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Psoriasis is a common, chronic, immune mediated inflammatory disease that involves the innate immunological system (keratinocyte, dendritic cell, histiocytes, mast cells and endothelial cells) and acquired immunological system (T lymphocytes). Essential trace elements like iron (Fe), copper (Cu) undergo redox cycling and have physiological significance in inflammatory process. This study is aimed at measuring the level of copper, ceruloplasmin, iron and transferrin in psoriasis patient and to assess its relationship with the severity of the disease. This is an observational cross sectional study. It was conducted at the department of Dermatology and Venereology, BSMMU, Dhaka. Age range of the patient was 18 to 65 years. The mean age of the patients was 39.1±13.54 years, 57.9% patients were male and 42.1% were female. Male: female ratio was 1.4:1. Male patients were predominant. Mean duration of disease 5.36±4.05 years with range from 1.0 to 14 years. Most of the (76.3%) patients had mild disease followed by 23.7% had moderate to severe disease. Serum level of trace elements was compared between mild and moderate to severe group of psoriasis patients but difference were not statistically significant (p>0.05). Weak negative correlation was found between PASI score and serum levels of copper (r = “0.134, P = 0.423), iron (r = –0.080, p = 0.632), transferrin (r = –0.079, p = 0.638) and weak positive correlation was found with ceruloplasmin (r = 0.228, p = 0.168). The results of the present research provide valuable information and correlation between the measured biomarkers and severity of psoriasis. Serum Ceruloplasmin, copper, iron and serum transferrin could serve as a biomarker of psoriasis but not as a marker of psoriasis severity. J Dhaka Medical College, Vol. 29, No.1, April, 2020, Page 59-68

Background: We aimed to evaluate the use of population-based-reference-intervals by calculating the individuality index and reference change value of iron, transferrin, ferritin, folate, vitamin B12, and 25-OH vitamin D parameters. Methods: A total of 5 venous blood samples were taken from 11 female and 10 male individuals on days 0, 7, 14, 21, and 28. All tests were performed on an autoanalyzer and CVI, CVG, II, and RCV values were calculated for both genders and the whole groups. Results: CVA (%)/CVI (%)/CVG (%) for iron, 0.67/27.3/32.3 transferrin, 0.62/3.60/10.27 ferritin, 2.27/6.21/105.6 folate 4.71/10.3/28.56 vitamin B12, 6.1/5.77/34.6, 25-OH Vitamin D 3.4/8.2/54.9 respectively. RCV calculated as a 2-tailed value at level of probability of significant change set at 0.95 - 0.99; 74.9/98.7 - 10.1/13.3 - 18.3/24.1 31.4/41.3 - 23.4/30.8 - 24.7/32.5 and II were 0.8-0.4-0.-0.4-0.17-0.1 respectively. Conclusions: CVI and CVG values for iron, transferrin, folate, vitamin B12, and 25-OH vitamin D are in accordance with the literature. Ferritin was calculated differently from the values in the database. This difference might be due to the characteristics of selected individuals for study. Evaluating the suitability and utility of the use of RR with values found for II. For iron, the use of RR was considered appropriate when taken as II < 0.6 and II > 1.4. However, the use of RCV is more appropriate for Transferrin, Folate, Vitamin B12, and 25-OH Vitamin D. (Clin. Lab. 2021;67:2048-2054. DOI: 10.7754/Clin.Lab.2021.210102)

AimTo study the regional variability of requests for anaemia chemistry tests in primary care in Spain and the associated economic costs of potential over-requesting.MethodsRequests for anaemia tests were examined in a cross-sectional study. Clinical laboratories from different autonomous communities (AACCs) were invited to report on primary care anaemia chemistry tests requested during 2014. Demand for iron, ferritin, vitamin B12 and folate tests per 1000 inhabitants and the ratios of the folate/vitamin B12 and transferrin/ferritin requests were compared between AACCs. We also calculated reagent costs and the number of iron, transferrin and folate tests and the economic saving if every AACC had obtained the results achieved by the AACC with best practice.Results110 laboratories participated (59.8% of the Spanish population). More than 12 million tests were requested, resulting in reagent costs exceeding €16.5 million. The serum iron test was the most often requested, and the ferritin test was the most costly (over €7 million). Close to €4.5 million could potentially have been saved if iron, transferrin and folate had been appropriately requested (€6 million when extrapolated to the whole Spanish population).ConclusionsThe demand for and expenditure on anaemia chemistry tests in primary care in Spain is high, with significant regional differences between different AACCs.

