## Abstract These studies were designed to establish which structural elements of cartilage are responsible for proton magnetization transfer between water (Hf) and macromolecules (Hr) observed in MRI studies on articular cartilage. Saturation transfer techniques were used to monitor magnetization
Magnetization transfer in cartilage and its constituent macromolecules
β Scribed by Martha L. Gray; Deborah Burstein; Leann M. Lesperance; Lee Gehrke
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 681 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0740-3194
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The goal of this work was to investigate magnetization transfer (MT) in cartilage by measuring water proton signals M~s~/M~o~, as an indicator of MT, in (i) singleβcomponent systems of the tissue's constituent macromolecules and (ii) intact cartilage under control conditions and after two pathomimetic interventions. M~s~/M~o~ was quantified with a 12βΞΌT saturation pulse applied 6 kHz off resonance. Both glycosaminoglycans (GAG) and collagen exhibited concentration dependent effects on M~s~/M~o~, being approximately linear for GAG solutions (M~s~/M~o~ = β0.0137[% GAG] + 1.02] and exponential for collagen suspensions (M~s~/M~o~ = 0.80 x exp[β(%collagen)/6.66] + 0.20); the direct saturation of water could not account for the measured M~s~/M~o~. Although the effect of collagen on M~s~/M~o~ is much stronger than for a corresponding concentration of GAG, M~s~/M~o~ is not very sensitive to changes in collagen concentration in the physiological range. Tissue degradation with 25 mg/ml trypsin led to an increase in__M__~s~/M~o~ from the baseline value of 0.2 (final/initial values = 1.15 Β± 0.13, n = 11, P < 0.001). In contrast, a 10βday treatment of cartilage with 100 ng/ml of interleukinβ1Ξ² (1Lβ1Ξ²) caused a 19% decrease in M~s~/M~o~ (final/initial values = 0.81 Β± 0.08, n = 3, P = 0.085). The changes in hydration and macromolecular content for the two treatments were comparable, suggesting that M~s~/M~o~ is sensitive to macromolecular structure as well as concentration. In conclusion, whereas the baseline M~s~/M~o~ value in cartilage may be primarily due to the tissue collagen concentration, changes in M~s~/M~o~ may be due to physiological or pathophysiological changes in GAG concentration and tissue structure, and the measured M~s~/M~o~ may differentiate between various pathomimetic degradative procedures.
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