Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues.
Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues.
复制标题
硫酸皮肤素蛋白多糖 (DS-PGII) 在软骨中的定位以及其他组织中免疫相关物种的存在。
DOI：
10.1177/34.5.3701029
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
L. Rosenberg
中科院分区：
文献类型：
--
作者：
A. Robin Poole;C. Webber;I. Pidoux;H. Choi;L. Rosenberg
从成年牛关节软骨中分离的富含硫酸皮肤素的小蛋白聚糖（DS-PGII）的核心蛋白相关表位的单克隆抗体（22）用于在牛关节软骨、软骨生长板和其他结缔组织中定位该分子或含有该表位的分子。使用间接的方法，采用过氧化物酶标记的猪抗小鼠免疫球蛋白G，DS-PGII被证明主要存在于成人关节髁软骨的掌-指关节的浅区。在胎儿关节和骺软骨中，分子均匀分布在整个基质中。到大约10月龄时，它主要局限于关节软骨的浅表区和中间区以及深层的区域间和细胞周围基质。在胎儿的初级生长板中未检测到DS-PGII，但在增殖区中除外，在增殖区中有时存在痕量DS-PGII。相反，它存在于整个相邻的基质发育骺软骨。在干骺端的骨小梁中，在脱钙类骨质和紧邻成骨细胞的骨中观察到DS-PGII的强染色。在皮肤、肌腱和韧带以及主动脉外膜和皮肤中较小动脉血管的胶原纤维上也观察到染色。这些观察结果表明，DS-PGII和/或含有该表位的分子广泛分布在胶原组织中，其中该分子与胶原原纤维密切相关;在成人软骨中，这种相关性主要限于在关节表面的浅表区中发现的狭窄的平行原纤维阵列。从它的密切联系和其他研究，这种分子可能在决定胶原纤维的大小和拉伸性能中发挥重要作用;它也可能参与类骨质的钙化，但不参与软骨的钙化。
A monoclonal antibody to a core-protein-related epitope of a small dermatan sulfate-rich proteoglycan (DS-PGII) isolated from adult bovine articular cartilage (22) was used to localize this molecule, or molecules containing this epitope, in bovine articular cartilages, in cartilage growth plate, and in other connective tissues. Using an indirect method employing peroxidase-labeled pig anti-mouse immunoglobulin G, DS-PGII was shown to be present mainly in the superficial zone of adult articular condylar cartilage of the metacarpal-phalangeal joint. In fetal articular and epiphyseal cartilages, the molecule was uniformly distributed throughout the matrix. By approximately 10 months of age it was confined mainly to the superficial and middle zones of articular cartilage and the inter-territorial and pericellular matrix of the deep zone. DS-PGII was not detected in the primary growth plate of the fetus except in the proliferative zone, where it was sometimes present in trace amounts. In contrast, it was present throughout the adjacent matrix of developing epiphyseal cartilage. In the trabeculae of the metaphysis, strong staining for DS-PGII was seen in decalcified osteoid and bone immediately adjacent to osteoblasts. Staining was also observed on collagen fibrils in skin, tendon, and ligament and in the adventitia of the aorta and of smaller arterial vessels in the skin. These observations indicate that DS-PGII and/or molecules containing this epitope are widely distributed in collagenous tissues, where the molecule is intimately associated with collagen fibrils; in adult cartilage this association is limited mainly to the narrow parallel arrays of fibrils which are found in the superficial zone at the articular surface. From its intimate association and other studies, this molecule may play an important role in determining the sizes and tensile properties of collagen fibrils; it may also be involved in the calcification of osteoid but not of cartilage.
从成熟牛关节软骨中分离硫酸皮肤素蛋白多糖。
DOI：
--
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Rosenberg,LC;Choi,HU;Tang,LH;Johnson,TL;Pal,S;Webber,C;Reiner,A;Poole,AR
通讯作者：
Poole,AR