The Multicommutated Flow Analysis (MCFA) system for the estimation of clinical iron parameters: Serum Iron (SI), Unsaturated Iron Binding Capacity (UIBC) and Total Iron Binding Capacity (TIBC) has been proposed. The developed MCFA system based on simple photometric detection of iron with chromogenic agent (ferrozine) enables a speciation of transferrin (determination of free and Fe-bound protein) in human serum. The construction of manifold was adapted to the requirements of measurements under changing conditions. In the course of studies, a different effect of proteins on SI and UIBC determination has been proven. That was in turn the reason to perform two kinds of calibration methods. For measurements in acidic medium for SI/holotransferrin determination, the calibration curve method was applied, characterized by limit of determination and limit of quantitation on the level of 3.4 μmol L−1 and 9.1 μmol L−1, respectively. The determination method for UIBC parameter (related to apotransferrin level) in physiological medium of pH 7.4 forced the use of standard addition method due to the strong influence of proteins on obtaining analytical signals. These two different methodologies, performed in the presented system, enabled the estimation of all three clinical iron/transferrin parameters in human serum samples. TIBC corresponding to total transferrin level was calculated as a sum of SI and UIBC.

The normal color of plasma is yellow, which is owing to the presence of factors such as bilirubin, hemoglobin, carotenoids, and iron transferrin. We recently came across an interesting case of greenish colored plasma in our blood bank. An extensive literature survey revealed that our conspicuous finding was not an isolated one and that similar such rare incidents have been reported in the past, on a sporadic basis. Several diverse reasons have been attributed to the peculiar greenish color like the presence of high ceruloplasmin levels, Pseudomonas aeruginosa infection and so on, but they were ruled out in our case. We thus, report our finding of greenish colored plasma in an otherwise healthy donor because of the rarity of its occurrence and also, to allay any sense of fear or alarm that an encounter may raise in the blood bank staff.

Iron storage disease (haemochromatosis) is thought to be the cause of many disorders unique to captive black rhinoceroses (Diceros bicornis). To establish reliable reference ranges for iron parameters, serum samples from 27 eastern black rhinoceroses (Diceros bicornis michaeli) from a translocation programme in Kenya were analysed and compared with the samples from 17 captive individuals. The transferrin saturation, serum iron concentration and gamma glutamyl transferase were significantly higher in the captive rhinoceroses, but these elevations were not evident when the results were compared with previously published data.

The role of transferrin in iron metabolism is evaluated, both with regard to iron uptake by transferrin and to iron uptake from transferrin by different cells. The heterogeneity of serum transferrin is described and the implications of the heterogeneity are discussed. The composition of ferritin is given and the value of serum ferritins are discussed.

EXAFS spectra have been collected on the oxalate complex of iron serum transferrin and compared to those of carbonate transferrin. Significant changes have been observed in the amplitude and position of the peaks in the Fourier transforms. The observed behavior is a clear indication for structural changes in the chromophore and in the conformation of the metal environment. The binding mode of the oxalate anion to the iron center is discussed.

We measured iron, ferritin, and transferrin in cerebrospinal fluid (CSF) of pediatric patients. Because the concentrations of iron and iron-binding proteins in CSF in these samples were lower than those ordinarily measured in older subjects, we had to modify the lower limit of detection of the methods used. The concentrations of these three analytes in patients with viral meningitis were higher than those in healthy infants and children.

