Dylan R. Graham, Kyle C. Edwards, Susan Darby Keith, Michael W. Gannon, John B. Vincent
{"title":"铬(III)的损失从混合铬(III),铁(III)血清转铁蛋白","authors":"Dylan R. Graham, Kyle C. Edwards, Susan Darby Keith, Michael W. Gannon, John B. Vincent","doi":"10.1016/j.jinorgbio.2025.113046","DOIUrl":null,"url":null,"abstract":"<div><div>Trivalent chromium has been shown to be transported <em>in vivo</em> from the bloodstream to the tissues <em>via</em> endocytosis by transferrin (Tf), the major iron transport protein in the blood. Recent <em>in vitro</em> studies using Cr(III)<sub>2</sub>-Tf have shown that under physiologically relevant conditions, the binding of Cr(III) to Tf and the loss of Cr(III) from the Cr(III)<sub>2</sub>-Tf/Tf receptor complex are rapid. However, the major form of transferrin in the bloodstream is monoferric Tf. Thus, given the low concentrations of Cr(III) in the bloodstream, the form of Cr(III)-containing transferrin in the bloodstream that is transported <em>via</em> endocytosis is monochromic, monoferric-Tf (Cr(III),Fe(III)-Tf). Given that Tf has two specific metal-binding sites, one in both the C-terminal and the N-terminal lobes of Tf, two forms of Cr(III),Fe(III)-Tf can form. The loss of Cr(III) from both forms of Cr(III),Fe(III)-Tf have been examined for the first time. The mixed metal Tf's lose Cr(III) in similar fashions to Cr(III) losses from Cr(III)<sub>2</sub>-Tf itself or from the Cr(III)<sub>2</sub>-Tf/Tf receptor complex.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"273 ","pages":"Article 113046"},"PeriodicalIF":3.2000,"publicationDate":"2025-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Loss of chromium(III) from mixed Cr(III),Fe(III) serum Transferrins\",\"authors\":\"Dylan R. Graham, Kyle C. Edwards, Susan Darby Keith, Michael W. Gannon, John B. Vincent\",\"doi\":\"10.1016/j.jinorgbio.2025.113046\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Trivalent chromium has been shown to be transported <em>in vivo</em> from the bloodstream to the tissues <em>via</em> endocytosis by transferrin (Tf), the major iron transport protein in the blood. Recent <em>in vitro</em> studies using Cr(III)<sub>2</sub>-Tf have shown that under physiologically relevant conditions, the binding of Cr(III) to Tf and the loss of Cr(III) from the Cr(III)<sub>2</sub>-Tf/Tf receptor complex are rapid. However, the major form of transferrin in the bloodstream is monoferric Tf. Thus, given the low concentrations of Cr(III) in the bloodstream, the form of Cr(III)-containing transferrin in the bloodstream that is transported <em>via</em> endocytosis is monochromic, monoferric-Tf (Cr(III),Fe(III)-Tf). Given that Tf has two specific metal-binding sites, one in both the C-terminal and the N-terminal lobes of Tf, two forms of Cr(III),Fe(III)-Tf can form. The loss of Cr(III) from both forms of Cr(III),Fe(III)-Tf have been examined for the first time. The mixed metal Tf's lose Cr(III) in similar fashions to Cr(III) losses from Cr(III)<sub>2</sub>-Tf itself or from the Cr(III)<sub>2</sub>-Tf/Tf receptor complex.</div></div>\",\"PeriodicalId\":364,\"journal\":{\"name\":\"Journal of Inorganic Biochemistry\",\"volume\":\"273 \",\"pages\":\"Article 113046\"},\"PeriodicalIF\":3.2000,\"publicationDate\":\"2025-08-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Inorganic Biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0162013425002260\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Inorganic Biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0162013425002260","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Loss of chromium(III) from mixed Cr(III),Fe(III) serum Transferrins
Trivalent chromium has been shown to be transported in vivo from the bloodstream to the tissues via endocytosis by transferrin (Tf), the major iron transport protein in the blood. Recent in vitro studies using Cr(III)2-Tf have shown that under physiologically relevant conditions, the binding of Cr(III) to Tf and the loss of Cr(III) from the Cr(III)2-Tf/Tf receptor complex are rapid. However, the major form of transferrin in the bloodstream is monoferric Tf. Thus, given the low concentrations of Cr(III) in the bloodstream, the form of Cr(III)-containing transferrin in the bloodstream that is transported via endocytosis is monochromic, monoferric-Tf (Cr(III),Fe(III)-Tf). Given that Tf has two specific metal-binding sites, one in both the C-terminal and the N-terminal lobes of Tf, two forms of Cr(III),Fe(III)-Tf can form. The loss of Cr(III) from both forms of Cr(III),Fe(III)-Tf have been examined for the first time. The mixed metal Tf's lose Cr(III) in similar fashions to Cr(III) losses from Cr(III)2-Tf itself or from the Cr(III)2-Tf/Tf receptor complex.
期刊介绍:
The Journal of Inorganic Biochemistry is an established international forum for research in all aspects of Biological Inorganic Chemistry. Original papers of a high scientific level are published in the form of Articles (full length papers), Short Communications, Focused Reviews and Bioinorganic Methods. Topics include: the chemistry, structure and function of metalloenzymes; the interaction of inorganic ions and molecules with proteins and nucleic acids; the synthesis and properties of coordination complexes of biological interest including both structural and functional model systems; the function of metal- containing systems in the regulation of gene expression; the role of metals in medicine; the application of spectroscopic methods to determine the structure of metallobiomolecules; the preparation and characterization of metal-based biomaterials; and related systems. The emphasis of the Journal is on the structure and mechanism of action of metallobiomolecules.