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软骨中 XII 型胶原蛋白的发育分布:与关节软骨和生长板的关联

Developmental distribution of collagen type XII in cartilage: association with articular cartilage and the growth plate.

作者信息

Gregory K E, Keene D R, Tufa S F, Lunstrum G P, Morris N P

机构信息

Shriners Hospitals for Children, Portland, Oregon 97201, USA.

出版信息

J Bone Miner Res. 2001 Nov;16(11):2005-16. doi: 10.1359/jbmr.2001.16.11.2005.

Abstract

Collagen type XII is a member of the fibril-associated collagens and is characterized by a short triple-helical domain with three extended noncollagenous NC3 domains. Previous studies suggested that collagen XII is a component of cartilage but little is known about its spatial-temporal distribution. This study uses a polyclonal antibody to the purified NC3 domain to investigate its developmental distribution in rat forelimb. Collagen XII was present at the joint interzone on embryonic day 16 (E16d) and restricted to the presumptive articular cartilage by E18d. Labeling of the articular surface intensified as development progressed postnatally (day 1 [1d] to 28d) and extended approximately six cell diameters deep. In juvenile rats, collagen XII antibodies also labeled the longitudinal and transverse septa of stacked chondrocytes in the growth plate. However, collagen XII was not associated at any developmental stage with the cartilaginous secondary ossification center and was only weakly expressed in epiphyseal cartilage. Ultrastructural localization of the NC3 domain epitope showed labeling of the surface of collagen II fibrils both in tissue and in isolated fibrils. The results presented provide further evidence that articular cartilage differs substantially from the underlying epiphyseal cartilage and that different chondrocytic developmental fates are reflected in the composition of their extracellular matrix starting early in development. In addition, collagen XII was distributed in areas of cartilage with more organized fibril orientation and may have a role in promoting alignment or stabilizing such an organization, thereby creating a matrix capable of withstanding load-bearing forces.

摘要

Ⅻ型胶原蛋白是原纤维相关胶原蛋白的成员之一,其特征在于具有短的三螺旋结构域以及三个延伸的非胶原蛋白NC3结构域。先前的研究表明,Ⅻ型胶原蛋白是软骨的一个组成部分,但对其时空分布了解甚少。本研究使用针对纯化的NC3结构域的多克隆抗体来研究其在大鼠前肢中的发育分布。Ⅻ型胶原蛋白在胚胎第16天(E16d)时出现在关节中间带,并在E18d时局限于推测的关节软骨。随着出生后发育进程(第1天[1d]至第28天)的推进,关节表面的标记增强,并延伸至大约六个细胞直径的深度。在幼年大鼠中,Ⅻ型胶原蛋白抗体还标记了生长板中堆叠软骨细胞的纵向和横向隔。然而,Ⅻ型胶原蛋白在任何发育阶段都与软骨性二级骨化中心无关,并且仅在骨骺软骨中弱表达。NC3结构域表位的超微结构定位显示,在组织和分离的原纤维中,Ⅱ型胶原原纤维表面均有标记。所呈现的结果进一步证明,关节软骨与下方的骨骺软骨有很大不同,并且不同的软骨细胞发育命运在发育早期就反映在其细胞外基质的组成中。此外,Ⅻ型胶原蛋白分布于原纤维取向更有序的软骨区域,可能在促进排列或稳定这种组织结构方面发挥作用,从而形成能够承受负荷力的基质。

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