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Background: Whole blood donors are screened for iron depletion through hemoglobin measurement alone or in combination with ferritin. Ferritin measurement gives the advantage of earlier detection of iron depletion. In a previous study we identified a ferritin level of 30 μg/L or less as a possible indicator of suboptimal erythropoiesis. In this study, erythropoietic parameters were measured to determine if a ferritin level of 30 μg/L or less is indicative of iron-deficient erythropoiesis in repeat whole blood donors.Study Design and Methods: Twenty-one healthy male repeat whole blood donors were divided into two groups according to their predonation ferritin values: 30 μg/L or less (low-ferritin group) and greater than 30 μg/L (normal-ferritin group). Ferritin and erythropoietic parameters were measured before whole blood donation and weekly in the 8 weeks after donation.Results: A significantly lower value was found for hemoglobin, mean corpuscular volume (MCV), reticulocytes, and reticulocyte hemoglobin content on at least three of the nine time points in the low-ferritin group compared to the normal-ferritin group (p < 0.05). Of these parameters, MCV and reticulocyte hemoglobin content were significantly lower before donation as well as during all 8 weeks following donation (p < 0.05).Conclusion: Based on the lower values of the erythropoietic parameters in the low-ferritin group, it can be concluded that repeat whole blood donors with a ferritin value of 30 μg/L or less have iron-deficient erythropoiesis and therefore require a longer donation interval than the current 56 days. [ABSTRACT FROM AUTHOR]

During aging, oxidized, misfolded, and aggregated proteins accumulate in cells, while the capacity to deal with protein damage declines severely. To cope with the toxicity of damaged proteins, cells rely on protein quality control networks, in particular proteins belonging to the family of heat-shock proteins ( HSPs). As safeguards of the cellular proteome, HSPs assist in protein folding and prevent accumulation of damaged, misfolded proteins. Here, we compared the capacity of all Drosophila melanogaster small HSP family members for their ability to assist in refolding stress-denatured substrates and/or to prevent aggregation of disease-associated misfolded proteins. We identified CG14207 as a novel and potent small HSP member that exclusively assisted in HSP70-dependent refolding of stress-denatured proteins. Furthermore, we report that HSP67 BC, which has no role in protein refolding, was the most effective small HSP preventing toxic protein aggregation in an HSP70-independent manner. Importantly, overexpression of both CG14207 and HSP67 BC in Drosophila leads to a mild increase in lifespan, demonstrating that increased levels of functionally diverse small HSPs can promote longevity in vivo. [ABSTRACT FROM AUTHOR]