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评估 Annexin A2/S100A10 复合物在人胎盘细胞中的定位。

Assessment of the cellular localisation of the annexin A2/S100A10 complex in human placenta.

机构信息

School of Pharmacy, Centre for Biomolecular Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.

Department of Histology, Minia Faculty of Medicine, Minia, Egypt.

出版信息

J Mol Histol. 2018 Oct;49(5):531-543. doi: 10.1007/s10735-018-9791-2. Epub 2018 Aug 24.

DOI:10.1007/s10735-018-9791-2
PMID:30143909
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6182581/
Abstract

The AnxA2/S100A10 complex has been implicated in various placental functions but although the localisation of these proteins individually has been studied, there is no information about the localisation of their complex in situ at the cellular level. Using the proximity ligation technique, we have investigated the in situ localisation of AnxA2/S100A10 complex in the placenta and have compared this with the location patterns of the individual proteins. High levels of expression of AnxA2/S100A10 complexes were observed in the amniotic membrane and in blood vessel endothelial cells. Lower levels were detected in the brush border area of the syncytium and in the trophoblasts. Immunohistochemical analysis of AnxA2 and S100A10 individually revealed broadly similar patterns of localisation. The brush border staining pattern suggests that in this location at least some of the AnxA2 is not in complex with S100A10. The formal location of the AnxA2/S100A10 complex is compatible with a role in cell-cell interaction, intracellular transport and secretory processes and regulation of cell surface proteases, implying contributions to membrane integrity, nutrient exchange, placentation and vascular remodelling in different parts of the placenta. Future applications will allow specific assessment of the association of the complex with pathophysiological disorders.

摘要

annexin A2/S100A10 复合物参与多种胎盘功能，但尽管已研究了这些蛋白质各自的定位，但关于其复合物在细胞水平上的原位定位尚无信息。我们使用邻近连接技术研究了胎盘中原位 annexin A2/S100A10 复合物的定位，并将其与单个蛋白质的定位模式进行了比较。在羊膜和血管内皮细胞中观察到 annexin A2/S100A10 复合物的高表达水平。在合体滋养层的刷状缘区域和滋养层中检测到较低水平。对 annexin A2 和 S100A10 进行单独的免疫组织化学分析显示出大致相似的定位模式。刷状缘染色模式表明，在该位置，至少一些 annexin A2 未与 S100A10 形成复合物。 annexin A2/S100A10 复合物的正式定位与其在细胞-细胞相互作用、细胞内运输和分泌过程以及细胞表面蛋白酶调节中的作用一致，这意味着其对膜完整性、营养交换、胎盘形成和血管重塑的贡献在胎盘的不同部位。未来的应用将允许对复合物与病理生理紊乱的关联进行特定评估。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/7c6e756c6f27/10735_2018_9791_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/4a013469c8f7/10735_2018_9791_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/18e6c9c1b901/10735_2018_9791_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/ca6eaf40e197/10735_2018_9791_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/734ea8754671/10735_2018_9791_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/71e80a75a109/10735_2018_9791_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/3c37fc46753d/10735_2018_9791_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/7c6e756c6f27/10735_2018_9791_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/4a013469c8f7/10735_2018_9791_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/18e6c9c1b901/10735_2018_9791_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/ca6eaf40e197/10735_2018_9791_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/734ea8754671/10735_2018_9791_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/71e80a75a109/10735_2018_9791_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/3c37fc46753d/10735_2018_9791_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c84e/6182581/7c6e756c6f27/10735_2018_9791_Fig7_HTML.jpg

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