The retina-specific basigin isoform does not induce IL-6 expression in mouse monocytes.

IF 1.8 3区 医学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY Molecular Vision Pub Date : 2023-01-01
Abigail D Solstad, Josephine M Brown, Judith D Ochrietor
{"title":"The retina-specific basigin isoform does not induce IL-6 expression in mouse monocytes.","authors":"Abigail D Solstad,&nbsp;Josephine M Brown,&nbsp;Judith D Ochrietor","doi":"","DOIUrl":null,"url":null,"abstract":"<p><strong>Purpose: </strong>Basigin gene products are positioned on adjacent cell types in the neural retina and are thought to compose a lactate metabolon important for photoreceptor cell function. The Ig0 domain of basigin isoform 1 (basigin-1) is highly conserved throughout evolution, which suggests a conserved function. It has been suggested that the Ig0 domain has proinflammatory properties, and it is hypothesized to interact with basigin isoform 2 (basigin-2) for cell adhesion and lactate metabolon formation. Therefore, the purpose of the present study was to determine whether the Ig0 domain of basigin-1 binds to basigin-2 and whether the region of the domain used for binding is also used to stimulate interleukin-6 (IL-6) expression.</p><p><strong>Methods: </strong>Binding was assessed using recombinant proteins corresponding to the Ig0 domain of basigin-1 and endogenously expressed basigin-2 from mouse neural retina and brain protein lysates. The proinflammatory properties of the Ig0 domain were analyzed with exposure of the recombinant proteins to the mouse monocyte RAW 264.7 cell line and subsequent measurement of the IL-6 concentration in the culture medium via enzyme-linked immunosorbent assay (ELISA).</p><p><strong>Results: </strong>The data indicate that the Ig0 domain interacts with basigin-2 through a region within the amino half of the domain and that the Ig0 domain does not stimulate the expression of IL-6 in mouse cells in vitro.</p><p><strong>Conclusions: </strong>The Ig0 domain of basigin-1 binds to basigin-2 in vitro. In addition, contrary to previous reports, there was no evidence that the Ig0 domain potentiates IL-6 expression in a mouse monocyte cell line in vitro. However, it is possible that the Ig0 domain stimulates the expression of proinflammatory cytokines other than IL-6, or that the potential involvement of the Ig0 domain of basigin-1 in the acute inflammatory response is dependent on species.</p>","PeriodicalId":18866,"journal":{"name":"Molecular Vision","volume":"29 ","pages":"13-24"},"PeriodicalIF":1.8000,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b8/73/mv-v29-13.PMC10243675.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular Vision","FirstCategoryId":"3","ListUrlMain":"","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Purpose: Basigin gene products are positioned on adjacent cell types in the neural retina and are thought to compose a lactate metabolon important for photoreceptor cell function. The Ig0 domain of basigin isoform 1 (basigin-1) is highly conserved throughout evolution, which suggests a conserved function. It has been suggested that the Ig0 domain has proinflammatory properties, and it is hypothesized to interact with basigin isoform 2 (basigin-2) for cell adhesion and lactate metabolon formation. Therefore, the purpose of the present study was to determine whether the Ig0 domain of basigin-1 binds to basigin-2 and whether the region of the domain used for binding is also used to stimulate interleukin-6 (IL-6) expression.

Methods: Binding was assessed using recombinant proteins corresponding to the Ig0 domain of basigin-1 and endogenously expressed basigin-2 from mouse neural retina and brain protein lysates. The proinflammatory properties of the Ig0 domain were analyzed with exposure of the recombinant proteins to the mouse monocyte RAW 264.7 cell line and subsequent measurement of the IL-6 concentration in the culture medium via enzyme-linked immunosorbent assay (ELISA).

Results: The data indicate that the Ig0 domain interacts with basigin-2 through a region within the amino half of the domain and that the Ig0 domain does not stimulate the expression of IL-6 in mouse cells in vitro.

Conclusions: The Ig0 domain of basigin-1 binds to basigin-2 in vitro. In addition, contrary to previous reports, there was no evidence that the Ig0 domain potentiates IL-6 expression in a mouse monocyte cell line in vitro. However, it is possible that the Ig0 domain stimulates the expression of proinflammatory cytokines other than IL-6, or that the potential involvement of the Ig0 domain of basigin-1 in the acute inflammatory response is dependent on species.

Abstract Image

Abstract Image

Abstract Image

分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
视网膜特异性basigin亚型不诱导IL-6在小鼠单核细胞中的表达。
目的:Basigin基因产物位于神经视网膜的邻近细胞类型上,被认为是构成对光感受器细胞功能重要的乳酸代谢。盆地蛋白异构体1 (basigin-1)的Ig0结构域在整个进化过程中高度保守,表明其具有保守功能。研究表明,Ig0结构域具有促炎特性,并可能与盆状蛋白2 (basigin-2)相互作用,促进细胞粘附和乳酸代谢形成。因此,本研究的目的是确定basigin-1的Ig0结构域是否与basigin-2结合,以及用于结合的结构域区域是否也用于刺激白细胞介素-6 (IL-6)的表达。方法:使用basigin-1 Ig0结构域对应的重组蛋白和小鼠神经视网膜和脑蛋白裂解物内源性表达的basigin-2来评估其结合情况。将重组蛋白暴露于小鼠单核细胞RAW 264.7细胞系,随后通过酶联免疫吸附试验(ELISA)测定培养基中IL-6的浓度,分析Ig0结构域的促炎特性。结果:数据表明Ig0结构域与basigin-2通过结构域的氨基部分的一个区域相互作用,并且Ig0结构域不刺激IL-6在体外小鼠细胞中的表达。结论:basigin-1的Ig0结构域在体外与basigin-2结合。此外,与先前的报道相反,没有证据表明Ig0结构域在体外小鼠单核细胞系中增强IL-6的表达。然而,Ig0结构域有可能刺激除IL-6以外的促炎细胞因子的表达,或者basigin-1的Ig0结构域在急性炎症反应中的潜在参与依赖于物种。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Molecular Vision
Molecular Vision 生物-生化与分子生物学
CiteScore
4.40
自引率
0.00%
发文量
25
审稿时长
1 months
期刊介绍: Molecular Vision is a peer-reviewed journal dedicated to the dissemination of research results in molecular biology, cell biology, and the genetics of the visual system (ocular and cortical). Molecular Vision publishes articles presenting original research that has not previously been published and comprehensive articles reviewing the current status of a particular field or topic. Submissions to Molecular Vision are subjected to rigorous peer review. Molecular Vision does NOT publish preprints. For authors, Molecular Vision provides a rapid means of communicating important results. Access to Molecular Vision is free and unrestricted, allowing the widest possible audience for your article. Digital publishing allows you to use color images freely (and without fees). Additionally, you may publish animations, sounds, or other supplementary information that clarifies or supports your article. Each of the authors of an article may also list an electronic mail address (which will be updated upon request) to give interested readers easy access to authors.
期刊最新文献
Erratum: A method for gene knockdown in the retina using a lipid-based carrier. Increased inflammatory mediators in the ocular surface tissue in keratoconus. Retraction: Swati Arora, Nagendra Verma. Exosomal microRNAs as potential biomarkers and therapeutic targets in corneal diseases. Molecular Vision 2024; 30:92-106. Complement C3 is downregulated following ranibizumab intervention in experimental central retinal vein occlusion. A potential novel role of the R36P mutation in CRYGD in congenial cataract.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1