Through a process resembling receptor-mediated internalization, liver endothelium binds and internalizes iron-transferrin (Fe-Tf) complexes, transporting them from the luminal to abluminal side. Since in most systems, the path of receptor-mediated endocytosis leads to the endosomal compartment where the medium is acidified, it is expected that Fe and Tf become dissociated in this acidified medium. However, experiments with double labeling (59Fe, 125I-Tf) indicate that these remain associated. To determine whether the endosomal pathway is used in the course of transendothelial transport of Fe-Tf, experiments were done by incubating purified liver endothelium with radiolabeled Fe-Tf in the presence and absence of endosomal inhibitors, NH4Cl, ethylamine and monensin. The discharge of radiolabeled protein was measured as a function of time. While there was an early phase inhibition in the presence of endosomal inhibitors, the discharge of Tf by endothelium in the presence of inhibitors, reached a plateau comparable to control cells after 4 h, indicating that endosomal inhibition does not inhibit transendothelial transport of Tf and, thus, the transport does not involve endosomal traffic.

The binding of iron to transferrin was studied by loading iron (III) onto apotransferrin in a chloride and a nitrilotriacetate form. When magnesium was added, a marked increase occured in both the rate of iron binding and the maximum level of iron loaded on transferrin utilizing either iron salt. In the absence of magnesium the amount of iron required to achieve 50 percent saturation of the binding sites was 1.6 × 10−4M, whereas when magnesium was added, only about one-third as much iron (0.54 × 10−4M) was required. These data suggest an allosteric effect on transferrin by magnesium which potentiates iron (III) binding.

Using a single-incubation two-site immunoradiometric assay, ferritin levels in human peripheral blood lymphocytes have been quantitated up to 72 h in culture. Ferritin levels were found to increase markedly when the cells were treated with phytohemagglutinin or with iron transferrin (in the presence or absence of phytohemagglutinin). On the other hand, zinc transferrin, with or without iron transferrin in the culture medium and in the presence and absence of phytohemagglutinin, produced a dose-dependent decrease in cellular ferritin compared to controls. Additionally, the increase in lymphocyte ferritin produced by phytohemagglutinin and iron transferrin appears to require transcriptional and translation events.

Whole-blood caeruloplasmin measured by electron spin resonance was studied in 41 patients with chronic lymphocytic leukaemia. The levels were above normal at all stages of the disease, rose with increasing clinical involvement, and were higher in progressive than inactive disease. Whole-blood iron transferrin levels were more variable, and were significantly raised only in patients with marrow failure.

The influence of the reducing agents sodium sulphite, sodium ascorbate and sodium thioglycollate on iron-transferrin dissociation has been studied. Sulphite and ascorbate augment acid dissociation but do not induce it at physiological pH. In contrast, thioglycollate induces dissociation at physiological and even higher pH levels. It is suggested that thioglycollate is directly reactive in iron-transferrin dissociation, possibly through the formation of a ternary complex, whereas the other reducing agents merely shift the equilibrium.

Measurement of the distribution of the four species of transferrin, viz, apotransferrin, diferric transferrin and the two monoferric transferrin, before and after incubation of iron-rich rabbit transferrin with rabbit reticulocytes showed that not all transferrin released from the cells were in the form of apotransferrin. Instead, a mixture of all four species of the protein was released with apotransferrin and C-terminal monoferric transferrin being the major fractions. The buffer solution containing 125I-labelled transferrin showed a continuous gain in percentages in apotransferrin and C-terminal monoferric transferrin after each incubation with reticulocytes. The N-terminal monoferric transferrin, however, remained unchanged suggesting that in the process of transferrin uptake by cells, the diferric transferrin releases its iron from the acid-labile site at N-domain first before the other iron from the acid-stable site.

