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Magnetization transfer in cartilage and its constituent macromolecules
Author(s) -
Gray Martha L.,
Burstein Deborah,
Lesperance Leann M.,
Gehrke Lee
Publication year - 1995
Publication title -
magnetic resonance in medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.696
H-Index - 225
eISSN - 1522-2594
pISSN - 0740-3194
DOI - 10.1002/mrm.1910340307
Subject(s) - magnetization transfer , cartilage , glycosaminoglycan , chemistry , macromolecule , nuclear magnetic resonance , proton , trypsin , analytical chemistry (journal) , magnetization , biophysics , chromatography , biochemistry , magnetic resonance imaging , anatomy , enzyme , magnetic field , biology , medicine , physics , radiology , quantum mechanics
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) single‐component 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 12‐μT 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 = ‐0.0137[% GAG] + 1.02] and exponential for collagen suspensions ( M s / M o = 0.80 x exp[‐(%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 ± 0.13, n = 11, P < 0.001). In contrast, a 10‐day treatment of cartilage with 100 ng/ml of interleukin‐1β (1L‐1β) caused a 19% decrease in M s / M o (final/initial values = 0.81 ± 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.