Abstract
Fourier transform infrared microscopic imaging (FTIRI) was used to quantitatively examine the anisotropies of proteoglycan (PG) and collagen in articular cartilage. Dried 6 μm thick sections of canine humeral cartilage were imaged at 6.25 μm pixel-size in FTIRI with an infrared analyzer set at 26 different angles between 0° and 180° polarization. Like the amide II and amide III peaks, the 1338 cm(-1) band confirms the anisotropy of collagen fibrils in cartilage. The absorption profile of the sugar band shows an anisotropic flipping at the deeper part in the radial zone, just above the tidemark. Together with the reduction in the PG concentration and subsequent increase in tissue calcification in this region, this anisotropy flipping of sugar might be caused by the orientational change in the collagen-attaching PG from orthogonal to parallel when the fibrils are entering the calcified zone.