Spatial organization of types I and II collagen in the canine meniscus
Spatial organization of types I and II collagen in the canine meniscus
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DOI：
10.1016/j.orthres.2004.06.016
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发表时间：
2005-01-01
影响因子：
2.8
通讯作者：
McDevitt, CA
中科院分区：
文献类型：
--
作者：
Kambic, HE;McDevitt, CA
膝关节的半月板是主要由I型胶原和少量的11型胶原组成的纤维软骨。用免疫组织化学和共聚焦显微镜观察了11型胶原在犬半月板中的分布及其与I型胶原的空间关系。取成年犬膝关节内侧和外侧半月板中段的背侧和冠状面切片，用链霉菌透明质酸裂解酶和细菌蛋白酶XXIV预消化。应用抗I型胶原（CP 17 L）、抗II型胶原（II-116133）的单克隆抗体和抗II型胶原多克隆抗体（AB 759）对透明关节软骨细胞外基质中的II型胶原进行染色，结果显示，透明关节软骨细胞外基质中的II型胶原呈弥漫性染色，无明显的空间结构。与此形成鲜明对比的是，半月板纤维软骨中的II型胶原染色为所有组织化的网络。II型胶原蛋白分布在整个半月板，除了包含血管的外区。半月板的冠状面和背侧染色显示I型胶原蛋白与II型胶原蛋白在特定部位共定位的环形纤维束。这些束被包裹在第二个组织的纤维系统的I型和II型胶原蛋白，也共定位。在冠状面的横截面上，环形原纤维束在第二系统的I型和II型胶原蛋白的网络所构成的间隙空间内作为点出现。共聚焦重叠显示，I型和II型胶原蛋白叠加，这表明两种胶原蛋白之间的空间接近。细胞局限于包裹纤维束的I型和II型胶原纤维。一个显着的特点，径向领带纤维是补丁的II型胶原蛋白没有共定位的I型collagen.Our的研究揭示了一个独特的网络的II型胶原蛋白纤维软骨的半月板，作为一个形态学的区别，透明软骨。(C)2004骨科研究学会。由爱思唯尔有限公司出版。保留所有权利。
The meniscus of the knee joint is a fibrocartilage mainly composed of type I collagen and smaller amounts of type 11 collagen. The distribution of type 11 collagen in the canine meniscus and its spatial relationship to type I collagen was examined by immunohistochemistry and confocal microscopy.Dorsal and coronal slices of the mid-section of medial and lateral menisci from the knee joints of skeletally mature dogs were predigested with Streptomyces hyaluronate lyase and bacterial Protease enzyme XXIV. Monoclonal antibodies against type I collagen (CP17L) and type II collagen (II-116133) and an anti-type II collagen polyclonal antibody (AB759) were employed.The staining for type II collagen in the extracellular matrix of hyaline articular cartilage was diffuse without any identifiable spatial organization. In striking contrast, type II collagen in the fibrocartilage of the meniscus stained as ail organized network. Type II collagen was distributed throughout the meniscus with the exception of the outer zone containing the blood vessels.Coronal and dorsal staining of the meniscus showed bundles of circumferential fibrils of type I that colocalized with type II collagen in specific sites. These bundles were enwrapped in a second organizational fibrillar system of types I and II collagen that also colocalized. Bundles of circumferential fibrils appeared in cross-section in coronal sections as dots within the interstitial spaces framed by the network of types I and II collagen of the second system. Confocal overlays showed that types I and II collagens were superimposed, suggesting a close spatial proximity between the two collagens. The cells were confined to the types I and II collagen fibrils that enwrapped the bundles. A striking feature of the radial tie fibers was patches of type II collagen without colocalized type I collagen.Our study reveals a unique network of type II collagen in fibrocartilage of the meniscus that serves as a morphological distinction between fibro- and hyaline cartilage. (C) 2004 Orthopaedic Research Society. Published by Elsevier Ltd. All rights reserved.