abbreviations used: Asp aspartate Cho choline Cr creatine EMCL extra‐myocellular lipids FID free induction decay FT Fourier transform GABA γ‐aminobutyric acid Glu glutamate Gln glutamine Glc glucose GPC glycerophosphocholine GPE glycerophosphoethanolamine HDL high density lipoprotein IDL intermediate density lipoprotein IMCL intra‐myocellular lipids LDL low density lipoprotein P i inorganic phosphate myo ‐Ins myo ‐inositol NAA N ‐acetyl‐aspartate NAAG N ‐acetylaspartylglutamate NTP nucleotide triphosphates PC phosphocholine PCr phosphocreatine PDE phosphodiesters PE phosphoethanolamine PME phosphomonoesters scyllo ‐Ins scyllo ‐inositol SNR signal‐to‐noise ratio Tau taurine TDFD frequency domain fitting using time domain models TLS total lineshape TSP sodium 3‐trimethylsilyl[2,2,3,3‐D 4 ] propionate VLDL very low density lipoprotein.