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海参捕捉型结缔组织中与可逆性硬化相关的超微结构变化

Ultrastructural Changes Associated with Reversible Stiffening in Catch Connective Tissue of Sea Cucumbers.

作者信息

Tamori Masaki, Ishida Kinji, Matsuura Eri, Ogasawara Katsutoshi, Hanasaka Tomohito, Takehana Yasuhiro, Motokawa Tatsuo, Osawa Tokuji

机构信息

Department of Biological Sciences, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Meguro-ku, Tokyo, Japan.

The Center for Electron Microscopy & Bio-imaging Research, Central Research Laboratories, Iwate Medical University, Morioka, Iwate, Japan.

出版信息

PLoS One. 2016 May 18;11(5):e0155673. doi: 10.1371/journal.pone.0155673. eCollection 2016.

Abstract

The dermis of sea cucumbers is a catch connective tissue or a mutable collagenous tissue that shows rapid, large and reversible stiffness changes in response to stimulation. The main component of the dermis is the extracellular material composed of collagen fibrils embedded in a hydrogel of proteoglycans. The stiffness of the extracellular material determines that of the dermis. The dermis has three mechanical states: soft (Sa), standard (Sb) and stiff (Sc). We studied the ultrastructural changes associated with the stiffness changes. Transverse sections of collagen fibrils in the dermis showed irregular perimeters with electron-dense protrusions or arms that cross-bridged between fibrils. The number of cross-bridges increased in stiffer dermis. The distance between the fibrils was shorter in Sc than that in other states, which was in accord with the previous report that water exuded from the tissue in the transition Sb→Sc. The ultrastructure of collagen fibrils that had been isolated from the dermis was also studied. Fibrils aggregated by tensilin, which causes the transition Sa→Sb possibly through an increase in cohesive forces between fibrils, had larger diameter than those dispersed by softenin, which antagonizes the effect of tensilin. No cross-bridges were found in isolated collagen fibrils. From the present ultrastructural study we propose that three different mechanisms work together to increase the dermal stiffness. 1.Tensilin makes collagen fibrils stronger and stiffer in Sa→Sb through an increase in cohesive forces between subfibrils that constituted fibrils; 2. Cross-bridging by arms caused the fibrils to be a continuous network of bundles both in Sa→Sb and in Sb→Sc; 3. The matrix embedding the fibril network became stiffer in Sb→Sc, which was produced by bonding associated with water exudation.

摘要

海参的真皮是一种弹性结缔组织或可变胶原组织,能对刺激做出快速、大幅度且可逆的硬度变化。真皮的主要成分是细胞外物质,由嵌入蛋白聚糖水凝胶中的胶原纤维组成。细胞外物质的硬度决定了真皮的硬度。真皮有三种力学状态:柔软(Sa)、标准(Sb)和坚硬(Sc)。我们研究了与硬度变化相关的超微结构变化。真皮中胶原纤维的横切面显示出不规则的周长,有电子致密的突起或臂,这些突起或臂在纤维之间形成交叉桥。在更硬的真皮中,交叉桥的数量增加。Sc状态下纤维之间的距离比其他状态下更短,这与之前关于在Sb→Sc转变过程中组织渗出水分的报道一致。我们还研究了从真皮中分离出的胶原纤维的超微结构。由张力蛋白聚集的纤维,可能通过增加纤维之间的内聚力导致Sa→Sb转变,其直径比由软化蛋白分散的纤维更大,软化蛋白可拮抗张力蛋白的作用。在分离的胶原纤维中未发现交叉桥。从目前的超微结构研究中我们提出,三种不同的机制共同作用以增加真皮的硬度。1. 张力蛋白通过增加构成纤维的亚纤维之间的内聚力,使胶原纤维在Sa→Sb状态下更强更硬;2. 臂的交叉桥接使纤维在Sa→Sb和Sb→Sc状态下都成为连续的束状网络;3. 嵌入纤维网络的基质在Sb→Sc状态下变得更硬,这是由与水分渗出相关的结合作用产生的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ad0/4871580/a4fd73d2141b/pone.0155673.g001.jpg

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