T2 and T1rho MRI in articular cartilage systems.
T2 and T1rho have potential to nondestructively detect cartilage degeneration. However, reports in the literature regarding their diagnostic interpretation are conflicting. In this study, T2 and T1rho were measured at 8.5 T in several systems: 1) Molecular suspensions of collagen and GAG (pure concentration effects): T2 and T1rho demonstrated an exponential decrease with increasing [collagen] and [GAG], with [collagen] dominating. T2 varied from 90 to 35 ms and T1rho from 125 to 55 ms in the range of 15-20% [collagen], indicating that hydration may be a more important contributor to these parameters than previously appreciated. 2) Macromolecules in an unoriented matrix (young bovine cartilage): In collagen matrices (trypsinized cartilage) T2 and T1rho values were consistent with the expected [collagen], suggesting that the matrix per se does not dominate relaxation effects. Collagen/GAG matrices (native cartilage) had 13% lower T2 and 17% lower T1rho than collagen matrices, consistent with their higher macromolecular concentration. Complex matrix degradation (interleukin-1 treatment) showed lower T2 and unchanged T1rho relative to native tissue, consistent with competing effects of concentration and molecular-level changes. In addition, the heterogeneous GAG profile in these samples was not reflected in T2 or T1rho. 3) Macromolecules in an oriented matrix (mature human tissue): An oriented collagen matrix (GAG-depleted human cartilage) showed T2 and T(1rho) variation with depth consistent with 16-21% [collagen] and/or fibril orientation (magic angle effects) seen on polarized light microscopy, suggesting that both hydration and structure comprise important factors. In other human cartilage regions, T2 and T1rho abnormalities were observed unrelated to GAG or collagen orientation differences, demonstrating that hydration and/or molecular-level changes are important. Overall, these studies illustrate that T2 and T1rho are sensitive to biologically meaningful changes in cartilage. However, contrary to some previous reports, they are not specific to any one inherent tissue parameter.
Harvard-Massachusetts Institute of Technology Division of Health Sciences & Technology, Cambridge, Massachusetts, USA.
Nina M
NM
Menezes
Martha L
ML
Gray
James R
JR
Hartke
Deborah
D
Burstein
D000818:Animals; D001834:Body Water / Q000737:chemistry; D002357:Cartilage Diseases / Q000175:diagnosis / Q000473:pathology; D002358:Cartilage, Articular / Q000033:anatomy & histology* / Q000737:chemistry; D002417:Cattle; D003094:Collagen / Q000737:chemistry; D003287:Contrast Media; D019786:Gadolinium DTPA; D006025:Glycosaminoglycans / Q000737:chemistry; D006801:Humans; D007089:Image Enhancement / Q000379:methods; D007375:Interleukin-1 / Q000494:pharmacology; D046911:Macromolecular Substances; D008279:Magnetic Resonance Imaging / Q000379:methods*; D008859:Microscopy, Polarization; D014357:Trypsin / Q000494:pharmacology
D003287:Contrast Media; D006025:Glycosaminoglycans; D007375:Interleukin-1; D046911:Macromolecular Substances; D003094:Collagen; D014357:Trypsin; D019786:Gadolinium DTPA