期刊
PHYSICS IN MEDICINE AND BIOLOGY
卷 52, 期 15, 页码 4601-4614出版社
IOP PUBLISHING LTD
DOI: 10.1088/0031-9155/52/15/016
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资金
- NIAMS NIH HHS [R01 AR045172, R01 AR 45172] Funding Source: Medline
The objective of this spectroscopic imaging study is to understand the anisotropic behavior of articular cartilage under polarized infrared radiation at 6.25 mu m pixel resolution. Paraffin embedded canine humeral cartilage-bone blocks were used to obtain 6 mu m thick tissue sections. Two wire grid polarizers were used to manipulate the polarization states of IR radiation by setting them for various polarizer/analyzer angles. The characteristics of the major chemical components (amide I, amide II, amide III and sugar) of articular cartilage were investigated using (a) a polarizer and (b) a combination of a polarizer and an analyzer. These results were compared to those obtained using only an analyzer. The infrared anisotropy (variation in infrared absorption as a function of polarization angles) of amide I, amide II and amide III bands correlates with the orientation of collagen fibrils along the tissue depth in different histological zones. An ' anisotropic flipping' region of amide profiles indicates the possibility of using Fourier transform infrared imaging (FTIRI) to determine the histological zones in cartilage. Cross-polarization experiment indicates the resolution of overlapping peaks of collagen triple helix and/or proteoglycan in articular cartilage.
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