Milz S, McNeilly C, Putz R, Ralphs J R, Benjamin M
Anatomische Anstalt, Ludwig-Maximilians-Universität, München, Germany.
Anat Rec. 1998 Oct;252(2):264-70. doi: 10.1002/(SICI)1097-0185(199810)252:2<264::AID-AR11>3.0.CO;2-L.
The extensor tendons of the fingers and toes form part of the capsule of the interphalangeal joint and press against the proximal phalanx during flexion. Previous work on the fingers has shown that there is a "sesamoid" fibrocartilage on the deep surface of each tendon that labels immunohistochemically for a variety of glycosaminoglycans and collagens. However, we know little about the molecular composition of the tendon in the toes. This question is of special interest, because the mechanics of the interphalangeal joints differ in the upper and lower limbs-the toes balance the forefoot, distribute load during the gait cycle, and transmit the pull of larger muscles. This means that their extensor tendons are more often under higher tension than those in the fingers. Here, we report the presence of an equivalent fibrocartilage and compare its immunolabelling characteristics in all the toes. Six forefeet were removed from elderly cadavers, and the interphalangeal (IP) joints were fixed in 90% methanol. The extensor tendon and its enthesis were dissected out from the IP joint of the big toe and from the proximal interphalangeal (PIP) joint of all lesser toes, decalcified, cryosectioned, and immunolabelled with a panel of monoclonal and polyclonal antibodies for type I, II, III, and VI collagens; chondroitin 4 and 6 sulphates; and dermatan and keratan sulphate. Antibody binding was detected with the Vectastain ABC Elite avidin-biotin-peroxidase kit (Vector Laboratories, Burlingame, CA). The extensor tendon in all the toes had a metachromatic, sesamoid fibrocartilage on its deep surface that immunolabelled for all glycosaminoglycans and for type I, III, and VI collagens. Labelling for type II collagen was seen in the sesamoid fibrocartilage of all toes but was particularly characteristic of the 2nd through 5th toes. The immunolabelling patterns of the enthesis fibrocartilage were similar in all toes and to results reported previously for fingers. The normal occurrence of type II collagen in the sesamoid fibrocartilage of the 2nd through 5th toes is in contrast to our published data on the fingers. The finding can be related to the more constant loading of the tendon in the toes. The greater prominence of type II collagen in the sesamoid fibrocartilage of the 2nd through 5th toes could be related to a difference in joint position during walking between the 1st toe and the 2nd through 5th toes--the PIP joints of the latter are usually more flexed than the IP joint of the former.
手指和脚趾的伸肌腱构成指间关节囊的一部分,并在屈曲时压迫近节指骨。先前对手指的研究表明,每条肌腱的深面都有一个“籽骨样”纤维软骨,通过免疫组织化学方法可标记多种糖胺聚糖和胶原蛋白。然而,我们对脚趾肌腱的分子组成知之甚少。这个问题特别引人关注,因为指间关节的力学机制在上下肢有所不同——脚趾平衡前足,在步态周期中分配负荷,并传递较大肌肉的拉力。这意味着它们的伸肌腱比手指的伸肌腱更常处于更高的张力之下。在此,我们报告了一种等效纤维软骨的存在,并比较了其在所有脚趾中的免疫标记特征。从老年尸体上取下六只前足,将指间(IP)关节固定在90%甲醇中。从大脚趾的IP关节以及所有小脚趾的近端指间(PIP)关节中解剖出伸肌腱及其附着点,进行脱钙、冷冻切片,并用一组针对I型、II型、III型和VI型胶原蛋白、硫酸软骨素4和6、硫酸皮肤素和硫酸角质素的单克隆和多克隆抗体进行免疫标记。使用Vectastain ABC Elite抗生物素蛋白-生物素-过氧化物酶试剂盒(Vector Laboratories,加利福尼亚州伯林盖姆)检测抗体结合情况。所有脚趾的伸肌腱在其深面都有一个异染性的籽骨样纤维软骨,可对所有糖胺聚糖以及I型、III型和VI型胶原蛋白进行免疫标记。在所有脚趾的籽骨样纤维软骨中都可见到II型胶原蛋白的标记,但在第2至第5趾中尤为明显。附着点纤维软骨的免疫标记模式在所有脚趾中相似,且与先前报道的手指结果一致。第2至第5趾籽骨样纤维软骨中II型胶原蛋白的正常出现与我们之前发表的关于手指的数据形成对比。这一发现可能与脚趾肌腱更持续的负荷有关。第2至第5趾籽骨样纤维软骨中II型胶原蛋白更为突出可能与行走时第1趾与第2至第5趾之间关节位置的差异有关——后者的PIP关节通常比前者的IP关节更屈曲。