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PubMed1990

Further studies on selective radioprotection by organic zinc salts and synergism of zinc aspartate with WR 2721.

The organic zinc salts zinc aspartate, zinc histidine, zinc orotate and zinc acetate reduced the fall of the haematocrit, thrombocytes, erythrocytes and leucocytes in irradiated mice. In general, zinc aspartate was more effective than the other organic zinc salts. Protection of the haematocrit and thrombocytes by small doses of the aminothiol radioprotector WR 2721 was markedly improved by the concomitant administration of small doses of zinc aspartate. Zinc aspartate was the only one of the four tested organic zinc salts that did not inhibit in any instance the regression induced by radiotherapy of human tumours grown as xenografts in immunosuppressed mice. This also applied to the combination of zinc aspartate with WR 2721. In an experiment performed to determine the toxicity of the combined regimen, a dose of zinc aspartate which afforded synergistic haematological protection did not enhance the toxicity of WR 2721. The synergism of zinc aspartate with WR 2721 and the differential radioprotection of the combined protocol may make it possible in clinical cancer radiotherapy to obtain selective radioprotection at a lower toxicity giving an improved therapeutic ratio compared with WR 2721 alone.

Acetates↗

PubMed2005

Single zinc-finger extension: enhancing transcriptional activity and specificity of three-zinc-finger proteins.

In order to demonstrate that an existing zinc-finger protein can be simply modified to enhance DNA binding and sequence discrimination in both episomal and chromatin contexts using existing zinc-finger DNA recognition code data, and without recourse to phage display and selection strategies, we have examined the consequences of a single zinc-finger extension to a synthetic three-zinc-finger VP16 fusion protein, on transcriptional activation from model target promoters harbouring the zinc-finger binding sequences. We report a nearly 10-fold enhanced transcriptional activation by the four-zinc-finger VP16 fusion protein relative to the progenitor three-finger VP16 protein in transient assays and a greater than five-fold enhancement in stable reporter-gene expression assays. A marked decrease in transcriptional activation was evident for the four-zinc-finger derivative from mutated regulatory regions compared to the progenitor protein, as a result of recognition site-size extension. This discriminatory effect was shown to be protein concentration-dependent. These observations suggest that four-zinc-finger proteins are stable functional motifs that can be a significant improvement over the progenitor three-zinc-finger protein, both in terms of specificity and the ability to target transcriptional function to promoters, and that single zinc-finger extension can therefore have a significant impact on DNA zinc-finger protein interactions. This is a simple route for modifying or enhancing the binding properties of existing synthetic zinc-finger-based transcription factors and may be particularly suited for the modification of endogenous zinc-finger transcription factors for promoter biasing applications.

Base Sequence↗

PubMed2000

[The effects of zinc supplementation on postburn nutritional status of zinc-deficient scalded rats].

OBJECTIVE: To investigate the effects of zinc supplementation on postburn nutritional status of zinc-deficient scalded rats. METHODS: Weanling Wistar rats were fed with zinc-deficient diets for one week to induce zinc-deficient status. The rats were inflicted with 20% TBSA deep partial thickness burn and thereafter fed with diets of low, normal and high zinc contents. The scalded rats fed with normal zinc-containing diet before and after injury were taken as normal control group. The changes of body weight, cumulative nitrogen balance and the contents of DNA and protein in jejunum mucous, liver, kidneys, spleen and testis were employed to represent the nutritional status of the rats. RESULTS: The rats fed with diets with normal and high contents of zinc were superior to those with low content of zinc in terms of body weight, food conversion rate, cumulative nitrogen balance and organ protein contents. The serum zinc level, alkaline phosphatase (ALP) activity and the DNA contents in jejunum mucous, kidneys, spleen and testis increased significantly after zinc supplementation. CONCLUSION: Zinc supplementation was helpful to improve postburn nutritional status in scalded rats. And relative higher amount of zinc supplementation might be beneficial to raise the DNA content in testis and kidneys when compared to that with normal zinc supplement.

