Anion transport during maturation of erythroblastic cells

Kirk, R. G.; Lee, Ping

doi:10.1007/bf01872832

Cited by 3 publications

(1 citation statement)

References 20 publications

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“…Failure to transport the other transition metals is probably a consequence of their inability to form such complexes. The anion exchanger of the red cell is represented by the membrane protein, band 3, which is synthesized in immature erythroid cells up to the reticulocyte stage and persists throughout the lifespan of the red cell (Foxwell & Tanner, 1981;Kirk & Lee, 1988). Since red cells decrease in size and show an increase in surface-to-volume ratio as they mature and age the relative concentration of band 3 increases.…”

Section: Discussionmentioning

confidence: 99%

Transport mechanisms for iron and other transition metals in rat and rabbit erythroid cells

Savigni

Morgan

1998

The Journal of Physiology

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Earlier studies have shown that Fe2+ transport into erythroid cells is inhibited by several transition metals (Mn2+, Zn2+, Co2+, Ni2+) and that Fe2+ transport can occur by two saturable mechanisms, one of high affinity and the other of low affinity. Also, the transport of Zn2+ and Cd2+ into erythroid cells is stimulated by NaHCO3 and NaSCN. The aim of the present investigation was to determine whether all of these transition metals can be transported by the processes described for Fe2+, Zn2+ and Cd2+ and to determine the properties of the transport processes. Rabbit reticulocytes and mature erythrocytes and reticulocytes from homozygous and heterozygous Belgrade rats were incubated with radiolabelled samples of the metals under conditions known to be optimal for high‐ and low‐affinity Fe2+ transport and for the processes mediated by NaHCO3 and NaSCN. All of the metals were transported by the high‐ and low‐affinity Fe2+ transport processes and could compete with each other for transport. The Km and Vmax values and the effects of incubation temperature and metabolic inhibitors were similar for all the metals. NaHCO3 and NaSCN increased the uptake of Zn2+ and Cd2+ but not the other metals. The uptake of all of the metals by the high‐affinity process was much lower in reticulocytes from homozygous Belgrade rats than in those from heterozygous animals, but there was no difference with respect to low‐affinity transport. It is concluded that the high‐ and low‐affinity ‘iron’ transport mechanisms can also transport several other transition metals and should therefore be considered as general transition metal carriers.

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Section: Discussionmentioning

confidence: 99%

Transport mechanisms for iron and other transition metals in rat and rabbit erythroid cells

Savigni

Morgan

1998

The Journal of Physiology

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Furosemide Stimulates K Transport in HCD57 Erythroid Cells

et al. 2000

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We examined the influence of serum and furosemide on K movement and cell volume in HCD57 cells, a murine erythroleukemia cell line, which require erythropoietin (EPO) for survival. We found that maintenance of cell volume depends on the concentration of serum in the culture medium. In isotonic medium containing 20% serum, HCD57 cells maintain their steady-state volume. In contrast, the cells shrink progressively as medium serum content is reduced. In serum-free medium, raising external K to 75 mm prevents cell shrinkage and a further increase in K to 145 mm results in swelling, revealing a role for K permeability in the regulation of cell volume. Of particular interest has been a serendipitous finding with furosemide. Below an external K concentration of 2.1 +/- 0.3 mm in medium containing 2% serum, furosemide inhibits K uptake, probably stemming from its well known inhibitory action on KCl cotransport. However, above that K concentration, furosemide stimulates K uptake in a dose-dependent manner. Moreover, furosemide potentiates cell shrinkage induced by serum withdrawal. These findings suggest that the transport machinery mediating cellular shrinkage, once primed by serum depletion, becomes receptive to a second stimulus.

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Platinum as a tracer for intracellular distribution of a drug (CIS-PLATIN) : x-ray microanalysis

Kirk¹,

Lee²

1992

Proc. annu. meet. Electron Microsc. Soc. Am.

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Cisplatin, cis-diamminedichloroplatinum (II) , contains a platinum atom in each of its molecule. It is an effective chemotherapeutic agent, used to treat ovarian, testicular and bladder tumors. The antitumor activity and cytoxity of this drug is generally attributed to its ability to cross-link DNA in the chromosome. Recent investigators show that there are also membrane and cytosolic components in the biological activity of cisplatin. Although the mechanism for the membrane transport of cisplatin is not known, it is thought that decrease in uptake of the drug is contributory to the cellular resistance to cisplatin. In addition cytosolic concentrations of glutathione, metallothionein or protein kinase C have been shown to affect the cytotoxicity of cisplatin. A frequent toxicity seen in patients that have received cisplatin treatment is the depression of the bone marrow cells. In order to gain some insight into this toxicity event, we have studied the uptake and intracellular distribution of cisplatin using the technique of cryomicrotomy and x-ray microanalysis.

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Anion transport during maturation of erythroblastic cells

Cited by 3 publications

References 20 publications

Transport mechanisms for iron and other transition metals in rat and rabbit erythroid cells

Transport mechanisms for iron and other transition metals in rat and rabbit erythroid cells

Furosemide Stimulates K Transport in HCD57 Erythroid Cells

Platinum as a tracer for intracellular distribution of a drug (CIS-PLATIN) : x-ray microanalysis

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