少突胶质细胞 Slc48a1(Hrg1)编码髓鞘完整性所需的功能性血红素转运体。

IF 5.4 2区 医学 Q1 NEUROSCIENCES
Glia Pub Date : 2025-02-01 Epub Date: 2024-11-06 DOI:10.1002/glia.24641
John H Stockley, Adrien M Vaquie, Zhaoyang Xu, Theresa Bartels, Gregory D Jordan, Staffan Holmqvist, Simon Gunter, Guy Lam, Daniel Yamamoto, Rini H Pek, Ian G Chambers, Andrew S Rock, Myfanwy Hill, Chao Zhao, Scott Dillon, Robin J M Franklin, Rosemary O'Connor, David M Bodine, Iqbal Hamza, David H Rowitch
{"title":"少突胶质细胞 Slc48a1(Hrg1)编码髓鞘完整性所需的功能性血红素转运体。","authors":"John H Stockley, Adrien M Vaquie, Zhaoyang Xu, Theresa Bartels, Gregory D Jordan, Staffan Holmqvist, Simon Gunter, Guy Lam, Daniel Yamamoto, Rini H Pek, Ian G Chambers, Andrew S Rock, Myfanwy Hill, Chao Zhao, Scott Dillon, Robin J M Franklin, Rosemary O'Connor, David M Bodine, Iqbal Hamza, David H Rowitch","doi":"10.1002/glia.24641","DOIUrl":null,"url":null,"abstract":"<p><p>Oligodendrocytes (OLs) of the central nervous system require iron for proteolipid biosynthesis during the myelination process. Although most heme is found complexed to hemoglobin in red blood cells, surprisingly, we found that Slc48a1, encoding the heme transporter Hrg1, is expressed at higher levels in OLs than any other cell type in rodent and humans. We confirmed in situ that Hrg1 is expressed in OLs but not their precursors (OPCs) and found that Hrg1 proteins in CNS white matter co-localized within myelin sheaths. In older Hrg1 null mutant mice we observed reduced expression of myelin associated glycoprotein (Mag) and ultrastructural myelin defects reminiscent of Mag-null animals, suggesting myelin adhesion deficiency. Further, we confirmed reduced myelin iron levels in Hrg1 null animals in vivo, and show that OLs in vitro can directly import both the fluorescent heme analogue ZnMP and heme itself, which rescued iron deficiency induced inhibition of OL differentiation in a heme-oxidase-dependent manner. Together these findings indicate OL Hrg1 encodes a functional heme transporter required for myelin integrity.</p>","PeriodicalId":174,"journal":{"name":"Glia","volume":" ","pages":"399-421"},"PeriodicalIF":5.4000,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Oligodendrocyte Slc48a1 (Hrg1) encodes a functional heme transporter required for myelin integrity.\",\"authors\":\"John H Stockley, Adrien M Vaquie, Zhaoyang Xu, Theresa Bartels, Gregory D Jordan, Staffan Holmqvist, Simon Gunter, Guy Lam, Daniel Yamamoto, Rini H Pek, Ian G Chambers, Andrew S Rock, Myfanwy Hill, Chao Zhao, Scott Dillon, Robin J M Franklin, Rosemary O'Connor, David M Bodine, Iqbal Hamza, David H Rowitch\",\"doi\":\"10.1002/glia.24641\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Oligodendrocytes (OLs) of the central nervous system require iron for proteolipid biosynthesis during the myelination process. Although most heme is found complexed to hemoglobin in red blood cells, surprisingly, we found that Slc48a1, encoding the heme transporter Hrg1, is expressed at higher levels in OLs than any other cell type in rodent and humans. We confirmed in situ that Hrg1 is expressed in OLs but not their precursors (OPCs) and found that Hrg1 proteins in CNS white matter co-localized within myelin sheaths. In older Hrg1 null mutant mice we observed reduced expression of myelin associated glycoprotein (Mag) and ultrastructural myelin defects reminiscent of Mag-null animals, suggesting myelin adhesion deficiency. Further, we confirmed reduced myelin iron levels in Hrg1 null animals in vivo, and show that OLs in vitro can directly import both the fluorescent heme analogue ZnMP and heme itself, which rescued iron deficiency induced inhibition of OL differentiation in a heme-oxidase-dependent manner. Together these findings indicate OL Hrg1 encodes a functional heme transporter required for myelin integrity.</p>\",\"PeriodicalId\":174,\"journal\":{\"name\":\"Glia\",\"volume\":\" \",\"pages\":\"399-421\"},\"PeriodicalIF\":5.4000,\"publicationDate\":\"2025-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Glia\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.1002/glia.24641\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/11/6 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q1\",\"JCRName\":\"NEUROSCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Glia","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1002/glia.24641","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/11/6 0:00:00","PubModel":"Epub","JCR":"Q1","JCRName":"NEUROSCIENCES","Score":null,"Total":0}
引用次数: 0

摘要

中枢神经系统的少突胶质细胞(OL)在髓鞘化过程中需要铁来进行蛋白脂的生物合成。虽然大多数血红素都与红细胞中的血红蛋白络合,但令人惊讶的是,我们发现编码血红素转运体 Hrg1 的 Slc48a1 在啮齿动物和人类 OL 中的表达水平高于任何其他细胞类型。我们在原位证实了 Hrg1 在 OLs 中的表达,而不是在其前体(OPCs)中的表达,并发现 Hrg1 蛋白在中枢神经系统白质中与髓鞘共定位。在年龄较大的 Hrg1 基因缺失突变小鼠中,我们观察到髓鞘相关糖蛋白(Mag)表达减少,髓鞘超微结构缺陷与 Mag 基因缺失动物相似,这表明髓鞘粘附能力不足。此外,我们还证实了 Hrg1 基因缺失动物体内髓鞘铁水平的降低,并表明体外 OL 可直接导入荧光血红素类似物 ZnMP 和血红素本身,从而以血红素氧化酶依赖的方式挽救了缺铁引起的 OL 分化抑制。这些发现共同表明,OL Hrg1编码了髓鞘完整性所需的功能性血红素转运体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Oligodendrocyte Slc48a1 (Hrg1) encodes a functional heme transporter required for myelin integrity.

Oligodendrocytes (OLs) of the central nervous system require iron for proteolipid biosynthesis during the myelination process. Although most heme is found complexed to hemoglobin in red blood cells, surprisingly, we found that Slc48a1, encoding the heme transporter Hrg1, is expressed at higher levels in OLs than any other cell type in rodent and humans. We confirmed in situ that Hrg1 is expressed in OLs but not their precursors (OPCs) and found that Hrg1 proteins in CNS white matter co-localized within myelin sheaths. In older Hrg1 null mutant mice we observed reduced expression of myelin associated glycoprotein (Mag) and ultrastructural myelin defects reminiscent of Mag-null animals, suggesting myelin adhesion deficiency. Further, we confirmed reduced myelin iron levels in Hrg1 null animals in vivo, and show that OLs in vitro can directly import both the fluorescent heme analogue ZnMP and heme itself, which rescued iron deficiency induced inhibition of OL differentiation in a heme-oxidase-dependent manner. Together these findings indicate OL Hrg1 encodes a functional heme transporter required for myelin integrity.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Glia
Glia 医学-神经科学
CiteScore
13.10
自引率
4.80%
发文量
162
审稿时长
3-8 weeks
期刊介绍: GLIA is a peer-reviewed journal, which publishes articles dealing with all aspects of glial structure and function. This includes all aspects of glial cell biology in health and disease.
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信