Are Collagen Protons Visible with the Zero Echo Time (ZTE) Magnetic Resonance Imaging Sequence: A D<sub>2</sub>O Exchange and Freeze-Drying Study
It is known that ultrashort echo time (UTE) magnetic resonance imaging (MRI) sequences can detect signals from water protons but not collagen protons in short T2 species such as cortical bone and tendons. However, whether collagen protons are visible with the zero echo time (ZTE) MRI sequence is sti...
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| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-12-01
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| Series: | Bioengineering |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2306-5354/12/1/16 |
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| Summary: | It is known that ultrashort echo time (UTE) magnetic resonance imaging (MRI) sequences can detect signals from water protons but not collagen protons in short T2 species such as cortical bone and tendons. However, whether collagen protons are visible with the zero echo time (ZTE) MRI sequence is still unclear. In this study, we investigated the potential of the ZTE MRI sequence on a clinical 3T scanner to directly image collagen protons via D<sub>2</sub>O exchange and freeze-drying experiments. ZTE and UTE MRI sequences were employed to image fully hydrated bovine cortical bone (<i>n</i> = 10) and human patellar tendon (<i>n</i> = 1) specimens. Then, each specimen was kept in a 30 mL syringe filled with D<sub>2</sub>O solution for two days. Fresh D<sub>2</sub>O was flushed every 2 h to reach a more complete D<sub>2</sub>O–H<sub>2</sub>O exchange. Later, the samples were lyophilized for over 40 h and then sealed in tubes. Finally, the samples were brought to room temperature and visualized using the identical 3D ZTE and UTE sequences. All hydrated bone and tendon specimens showed high signals with ZTE and UTE sequences. However, all specimens showed zero signal after the D<sub>2</sub>O exchange and freeze-drying procedures. Therefore, similar to UTE imaging, the signal source in ZTE imaging is water. The ZTE sequence cannot directly detect signals from collagen protons in bone and tendons. |
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| ISSN: | 2306-5354 |