Antoniou J, Goudsouzian N M, Heathfield T F, Winterbottom N, Steffen T, Poole A R, Aebi M, Alini M
Orthopaedic Research Laboratory, Royal Victoria Hospital, McGill University, Montreal, Quebec, Canada.
Spine (Phila Pa 1976). 1996 May 15;21(10):1153-61. doi: 10.1097/00007632-199605150-00006.
The authors measured concentrations of specific molecules reflecting matrix synthesis and degradation in 121 human endplates and correlated them with aging and grade of degeneration.
Abnormal endplate development has been implicated in many spinal abnormalities, yet little is known about endplate matrix component turnover.
Techniques are available to perform an in situ investigation of matrix component turnover with aging and degeneration.
Newly synthesized aggrecan and Type I and Type II procollagens were measured with recently developed immunoassays. Percentage of denatured Type II collagen was assessed with a new enzyme-linked immunosorbent inhibition assay.
Synthesis in endplates, measured by content of an aggrecan marker (846) and content of Types I and II procollagen markers (CPI and CPII), is highest in the neonatal and 2- to 5-year age groups and steadily diminishes with increasing age. However, in the oldest age group and in highly degenerated discs, the CPI epitope level increased significantly. Percentage of denatured Type II collagen, assessed by the presence of an epitope exposed with the cleavage of Type II collagen, increased from the neonatal to the 2- to 5-year age groups. The percentage progressively decreased with increasing age. However, it significantly increased in endplates from highly degenerated discs.
The authors identified three matrix turnover phases, related to age and grade of degeneration. Phase I (growth) is characterized by active synthesis of matrix molecules and active denaturation of Type II collagen. Phase II (aging and maturation) is distinguished by a drop in synthetic activity and a reduction in denaturation of Type II collagen. Phase III (degenerative) is illustrated by an increase in Type II collagen denaturation and Type I procollagen synthesis, both related to grade of tissue degeneration.
作者测量了121个人类终板中反映基质合成和降解的特定分子浓度，并将其与衰老及退变程度相关联。
异常的终板发育与许多脊柱异常有关，但关于终板基质成分的更新情况却知之甚少。
现有技术可用于对基质成分随衰老和退变的原位研究。
采用最近开发的免疫测定法测量新合成的聚集蛋白聚糖以及I型和II型前胶原。用一种新的酶联免疫吸附抑制测定法评估变性II型胶原的百分比。
通过聚集蛋白聚糖标记物（846）的含量以及I型和II型前胶原标记物（CPI和CPII）的含量来衡量，终板中的合成在新生儿组以及2至5岁年龄组中最高，并随着年龄的增长而稳步下降。然而，在最年长的年龄组以及高度退变的椎间盘终板中，CPI表位水平显著升高。通过II型胶原裂解后暴露的表位的存在来评估，变性II型胶原的百分比从新生儿组到2至5岁年龄组有所增加。该百分比随着年龄的增长而逐渐下降。然而，在高度退变椎间盘的终板中其显著增加。
作者确定了与年龄和退变程度相关的三个基质更新阶段。第一阶段（生长）的特征是基质分子的活跃合成以及II型胶原的活跃变性。第二阶段（衰老和成熟）的特点是合成活性下降以及II型胶原变性减少。第三阶段（退变）表现为II型胶原变性增加以及I型前胶原合成增加，两者均与组织退变程度相关。
