We are analyzing https://link.springer.com/article/10.1007/s10534-012-9528-8.

Title:
Uptake of copper from plasma proteins in cells where expression of CTR1 has been modulated | BioMetals
Description:
Plasma proteins rather than amino acid chelates are the direct sources of copper for mammalian cells. In continuing studies on the mechanisms by which albumin and transcuprein deliver copper and the potential involvement of CTR1, rates of uptake from these proteins and Cu–histidine were compared in cells with/without CTR1 knockdown or knockout. siRNA knocked down expression of CTR1 mRNA 60–85% in human mammary epithelial and hepatic cell models, but this had little or no effect on uptake of 1 μM Cu(II) attached to pure human albumin or alpha-2-macroglobulin. Mouse embryonic fibroblasts that did/did not express Ctr1 took up Cu(II) bound to albumin about as readily as from the histidine complex at physiological concentrations and by a single saturable process. Uptake from mouse albumin achieved a 2–4-fold higher Vmax (with a lower Km) than from heterologous human albumin. Maximum uptake rates from Cu(I)–histidine were >12-fold higher (with higher Km) than for Cu(II), suggesting mediation by a reductase. The presence of cell surface Cu(II) and Fe(III) reductase activity responding only slightly to dehydroascorbate was verified. Excess Fe(III) inhibited uptake from albumin–Cu(II). Ag(I) also inhibited, but kinetics were not or un-competitive. In general there was little difference in rates/kinetics of uptake in the Ctr1+/+ and −/− cells. Endocytosis was not involved. We conclude that plasma proteins deliver Cu(II) to homologous cells with greater efficiency than ionic copper at physiological concentrations, probably through the mediation of a Steap Cu(II)-reductase, and confirm the existence of an additional copper uptake system in mammalian cells.
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Keywords {🔍}

copper, google, scholar, article, cas, pubmed, ctr, human, uptake, cells, proteins, biol, plasma, linder, chem, albumin, lee, transporter, research, cell, mouse, physiol, biochem, privacy, essential, cookies, content, biometals, cuii, embryonic, complex, reductase, access, blood, serum, thiele, usa, publish, search, kidane, farhad, mammalian, metabolism, transport, nutr, proc, natl, biochemistry, data, information,

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month download article/chapter high affinity site related subjects cupric ion-binding sites plasma protein full article pdf copper transporter ctr1 multiple copper proteins van dyke br privacy choices/manage cookies article biometals aims kyoung jin lee reductase activity responding california state university plasma proteins stimulates copper uptake copper uptake identified check access instant access human mammary epithelial european economic area amino acid chelates single saturable process controls tumor growth trace element species size exclusion chromatography gratefully acknowledge receipt subsidizing 64cu production hepatic cell models conditions privacy policy transcuprein deliver copper copper deficient rat human cutc gene human copper homeostasis mouse embryonic fibroblasts metal-based drugs 1–9 direct injection nebulization functional ferric reductases ternary coordination complex copper transport maximum uptake rates mammalian embryonic development caco2 cell model pure human albumin heterologous human albumin turnlund jr cultured human cells accepting optional cookies stable isotope 65cu golgi complex organization

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         headline:Uptake of copper from plasma proteins in cells where expression of CTR1 has been modulated
         description:Plasma proteins rather than amino acid chelates are the direct sources of copper for mammalian cells. In continuing studies on the mechanisms by which albumin and transcuprein deliver copper and the potential involvement of CTR1, rates of uptake from these proteins and Cu–histidine were compared in cells with/without CTR1 knockdown or knockout. siRNA knocked down expression of CTR1 mRNA 60–85% in human mammary epithelial and hepatic cell models, but this had little or no effect on uptake of 1 μM Cu(II) attached to pure human albumin or alpha-2-macroglobulin. Mouse embryonic fibroblasts that did/did not express Ctr1 took up Cu(II) bound to albumin about as readily as from the histidine complex at physiological concentrations and by a single saturable process. Uptake from mouse albumin achieved a 2–4-fold higher Vmax (with a lower Km) than from heterologous human albumin. Maximum uptake rates from Cu(I)–histidine were >12-fold higher (with higher Km) than for Cu(II), suggesting mediation by a reductase. The presence of cell surface Cu(II) and Fe(III) reductase activity responding only slightly to dehydroascorbate was verified. Excess Fe(III) inhibited uptake from albumin–Cu(II). Ag(I) also inhibited, but kinetics were not or un-competitive. In general there was little difference in rates/kinetics of uptake in the Ctr1+/+ and −/− cells. Endocytosis was not involved. We conclude that plasma proteins deliver Cu(II) to homologous cells with greater efficiency than ionic copper at physiological concentrations, probably through the mediation of a Steap Cu(II)-reductase, and confirm the existence of an additional copper uptake system in mammalian cells.
         datePublished:2012-02-22T00:00:00Z
         dateModified:2012-02-22T00:00:00Z
         pageStart:697
         pageEnd:709
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            CTR1
            Plasma proteins
            Copper reductase
            Silver inhibition
            Biochemistry
            general
            Pharmacology/Toxicology
            Microbiology
            Cell Biology
            Plant Physiology
            Medicine/Public Health
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      headline:Uptake of copper from plasma proteins in cells where expression of CTR1 has been modulated
      description:Plasma proteins rather than amino acid chelates are the direct sources of copper for mammalian cells. In continuing studies on the mechanisms by which albumin and transcuprein deliver copper and the potential involvement of CTR1, rates of uptake from these proteins and Cu–histidine were compared in cells with/without CTR1 knockdown or knockout. siRNA knocked down expression of CTR1 mRNA 60–85% in human mammary epithelial and hepatic cell models, but this had little or no effect on uptake of 1 μM Cu(II) attached to pure human albumin or alpha-2-macroglobulin. Mouse embryonic fibroblasts that did/did not express Ctr1 took up Cu(II) bound to albumin about as readily as from the histidine complex at physiological concentrations and by a single saturable process. Uptake from mouse albumin achieved a 2–4-fold higher Vmax (with a lower Km) than from heterologous human albumin. Maximum uptake rates from Cu(I)–histidine were >12-fold higher (with higher Km) than for Cu(II), suggesting mediation by a reductase. The presence of cell surface Cu(II) and Fe(III) reductase activity responding only slightly to dehydroascorbate was verified. Excess Fe(III) inhibited uptake from albumin–Cu(II). Ag(I) also inhibited, but kinetics were not or un-competitive. In general there was little difference in rates/kinetics of uptake in the Ctr1+/+ and −/− cells. Endocytosis was not involved. We conclude that plasma proteins deliver Cu(II) to homologous cells with greater efficiency than ionic copper at physiological concentrations, probably through the mediation of a Steap Cu(II)-reductase, and confirm the existence of an additional copper uptake system in mammalian cells.
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      dateModified:2012-02-22T00:00:00Z
      pageStart:697
      pageEnd:709
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         CTR1
         Plasma proteins
         Copper reductase
         Silver inhibition
         Biochemistry
         general
         Pharmacology/Toxicology
         Microbiology
         Cell Biology
         Plant Physiology
         Medicine/Public Health
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