Animals↗

PubMedDate not supplied

Ineffectiveness of zinc gluconate nasal spray and zinc orotate lozenges in common-cold treatment: a double-blind, placebo-controlled clinical trial.

BACKGROUND: Zinc gluconate and zinc acetate lozenges have been reported to shorten the duration of common colds in a dose-response manner when the amount of the active ingredient, positively charged zinc ions, is sufficient. OBJECTIVE: To improve results using a zinc gluconate nasal spray with zinc orotate lozenges. DESIGN: Double-blind, placebo-controlled clinical trial. SETTING: Private physician's clinic in Austin, Texas. PARTICIPANTS: Seventy-seven volunteers, all of whom had 2 or more signs and symptoms of common colds (with at least 1 nasal symptom) on enrollment in the study. METHODS: Zinc gluconate nasal spray (10 mmol) or placebo was used every 15 to 30 minutes, and lozenges were used each several hours to reduce duration and severity of common colds. An intention of treatment was to keep the nasal tissues wet with zinc gluconate solution during wakeful hours. RESULTS: After 7 days of treatment, 10 of 16 (63%) zinc-treated patients were asymptomatic compared to 9 of 17 (53%) placebo-treated patients (P = .57). This treatment caused olfactory region pain in some patients and did not reduce the duration or severity of common colds. Treatment did not produce anosmia, which has been reported in other studies following olfactory region administration of ionic zinc in many species and in humans from zinc nasal sprays and gels. CONCLUSION: We contend that it is unethical to introduce any potentially permanent anosmia-inducing agent such as zinc or other heavy metals into the interior of the nose in a manner that could result in contact with the olfactory region to treat a temporary discomfort such as a common cold or allergy. We found no reason to recommend intranasal zinc gluconate or zinc orotate lozenges in treating common colds.

Administration, Intranasal↗

PubMed1989

Zinc in mononuclear leucocytes in alcoholics with liver cirrhosis or chronic pancreatitis and in patients with Crohn's disease before and after zinc supplementation.

Mononuclear leucocyte zinc was determined together with serum zinc, albumin and serum alkaline phosphatase activity before and after zinc supplementation (2 x 50 mg of zinc-gluconate daily during 3 months) in patients with alcoholic liver cirrhosis (n = 10), alcoholic chronic pancreatitis (n = 10) and Crohn's disease (n = 10). Initial mononuclear leucocyte zinc concentrations did not differ between the patient groups and the reference group (n = 10), whereas initial serum zinc values were lower in the patients with alcoholic liver cirrhosis and Crohn's disease. This difference disappeared, however, when serum zinc concentrations were corrected for albumin levels, which were lower in all the patient groups. Higher initial activity of serum alkaline phosphatase was found in the alcoholic patients. In all the patient groups serum zinc concentrations increased significantly after zinc supplementation. Only in patients with Crohn's disease was there also an increase in serum alkaline phosphatase and albumin. Mononuclear leucocyte zinc did not respond to zinc supplementation in any of the patient groups. The results of our study indicate that mononuclear leucocyte zinc is not a sensitive indicator of marginal zinc deficiency.

Adult↗

PubMed1993

Zinc taste test in pregnant women and its correlation with serum zinc level.

Pregnant women in different trimesters of pregnancy were divided into control (n = 58) and study (n = 104) groups. Study group subjects were given 45 mg zinc/p.o./day as 200 mg 'zinc sulphate tablets from the day of reporting till term. Body zinc status was clinically assessed by 'zinc taste test'. Blood samples were drawn at the same time and serum zinc levels measured. Zinc taste test scores decreased with advancement of pregnancy (P < 0.05) and increased significantly following zinc administration (P < 0.05). Serum zinc level declined significantly with advancement of pregnancy (P < 0.001). Following zinc administration, serum zinc level increased significantly (P < 0.001). Accuracy of zinc taste test in individual cases ranged between 70 and 100 percent. On the whole, zinc taste test was well correlated with serum zinc level, and provides a fair idea of zinc deficiency.

