MRS thermometry calibration at 3T: effects of protein, ionic concentration and magnetic field strength

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MRS thermometry calibration at 3T: effects of protein, ionic concentration and magnetic field strength. / Babourina-Brooks, Ben; Simpson, Robert; Arvanitis, Theodoros; Machin, Graham ; Peet, Andrew; Davies, Nigel.

In: NMR in biomedicine, Vol. 28, No. 7, 07.2015, p. 792-800.

Research output: Contribution to journalArticlepeer-review

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Babourina-Brooks, Ben ; Simpson, Robert ; Arvanitis, Theodoros ; Machin, Graham ; Peet, Andrew ; Davies, Nigel. / MRS thermometry calibration at 3T: effects of protein, ionic concentration and magnetic field strength. In: NMR in biomedicine. 2015 ; Vol. 28, No. 7. pp. 792-800.

Bibtex

@article{8f3971532a344a2cad302903e3f1994a,
title = "MRS thermometry calibration at 3T: effects of protein, ionic concentration and magnetic field strength",
abstract = "MRS thermometry has been utilized to measure temperature changes in the brain, which may aid in the diagnosis of brain trauma and tumours. However, the temperature calibration of the technique has been shown to be sensitive to non-temperature-based factors, which may provide unique information on the tissue microenvironment if the mechanisms can be further understood. The focus of this study was to investigate the effects of varied protein content on the calibration of MRS thermometry at 3 T, which has not been thoroughly explored in the literature. The effects of ionic concentration and magnetic field strength were also considered. Temperature reference materials were controlled by water circulation and freezing organic fixed-point compounds (diphenyl ether and ethylene carbonate) stable to within 0.2 °C. The temperature was measured throughout the scan time with a fluoro-optic probe, with an uncertainty of 0.16 °C. The probe was calibrated at the National Physical Laboratory (NPL) with traceability to the International Temperature Scale 1990 (ITS-90). MRS thermometry measures were based on single-voxel spectroscopy chemical shift differences between water and N-acetylaspartate (NAA), Δ(H20-NAA), using a Philips Achieva 3 T scanner. Six different phantom solutions with varying protein or ionic concentration, simulating potential tissue differences, were investigated within a temperature range of 21–42 °C. Results were compared with a similar study performed at 1.5 T to observe the effect of field strengths. Temperature calibration curves were plotted to convert Δ(H20-NAA) to apparent temperature. The apparent temperature changed by −0.2 °C/% of bovine serum albumin (BSA) and a trend of 0.5 °C/50 mM ionic concentration was observed. Differences in the calibration coefficients for the 10% BSA solution were seen in this study at 3 T compared with a study at 1.5 T. MRS thermometry may be utilized to measure temperature and the tissue microenvironment, which could provide unique unexplored information for brain abnormalities and other pathologies.",
keywords = "MRS thermometry, brain temperature, proton resonance frequency, chemical shift, MRI, calibration",
author = "Ben Babourina-Brooks and Robert Simpson and Theodoros Arvanitis and Graham Machin and Andrew Peet and Nigel Davies",
year = "2015",
month = jul,
doi = "10.1002/nbm.3303",
language = "English",
volume = "28",
pages = "792--800",
journal = "NMR in biomedicine",
issn = "0952-3480",
publisher = "Wiley",
number = "7",

}

RIS

TY - JOUR

T1 - MRS thermometry calibration at 3T: effects of protein, ionic concentration and magnetic field strength

AU - Babourina-Brooks, Ben

AU - Simpson, Robert

AU - Arvanitis, Theodoros

AU - Machin, Graham

AU - Peet, Andrew

AU - Davies, Nigel

PY - 2015/7

Y1 - 2015/7

N2 - MRS thermometry has been utilized to measure temperature changes in the brain, which may aid in the diagnosis of brain trauma and tumours. However, the temperature calibration of the technique has been shown to be sensitive to non-temperature-based factors, which may provide unique information on the tissue microenvironment if the mechanisms can be further understood. The focus of this study was to investigate the effects of varied protein content on the calibration of MRS thermometry at 3 T, which has not been thoroughly explored in the literature. The effects of ionic concentration and magnetic field strength were also considered. Temperature reference materials were controlled by water circulation and freezing organic fixed-point compounds (diphenyl ether and ethylene carbonate) stable to within 0.2 °C. The temperature was measured throughout the scan time with a fluoro-optic probe, with an uncertainty of 0.16 °C. The probe was calibrated at the National Physical Laboratory (NPL) with traceability to the International Temperature Scale 1990 (ITS-90). MRS thermometry measures were based on single-voxel spectroscopy chemical shift differences between water and N-acetylaspartate (NAA), Δ(H20-NAA), using a Philips Achieva 3 T scanner. Six different phantom solutions with varying protein or ionic concentration, simulating potential tissue differences, were investigated within a temperature range of 21–42 °C. Results were compared with a similar study performed at 1.5 T to observe the effect of field strengths. Temperature calibration curves were plotted to convert Δ(H20-NAA) to apparent temperature. The apparent temperature changed by −0.2 °C/% of bovine serum albumin (BSA) and a trend of 0.5 °C/50 mM ionic concentration was observed. Differences in the calibration coefficients for the 10% BSA solution were seen in this study at 3 T compared with a study at 1.5 T. MRS thermometry may be utilized to measure temperature and the tissue microenvironment, which could provide unique unexplored information for brain abnormalities and other pathologies.

AB - MRS thermometry has been utilized to measure temperature changes in the brain, which may aid in the diagnosis of brain trauma and tumours. However, the temperature calibration of the technique has been shown to be sensitive to non-temperature-based factors, which may provide unique information on the tissue microenvironment if the mechanisms can be further understood. The focus of this study was to investigate the effects of varied protein content on the calibration of MRS thermometry at 3 T, which has not been thoroughly explored in the literature. The effects of ionic concentration and magnetic field strength were also considered. Temperature reference materials were controlled by water circulation and freezing organic fixed-point compounds (diphenyl ether and ethylene carbonate) stable to within 0.2 °C. The temperature was measured throughout the scan time with a fluoro-optic probe, with an uncertainty of 0.16 °C. The probe was calibrated at the National Physical Laboratory (NPL) with traceability to the International Temperature Scale 1990 (ITS-90). MRS thermometry measures were based on single-voxel spectroscopy chemical shift differences between water and N-acetylaspartate (NAA), Δ(H20-NAA), using a Philips Achieva 3 T scanner. Six different phantom solutions with varying protein or ionic concentration, simulating potential tissue differences, were investigated within a temperature range of 21–42 °C. Results were compared with a similar study performed at 1.5 T to observe the effect of field strengths. Temperature calibration curves were plotted to convert Δ(H20-NAA) to apparent temperature. The apparent temperature changed by −0.2 °C/% of bovine serum albumin (BSA) and a trend of 0.5 °C/50 mM ionic concentration was observed. Differences in the calibration coefficients for the 10% BSA solution were seen in this study at 3 T compared with a study at 1.5 T. MRS thermometry may be utilized to measure temperature and the tissue microenvironment, which could provide unique unexplored information for brain abnormalities and other pathologies.

KW - MRS thermometry

KW - brain temperature

KW - proton resonance frequency

KW - chemical shift

KW - MRI

KW - calibration

U2 - 10.1002/nbm.3303

DO - 10.1002/nbm.3303

M3 - Article

VL - 28

SP - 792

EP - 800

JO - NMR in biomedicine

JF - NMR in biomedicine

SN - 0952-3480

IS - 7

ER -