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在环境温度和预计本世纪末温度条件下饲养的幼幼年小星鲨胸鳍上的凝集素结合。

Lectin binding to pectoral fin of neonate little skates reared under ambient and projected-end-of-century temperature regimes.

机构信息

Department of Biology and Marine Biology, University of North Carolina at Wilmington, Wilmington, North Carolina, USA.

College of Agricultural Sciences, Coastal Oregon Marine Experiment Station, Oregon State University, Corvallis, Oregon, USA.

出版信息

J Morphol. 2024 May;285(5):e21698. doi: 10.1002/jmor.21698.

DOI:10.1002/jmor.21698
PMID:38669130
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11064730/
Abstract

The glycosylation of macromolecules can vary both among tissue structural components and by adverse conditions, potentially providing an alternative marker of stress in organisms. Lectins are proteins that bind carbohydrate moieties and lectin histochemistry is a common method to visualize microstructures in biological specimens and diagnose pathophysiological states in human tissues known to alter glycan profiles. However, this technique is not commonly used to assess broad-spectrum changes in cellular glycosylation in response to environmental stressors. In addition, the binding of various lectins has not been studied in elasmobranchs (sharks, skates, and rays). We surveyed the binding tissue structure specificity of 14 plant-derived lectins, using both immunoblotting and immunofluorescence, in the pectoral fins of neonate little skates (Leucoraja erinacea). Skates were reared under present-day or elevated (+5°C above ambient) temperature regimes and evaluated for lectin binding as an indicator of changing cellular glycosylation and tissue structure. Lectin labeling was highly tissue and microstructure specific. Dot blots revealed no significant changes in lectin binding between temperature regimes. In addition, lectins only detected in the elevated temperature treatment were Canavalia ensiformis lectin (Concanavalin A) in spindle cells of muscle and Ricinus communis agglutinin in muscle capillaries. These results provide a reference for lectin labeling in elasmobranch tissue that may aid future investigations.

摘要

糖基化的大分子可以在组织结构成分之间变化,也可以在不利条件下变化,这可能为生物体内的应激提供了另一种替代标志物。凝集素是一种能结合碳水化合物的蛋白质,而凝集素组织化学是一种常见的方法,可以在生物标本中可视化微观结构,并诊断已知改变聚糖谱的人类组织的病理生理状态。然而,这种技术通常不用于评估细胞糖基化对环境胁迫的广谱变化。此外,各种凝集素的结合在软骨鱼类(鲨鱼、鳐鱼和鳐鱼)中尚未得到研究。我们使用免疫印迹和免疫荧光法,在新生儿小鳐鱼(Leucoraja erinacea)的胸鳍中调查了 14 种植物来源的凝集素的结合组织结构特异性。鳐鱼在当今或升高(比环境温度高+5°C)的温度条件下饲养,并评估了凝集素结合情况,作为细胞糖基化和组织结构变化的指标。凝集素标记具有高度的组织和微观结构特异性。斑点印迹显示温度条件之间的凝集素结合没有显著变化。此外,仅在升高的温度处理中检测到的凝集素是纺锤形细胞中的刀豆球蛋白(Concanavalin A)和肌肉毛细血管中的蓖麻凝集素。这些结果为软骨鱼类组织中的凝集素标记提供了参考,可能有助于未来的研究。

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