Karyn Elizabeth Chappell1, Mihailo Ristic2, Donald McRobbie3, Wladyslaw Gedroyc4, Djordje Brujic2, and Catherine Van Der Straeten5
1Medicine, Orthopaedic Surgery, Stanford University, Redwood City, CA, United States, 2Mechanical Engineering, Imperial College London, London, United Kingdom, 3University of Adelaide, Adelaide, Australia, 4Imperial College London, London, United Kingdom, 5Imperial College London/Ghent University, Ghent, Belgium
Synopsis
Does freeze/thaw of cadaveric specimens’ damage collagen fibre
orientation? Magic angle directional
imaging (MADI) in caprine knees assessed the underlying tissue structure before
and after freezing for three and six weeks. Tendon thickness reduced after 6
weeks of freezing. Segmented collagen
containing voxels decreased by half after freezing. Voids appeared in the internal tendon
structure suggestive of ice crystal formation that disrupted collagen fibre
orientation. The
severity of the structural changes increased the longer the tissue was frozen.
Interpreting results with frozen/thawed cadaveric
specimens needs care as freezing damages collagen fibre structure that may impact on biomechanical and other properties.
Introduction
Cadaveric tissue preserved by chemical fixation
or freezing is widely used for developing musculoskeletal (MSK) research. Limbs are frozen then thawed before scanning
during MR imaging experiments. Van der Made et
al. found that freeze thawing does not affect the MR image quality unless
repeated too often1. However,
in rabbit patellar tendons biomechanical and structural changes to tissues after
freezing at -80˚C worsened the longer the tissue was frozen2. When Chang et al. studied tendons they found no significant changes to T2 or
T2* after five freeze/thaw cycles3 but Powdner et al. measured a 12% reduction to T2* after multiple cycles4. In developing the MADI technique we investigated if freeze/thawed tissue could be utilised for a repeatability study or does the freeze/thaw process alter the collagen structure of tendons?Methods
The effect of freezing on collagen fibre structure
was explored using two fresh caprine knees that were scanned then frozen at
-20˚C for a period of three or six weeks before being thawed and
re-scanned. The two time points were
chosen to reflect the changes in collagen fibre bundles noted by Tsuchida et al.2. The caprine knees were scanned in nine orientations using the MADI
technique5. Fibre orientation
maps (FOM) of the segmented patellar tendon before and after freezing were
computed using Matlab 2015b. 1mm3
voxel glyphs showing net collagen fibre orientation in the patellar tendons were
computed using ParaView 5.1.2. Comparison of
FOM and glyphs before and after freezing at the two time points are visualised.Results
No changes to MR image quality were noted
between the two caprine knees before and after freezing. The thickness of the patellar tendon remained
unchanged after three weeks of freezing. However after six weeks of freezing
the patellar tendon thinned and altered signal intensity occurred
within the trabecular bone in the tibial growth plate (fig1). On the FOM voxel
voids are seen in the patellar tendon three weeks after freezing but not in
the fresh specimen (fig2A). At six weeks after freezing the voxel voids
on the FOM are more prevalent with larger spaces opening up within the tendon (fig2B).
Voxel voids indicate areas where the magic angle effect has disappeared
because the voxels are no longer exhibiting a variation in signal intensity
with the MADI technique. Segmented
voxels decreased from fresh to frozen tissue.
Fresh samples had 1452 and 2053 voxels respectively which decreased by
43% (824 voxel) at three weeks and 56% (909 voxels) at six weeks. ParaView glyph visualisation of the tendons
before and after freezing demonstrated a change in thickness and damage
to the collagen fibre structure (coronal and axial images) which is more pronounced
at six weeks (fig3).Discussion
There was little variation in MR image quality of the 3D T1-W images between
the freshly scanned and freeze/thawed caprine knees. This finding is in agreement with a number of
other researchers6, 7, 8, 9.
Powdner et al. demonstrated
that multiple freeze thaw cycles reduced T2* indicative of collagen
structure alteration4. This
was why a single freeze thaw cycle was used for this work. However there was a notable change in
thickness of the patellar tendon after six weeks of freezing that may reflect
changes to the collagen structure.
Voxel voids on the
FOM and ParaView glyphs after freezing are suggestive of ice crystal formation
that caused interfibrillar gaps to form in the tendon2, 10, 11. Giannini et
al. noted a decrease in collagen fibrils after freezing as ice crystals
caused swelling, splitting and fragmentation of the collagen bundles
histologically11. Tsuchida et al. found freezing significantly
altered the microstructure of normal patellar tendon after 3 weeks and the
ultrastructure after 6 weeks2. Our findings are in line with Giannini et al. and Tschida et al.11,2. An alteration of
the caprine patellar tendon structure was detected after freezing. Unfortunately without a histological
reference which was not possible in this study a
definitive conclusion was not possible. It would also be difficult to say with
certainty due to the one millimetre resolution whether the ultrastructure
of collagen had altered because it was not measured. The longer the tendon was frozen the less
voxels were segmented (decreased by 56%) and the greater the number of voxels
voids within the tendon, which is suggestive of damage to collagen fibre
structure. Conclusion
Frozen/thawed cadaveric tissue is commonly used
in MSK MRI research development. Careful interpretation of results
concerning collagen fibre structure after freezing is necessary. Ice crystals
may alter the hydrogen bonding on the surface of the protein molecular
structure causing damage to the collagen fibre bundles. The severity of the structural
changes appears to increase with the length of time the tissue is frozen before
being thawed and scanned. Increasing
tissue longevity by freezing then thawing in repeatability experiments is not
advisable due to damage of the collagen fibre structure after freezing for three and six weeks. Further work may be useful to
assess shorter periods of freezing such as two weeks or less. A faster freeze method with colder storage temperature (i.e.
-80˚C) could also be assessed to determine if that reduced the ice crystal
formation and damage.Acknowledgements
This
work was supported by the National Institute for Health Research (NIHR)
Invention for Innovation (i4i) under Grant II-LA-1111-20005. We are grateful to Charing Cross Hospital MRI
department and Imaging Committee for the kind use of the Siemens 3T Verio.References
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