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Anisotropic analysis of multi-component T2 and T1? relaxations in achilles tendon by NMR spectroscopy and microscopic MRI.

ABSTRACT: To study the anisotropic characteristics of both multi-component T2 and T1? relaxation times in tendon.T2 and T1? were measured in tendon by NMR spectroscopy at different orientations and by microscopic MRI at the magic angle. Several experimental issues in the multi-component relaxation measurements were investigated, including the effects of echo spacing, the resolution of MRI experiments, the influence of the specimen orientations, and the strengths of different spin-lock frequencies in T1? experiments.Both the values and fractions of T2 in tendon showed significant orientational dependence. The values and fractions of T1? strongly depended on both the specimen orientation and the spin-lock strength. The imaging resolution (35-280 ?m) had little influence in the T2 experiments. Both the echo spacings (0.6-3.0 ms) in the T2 experiment and the spin-lock strengths (0.5-5 kHz) in the T1? experiment affected the quantification of the multi-component relaxation. Up to three T2 and T1? components were resolved in tendon.Multi-component relaxations could be attributed to different populations of water in the tissue. The transitions between a mono-component and multi-component result call for the caution in interpreting the relaxation results.

SUBMITTER: Wang N

PROVIDER: S-EPMC3638061 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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Anisotropic analysis of multi-component T2 and T1ρ relaxations in achilles tendon by NMR spectroscopy and microscopic MRI.

Wang Nian N Xia Yang Y

Journal of magnetic resonance imaging : JMRI 20130124 3

<h4>Purpose</h4>To study the anisotropic characteristics of both multi-component T2 and T1ρ relaxation times in tendon.<h4>Materials and methods</h4>T2 and T1ρ were measured in tendon by NMR spectroscopy at different orientations and by microscopic MRI at the magic angle. Several experimental issues in the multi-component relaxation measurements were investigated, including the effects of echo spacing, the resolution of MRI experiments, the influence of the specimen orientations, and the strengt ...[more]

PMID: 23349070

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Project description:This paper presents a more systematic study of steady-state and time-resolved autofluorescence spectroscopy of collagen isolated from bovine Achilles tendon. In steady-state fluorescence measurements, the excitation and emission spectra of collagen powder, recorded at different fluorescence excitation and detection wavelengths, were compared with the fluorescence excitation and emission spectra of the amino acids phenylalanine, tyrosine, and tryptophan, as well as with similar spectra for 13 autofluorescent collagen cross-links, which have been identified and described in the literature so far. In time-resolved studies, fluorescence was excited by the pulsed light of different wavelengths, and for each excitation wavelength, fluorescence decay was recorded for several detection wavelengths. Data analysis allowed recovery of the fluorescence decay times for each experimental excitation detection event. The obtained information on the decay times of the measured fluorescent signals was discussed, taking into account the available literature data from similar studies of isolated collagen and collagen-rich tissues. Based on the obtained results, it was found that the shape and position of the measured fluorescence excitation and emission spectra of collagen strongly depend on the emission and excitation wavelengths selected in the measurements. From the recorded excitation and emission bands of collagen, it can be concluded with high probability that there are additional, so far unidentified, collagen cross-links, which can be excited at longer excitation wavelengths. In addition, the collagen excitation spectra were measured at longer emission wavelengths at which the collagen cross-links emit fluorescent light. In addition to the emission spectra obtained for excitation in the deep-UV region, the results of time-resolved fluorescence studies with excitation in the deep-UV region and detection at longer wavelengths suggest that fluorescence excitation energy transfer processes occur from the amino acids to the collagen cross-links, and also between the cross-links themselves.

Dataset Information

Anisotropic analysis of multi-component T2 and T1? relaxations in achilles tendon by NMR spectroscopy and microscopic MRI.

Publications

Anisotropic analysis of multi-component T2 and T1ρ relaxations in achilles tendon by NMR spectroscopy and microscopic MRI.

Similar Datasets

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