Schollmeier G, Lahr-Eigen R, Lewandrowski K U
Department of Surgery, Faculty of Medicine, University of Ottawa, Ontario, Canada.
Spine (Phila Pa 1976). 2000 Nov 1;25(21):2736-41. doi: 10.1097/00007632-200011010-00004.
The spatial distribution of fiber-forming collagens in the anulus fibrosus was investigated in the complete longitudinal and horizontal sections of human lumbar intervertebral discs of seven individuals.
To obtain a more detailed structural definition of the anulus fibrosus because structural alterations of its collagen fiber network have been implicated in discal degeneration and other spinal pathologies.
Prior biochemical or immunofluorescence studies permitted only limited conclusions concerning the spatial distribution of the fiber-forming collagens in relation to anatomic structures because they were based on intraoperative tissue specimens or performed on incomplete sections of human intervertebral discs.
Complete human intervertebral discs with their adjacent vertebral bodies were fixed, decalcified, and embedded in paraffin. The intervertebral disc and its adjacent structures were reviewed in their entirety on one histologic slide. Monoclonal antibodies against human Types I, II, and III collagen were used for immunohistochemistry. A comparative analysis based on both immunohistochemical and histologic evaluation was performed.
Type I collagen was seen abundantly in the outer zone and outer lamellas of the inner zone of the anulus fibrosus. On longitudinal sections, the Type I collagen distribution took the shape of a wedge. On horizontal sections, the Type I collagen positive area took the shape of a ring that was wider anteriorly than posteriorly. This suggests that the three-dimensional shape of the Type I collagen-positive tissue in the anulus fibrosus can be described by a donut that is wider anteriorly than posteriorly. Type II collagen was present in the entire inner of the anulus fibrosus, but not in the outer zone. In addition, it was found in the cartilaginous endplates. Type III collagen showed some codistribution with Type II collagen, particularly in pericellular locations in areas of spondylosis, which was noted at the endplates, vertebral rim, and insertion sites of the anulus fibrosus.
These observations on the location of Types I and II collagen provide a more detailed structural definition of the anulus fibrosus, which may assist in further investigation of discal herniation.
在7例人类腰椎间盘的完整纵向和水平切片中，研究纤维形成性胶原在纤维环中的空间分布。
获得纤维环更详细的结构定义，因为其胶原纤维网络的结构改变与椎间盘退变及其他脊柱病变有关。
先前的生化或免疫荧光研究，由于基于术中组织标本或在人类椎间盘的不完整切片上进行，因此关于纤维形成性胶原相对于解剖结构的空间分布只能得出有限的结论。
将完整的人类椎间盘及其相邻椎体固定、脱钙并石蜡包埋。在一张组织学切片上对椎间盘及其相邻结构进行整体观察。使用抗人I、II和III型胶原的单克隆抗体进行免疫组织化学。基于免疫组织化学和组织学评估进行比较分析。
I型胶原在纤维环外层和内层的外层板层中大量存在。在纵向切片上，I型胶原分布呈楔形。在水平切片上，I型胶原阳性区域呈环形，前部比后部宽。这表明纤维环中I型胶原阳性组织的三维形状可以用一个前部比后部宽的甜甜圈来描述。II型胶原存在于纤维环的整个内层，但不在外层。此外，在软骨终板中也发现了II型胶原。III型胶原与II型胶原存在一些共分布，特别是在椎间隙变窄区域的细胞周围位置，在终板、椎体边缘和纤维环的插入部位可见。
这些关于I型和II型胶原位置的观察结果为纤维环提供了更详细的结构定义，这可能有助于进一步研究椎间盘突出症。
