The Involvement of Transferrin in the Uptake of Iron-59 by Hepatocytes of Carbon Tetrachloride-Damaged Rats

Suyama, Satoko; Abe, Shinya; Inoué, Yoshihiro; Toukairin, Ai; Ohtake, Yosuke; Ohkubo, Yasuhito

doi:10.1248/bpb.29.1387

Cited by 3 publications

(3 citation statements)

References 24 publications

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“…After 2 h incubation at room temperature, plates were centrifuged at 3000 g for 2 min, and the absorbance was read at 492 nm using a Spectramax microtitre plate reader (Molecular Devices). Fe binding assay was performed as described by Suyama et al (2006). Briefly, 50 mg of either recombinant YtgA, human transferrin (Sigma-Aldrich) or BSA was suspended in 0.5 ml Tris/HCl buffered saline.…”

Section: Methodsmentioning

confidence: 99%

“…Competition assays were performed by adding 6.6 ml non-radioactive FeCl 3 , ZnCl 2 , or MnCl 2 (each 25 mmol ml 21 ) to the reaction mixtures prior to incubation. The results are expressed as the percentage of 59 Fe in the protein or supernatant fraction (Suyama et al, 2006). (Sigma-Aldrich)] was added to each flask (referred to as time 0), and the infected flasks were moved back to 35 uC.…”

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Chlamydia trachomatis YtgA is an iron-binding periplasmic protein induced by iron restriction

et al. 2009

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Chlamydia trachomatis is a Gram-negative obligate intracellular bacterium that is the causative agent of common sexually transmitted diseases and the leading cause of preventable blindness worldwide. It has been observed that YtgA (CT067) is very immunogenic in patients with chlamydial genital infections. Homology analyses suggested that YtgA is a soluble periplasmic protein and a component of an ATP-binding cassette (ABC) transport system for metals such as iron. Since little is known about iron transport in C. trachomatis, biochemical assays were used to determine the potential role of YtgA in iron acquisition. 59Fe binding and competition studies revealed that YtgA preferentially binds iron over nickel, zinc or manganese. Western blot and densitometry techniques showed that YtgA concentrations specifically increased 3–5-fold in C. trachomatis, when cultured under iron-starvation conditions rather than under general stress conditions, such as exposure to penicillin. Finally, immuno-transmission electron microscopy provided evidence that YtgA is more concentrated in C. trachomatis during iron restriction, supporting a possible role for YtgA as a component of an ABC transporter.

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Section: Methodsmentioning

confidence: 99%

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Chlamydia trachomatis YtgA is an iron-binding periplasmic protein induced by iron restriction

et al. 2009

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“…The gene structure analysis for identified HSFs was constructed using the Gene Structure Display Server (GSDS) ( http://gsds.cbi.pku.edu.cn/ ) ( Suyama et al, 2006 ), while domain composition was presented by using the Tbtools ( Chen et al, 2020 ).…”

Section: Methodsmentioning

confidence: 99%

Comparative Analysis of HSF Genes From Secale cereale and its Triticeae Relatives Reveal Ancient and Recent Gene Expansions

Feng

Zeng

et al. 2021

Front. Genet.

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Plants have evolved sophisticated systems to cope with the environmental stresses, with the heat shock factor (HSF) family proteins composing an integral part of the transcriptional regulation system. Understanding the evolutionary history and functional diversity of HSFs will facilitate improving tolerance of crops to adverse environmental conditions. In this study, genome-wide analysis of Secale cereale identified 31 HSF genes. The total number of HSF genes in S. cereale is larger than that in barley and the three subgenomes of wheat, suggesting it is a valuable resource for mining functional HSFs. Chromosome analysis revealed an uneven distribution of HSF genes among the 7 S. cereale chromosomes, with no HSF gene was detected on chromosome 4. Further interspecies synteny analysis revealed that chromosome reorganization during species-speciation may lead to the escape of HSF genes from the S. cereale chromosome 4. Phylogenetic analysis revealed that S. cereale experienced more HSF gene duplications than barley and the three wheat subgenomes. Expression analysis demonstrated that S. cereale HSF genes showed diverse expression patterns across plant developmental stages and upon drought and freezing treatment, suggesting functional diversity of the gene family. Notably, we detected distinct expression patterns for a recently duplicated HSF gene pair, indicating functional divergence may have occurred between the two genes. The study presents the genome organization, evolutionary features and expression patterns of the S. cereale HSF genes. These results provide new insights into the evolution of HSF genes in Triticeae and may serve as a resource for Triticeae molecular breeding.

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Oxygen-dependent Oxidation of Fe(II) to Fe(III) and Interaction of Fe(III) with Bovine Serum Albumin, Leading to a Hysteretic Effect on the Fluorescence of Bovine Serum Albumin

Zhang

Shen

et al. 2007

J Fluoresc

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The serum albumin is the most abundant protein in blood plasma and the iron is essential for many cellular processes. However, the interaction between Fe(3+) and haem-free serum albumin remains unclear. Here we provide evidence for the fact that haem-free BSA possesses one specific Fe(3+)-binding site. The binding of Fe(3+) to BSA results in a significant quenching of the Trp fluorescence of BSA. The average apparent dissociation constant value for the interaction of Fe(3+) and BSA is 3.46 x 10(-8)+/-3 x 10(-10) M at 37 degrees C and 3.30 x 10(-8)+/-5 x 10(-10) M at 25 degrees C, respectively, as determined by fluorescence titration. Addition of 50 microM Fe(2+) to 1 microM BSA results in an obvious hysteretic effect on the fluorescence of BSA. The time-dependent fluorescence quenching of BSA by Fe(2+) is not caused by the Fe(2+)-induced conformational change of BSA, but the oxygen-dependent oxidation of Fe(2+) to Fe(3+). Fe(2+) undergoes an oxygen-dependent oxidation to Fe(3+) under aerobic conditions, which is accelerated by the interaction of BSA with Fe(3+) and extensively inhibited under anaerobic conditions. The results suggest that BSA may take part in non-transferrin bound iron transfer.

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The Involvement of Transferrin in the Uptake of Iron-59 by Hepatocytes of Carbon Tetrachloride-Damaged Rats

Abstract: Gallium-67 (67 Ga) has been used for detecting various tumors 1-4) and acute and chronic inflammations, 5,6) since the first observation of its accumulation in those lesions was reported.7-9) However, underlying molecular mechanisms of 67

Cited by 3 publications

References 24 publications

Chlamydia trachomatis YtgA is an iron-binding periplasmic protein induced by iron restriction

Chlamydia trachomatis YtgA is an iron-binding periplasmic protein induced by iron restriction

Comparative Analysis of HSF Genes From Secale cereale and its Triticeae Relatives Reveal Ancient and Recent Gene Expansions

Oxygen-dependent Oxidation of Fe(II) to Fe(III) and Interaction of Fe(III) with Bovine Serum Albumin, Leading to a Hysteretic Effect on the Fluorescence of Bovine Serum Albumin

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