■在鸟类和其他物种中,粘蛋白(MUC)在胃肠道(GIT)中起着至关重要的作用,构成一大组O-糖基化糖蛋白,是糖结合蛋白。MUC以两种形式存在:(1)膜附着在细胞表面以抵御外部威胁;(2)可拆卸,可溶形式的凝胶形成蛋白。在鹌鹑GIT,表达的MUC的具体类型仍然是未知的。我们调查了MUC1和MUC4MUC在伊拉克普通鹌鹑GIT中的表达,并对鹌鹑品种的所有已知MUC类型进行了网络和结构分析。
■使用来自10只鹌鹑的新鲜小肠和大肠样品进行MUC1和MUC4的组织学和基因表达分析。使用STRING数据库,Chimera软件,和PrankWeb-配体结合位点预测工具,对所有报道类型的鹌鹑MUC进行了网络和结构分析。
■鹌鹑的大多数肠道MUC是酸性的,通过阿尔辛蓝和高碘酸希夫染色检测到很少的中性MUC。酸性MUC在十二指肠中表达更多,回肠,盲肠,和结肠,而中性MUC在空肠中表达更多。MUC1和MUC4信使RNA在空肠和结肠中的表达显著高于十二指肠和回肠。对网络的分析表明,MUC1、15、16和24形成了同源网络,而MUC2、4、5和6形成异源网络。特定的MUC组合,包括MUC5A-MUC6、MUC5A-MUC5B、和MUC5B-MUC6显示出更高的分子间氢键形成亲和力。MUC15、MUC16和MUC24显示与其他MUC类型的最小相互作用。在分析的MUC中,MUC5B,MUC6具有最高的结合概率,而MUC2,MUC4和MUC5A显示较低的概率,尽管有更多的结合位点。
■这项研究的结果为鹌鹑“MUCs”的组成提供了重要的见解,表达式,网络互动,和结合位点,推进胃肠道生理学中MUC相关过程的知识及其与胃肠道疾病的潜在联系。
UNASSIGNED: In avian and other species, mucins (MUCs) play a crucial role in the gastrointestinal tract (GIT), and constitute a large group of O-glycosylated glycoproteins, are glycoconjugate proteins. MUCs present in two forms: (1) membrane-attached on cell surfaces to repel external threats and (2) detachable, gel-forming proteins in the soluble form. In quail GIT, the specific types of MUCs that are expressed remain largely unknown. We investigated the expression of MUC1 and MUC4 MUCs in the GIT of Iraqi common quails and conducted network and structural analyses of all known MUC types across quail breeds.
UNASSIGNED: Histological and gene expression analyses of MUC1 and MUC4 were conducted using fresh small intestine and large intestine samples from 10 quails. Using the STRING Database, Chimera software, and PrankWeb-ligand binding site prediction tool, network and structural analyses of all reported types of quail MUCs were conducted.
UNASSIGNED: Most intestinal MUCs in quails were acidic, with few neutral MUCs detectable through Alcian blue and periodic acid-schiff stains. Acidic MUCs were more expressed in the duodenum, ileum, cecum, and colon, whereas neutral MUCs were more expressed in the jejunum. MUC1 and MUC4 messenger RNA expression was significantly higher in the jejunum and colon than in the duodenum and ileum. The analysis of the network revealed that MUC 1, 15, 16, and 24 formed homologous networks, while MUC 2, 4, 5, and 6 formed heterologous networks. Specific MUC combinations, including MUC5A-MUC6, MUC5A-MUC5B, and MUC5B-MUC6, show higher intermolecular hydrogen bond formation affinity. MUC15, MUC16, and MUC24 showed minimal interaction with other MUC types. Among the analyzed MUCs, MUC5B, and MUC6 had the highest probability for binding, while MUC2, MUC4, and MUC5A showed lower probabilities despite greater numbers of binding sites.
UNASSIGNED: This study\'s results offer significant insights into quails\' MUCs\' composition, expression, network interactions, and binding sites, advancing knowledge of MUC-related processes in gastrointestinal physiology and their potential connection to gastrointestinal diseases.