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II 型和 VI 型胶原蛋白在鼻软骨和关节软骨中的分布及白介素-1α对其分布的影响。

Type II and VI collagen in nasal and articular cartilage and the effect of IL-1alpha on the distribution of these collagens.

机构信息

Department of Periodontology, Academic Center for Dentistry Amsterdam (ACTA), University of Amsterdam and VU University, Research Institute MOVE, Amsterdam, The Netherlands.

出版信息

J Mol Histol. 2010 Feb;41(1):9-17. doi: 10.1007/s10735-010-9257-7. Epub 2010 Mar 6.

Abstract

The distribution of type II and VI collagen was immunocytochemically investigated in bovine articular and nasal cartilage. Cartilage explants were used either fresh or cultured for up to 4 weeks with or without interleukin 1alpha (IL-1alpha). Sections of the explants were incubated with antibodies for both types of collagen. Microscopic analyses revealed that type II collagen was preferentially localized in the interchondron matrix whereas type VI collagen was primarily found in the direct vicinity of the chondrocytes. Treatment of the sections with hyaluronidase greatly enhanced the signal for both types of collagen. Also in sections of explants cultured with IL-1alpha a higher level of labeling of the collagens was found. This was apparent without any pre-treatment with hyaluronidase. Under the influence of IL-1alpha the area positive for type VI collagen that surrounded the chondrocytes broadened. Although the two collagens in both types of cartilage were distributed similarly, a remarkable difference was the higher degree of staining of type VI collagen in articular cartilage. Concomitantly we noted that digestion of this type of cartilage hardly occurred in the presence of IL-1alpha whereas nasal cartilage was almost completely degraded within 18 days of culture. Since type VI collagen is known to be relatively resistant to proteolysis we speculate that the higher level of type VI collagen in articular cartilage is important in protecting cartilage from digestion.

摘要

本研究采用免疫细胞化学方法观察了Ⅱ型和Ⅵ型胶原在牛关节和鼻软骨中的分布。分别对新鲜软骨和培养 4 周的软骨进行实验,培养过程中可加入或不加入白细胞介素 1α(IL-1α)。将软骨标本切片后与两种胶原的抗体孵育,显微镜观察发现Ⅱ型胶原主要分布在软骨细胞间基质,而Ⅵ型胶原主要位于软骨细胞周围。用透明质酸酶处理后,两种胶原的信号均显著增强。在加入 IL-1α的培养软骨标本中,胶原的染色水平也显著升高,且无需透明质酸酶预处理。在 IL-1α的作用下,围绕软骨细胞的Ⅵ型胶原阳性区域变宽。尽管两种软骨中的两种胶原分布相似,但关节软骨中Ⅵ型胶原的染色程度明显更高。同时我们注意到,在 IL-1α存在的情况下,这种类型的软骨几乎不会被消化,而鼻软骨在培养 18 天后几乎完全降解。由于已知Ⅵ型胶原相对不易被蛋白水解酶降解,我们推测关节软骨中Ⅵ型胶原水平较高对于保护软骨免受消化至关重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d867/2852591/9b97635d086a/10735_2010_9257_Fig1_HTML.jpg

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