Caeruloplasmin and iron transferrin level were measured in blood of patients with non-Hodgkin's lymphoma in different stages of disease activity and compared with erythrocyte sedimentation rate and NAP level in the same samples. It was found that both caeruloplasmin level and sedimentation rate showed a slight increase in mean level in patients with active disease as compared with those in remission, particularly in the group of patients with poorly or undifferentiated diffuse disease. No difference was observed in levels of iron transferrin or NAP. Both caeruloplasmin and sedimentation rate showed occasional abnormal values in patients in remission but in most cases where both were elevated the patients subsequently entered a more active phase of the disease.

1. 1. The iron-bearing components obtained by chromatographic fractionation of human reticulocytes have been further studied in relation to their role in intracellular iron transport. 2. 2. In timed and chaser experiments membrane component A, like haemoglobin, behaved as an end product, while membrane component B1 and cytosol component C behaved as intermediates. 3. 3. We confirm that component B2, molecular weight 230 000, behaves as a complex of iron-transferrin and its membrane binding site. 4. 4. Sulphydryl inhibition with p- hydroxymercuribenzoate does not affect iron-transferring binding, but blocks the pathway between components B2 and B1 leading to an accumulation of the iron-transferrin-receptor complex. 5. 5. The results suggest that initially iron moves from the iron-transferrin-receptor complex (B2) to membrane component B1 from which it may diverge into membrane component A or follow the main pathway through cytosol component C to haemoglobin.

In serum-free cultures of phytohemagglutinin-stimulated human lymphocytes, iron transferrin causes enhanced uptake of both tritiated thymidine and tritiated uridine over that seen with only phytohemagglutinin. This effect is specific for the iron transferrin complex, no enhancement produced by either free iron(III) or apotransferrin. Iron bound to transferrin is quantitatively taken up by stimulated lymphocyte cultures, while under similar conditions only 10% of transferrin-bound zinc is incorporated. The relative specificity of action of iron and zinc on nucleic acid synthesis is discussed.

Transferrin determination was performed in 100 native human sera by RID, laser nephelometry and kinetic turbidimetry; the serum iron-saturation ranged between 0.03 and 1.00. No statistical difference could be observed between 3 immunochemical methods.

Iron transferrin, the highly stable carrier of plasma iron, may be dissociated, under physiological conditions, by sodium thioglycollate, a reaction which involves the formation of iron thioglycollate complexes. This suggested that sulphydryl radicals, which are the active groups in thioglycollate and related compounds, may play a part in the uptake of iron by immature red cells from iron transferrin. If this were so, it could be predicted that the sulphydryl inhibitor, p-hydroxymercuribenzoate, would depress the uptake of iron by reticulocytes. It is demonstrated here that inhibition of uptake of transferrin-bound iron by reticulocytes, which have been exposed to micromolar concentration of p-hydroxymercuribenzoate, is virtually complete. It is suggested that sulphydryl-containing compounds are intimately involved in the process of iron uptake by immature red cells.

Summary Previous electron paramagnetic resonance (e.p.r.) studies [1,2] have been used to demonstrate the formation of an iron transferrin complex in the absence of bicarbonate. In direct contrast, our findings are first, that there is no e.p.r. evidence for complex formation between ferric ions and transferrin in the absence of bicarbonate and second, that the e.p.r. signals which are said to be characteristic of bicarbonate-free iron transferrin are indistinguishable from those of ferric citrate complexes. A simple purification step for the removal of low-molecular-weight chelating agents from transferrin and conalbumin is suggested.

Iron metabolism is altered in critically ill patients leading to hypoferremia. Several studies related it to inflammatory response [1,2]. The present study aims to evaluate iron, transferrin and ferritin serum levels in patients with severe sepsis and septic shock and its association with severity of organ dysfunction.

SummaryOsteoclasts are the primary cells that resorb bone; they require high energy levels to degrade bone matrix, releasing minerals to maintain calcium homeostasis. Recent work on osteoclast differentiation and activity highlights an important role for mitochondrial biogenesis and explores the role of iron transferrin in generating a positive osteoclastogenic feedback loop.