Abstract

In order to investigate the morphology of ultramicrostructure in molecular level of nucleus herniation, the authors studied the ultramicrostructure of three cases of nucleus herniation of lumbar intervertebral disc and one case of normal nucleus pulposus of fresh corpse by using atomic force microscopy. The results showed that the arrangements of collagen bundle, collagen fiber and procollagen fiber were different between the two conditions, and the morphology of molecular particles of proteoglycan in nucleus herniation was different from that in the normal condition. In the condition of nucleus herniation, the collagen fiber formed procollagen fiber reticular meshes adhering to the molecules of protein and proteoglycan, and the DNA adhering to the monochain of RNA in fiber cell nuclei, in the form of bichain and multichain three dimensions helix structures. The banded structure (64-78 nm) of the procollagen fiber, the collagenation and calcification of the degenerated nucleus pulposuses, the quantity of which was significantly greater than normal (P<0.05) indicated that the chronic injury of lumbar intervertebral nucleus pulposuses gave rise to the injury and the break of the collagen fiber which resulted in twist or tangle phenomenon so that nucleus pulposuses lost their normal resistance strength.

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