Administration, Oral↗

PubMed1998

A binding shift assay for the zinc-bound and zinc-free HIV-1 nucleocapsid protein by capillary electrophoresis.

Affinity capillary electrophoresis was used to detect a shift in mobility when a zinc ion binds to the highly basic nucleocapsid protein (NCp7) of HIV-1. NCp7 contains two Cys-X2- Cys-X4-His-X4-Cys zinc fingers. With constant concentrations of NCp7 as a receptor and various concentrations of zinc as a ligand in the sample buffer and the electrophoresis buffer, we observed changes in electrophoretic mobilities of NCp7 protein when complexes were formed with zinc. Scatchard analysis of the mobility indicates the presence of at least two types of binding sites for zinc. At pH 6.0, one site is shown to bind zinc strongly with a binding constant Kb = 3.25 x 10(5) M-1 and the second site has a Kb = 1.8 x 10(5) M-1. The binding of zinc to the first zinc finger decreased the affinity of zinc for the second zinc finger approximately twofold. The Hill coefficient for this negative cooperativity is 0.9. A series of NCp7 mutants were also examined in the assay to determine their ability to bind zinc. This assay affords a quick method to observe a zinc ion binding to NCp7 and to calculate binding constants.

Amino Acid Sequence↗

PubMed1983

Effect of low-dose androgen and zinc sulfate on sperm motility and seminal zinc levels in infertile men.

Beneficial effects of zinc therapy in some infertile patients with low seminal zinc concentrations and decreased sperm motility have been reported recently. The effects of zinc therapy, low-dose (5-10 mg/day) androgen therapy, and combination therapy of both zinc and low-dose androgen, on sperm motility and seminal zinc concentration were studied in patients referred to the andrology clinic. Low-dose androgen therapy increased seminal zinc concentrations and sperm motility, only when pretreatment seminal zinc concentrations were low. Furthermore, patients with low seminal zinc concentrations and poor sperm motility showed greater improvement of sperm motility and seminal zinc levels in response to zinc sulfate with fluoxymesterone than did fluoxymesterone alone or zinc sulfate alone, possible due to a synergistic effect of zinc and androgen.

Fluoxymesterone↗

PubMed2002

Contribution of individual zinc ligands to metal binding and peptide folding of zinc finger peptides.

Little is known about the contribution of individual zinc-ligating amino acid residues for coupling between zinc binding and protein folding in zinc finger domains. To understand such roles of each zinc ligand, four zinc finger mutant peptides corresponding to the second zinc finger domain of Sp1 were synthesized. In the mutant peptides, glycine was substituted for one of four zinc ligands. Their metal binding and folding properties were spectroscopically characterized and compared to those of the native zinc finger peptide. In particular, the electronic charge-transfer and d-d bands of the Co(II)-substituted peptide complexes were used to examine the metal coordination number and geometry. Fluorescence emission studies revealed that the mutant peptides are capable of binding zinc despite removing one ligand. Circular dichroism results clearly showed the induction of an alpha-helix by zinc binding. In addition, the structures of certain mutant zinc finger peptides were simulated by molecular dynamics calculation. The information indicates that His23 and the hydrophobic core formed between the alpha-helix and the beta-sheet play an essential role in alpha-helix induction. This report demonstrates that each ligand does not contribute equally to alpha-helix formation and coordination geometry in the zinc finger peptide.

Amino Acid Sequence↗

PubMed1972

Zinc transport in rabbit tissues. Some hormonal aspects of the turnover of zinc in female reproductive organs, liver and body fluids.

1. To investigate the influence of hormonal conditions upon the kinetics of zinc transport, specific radioactivity of (65)Zn was determined in certain tissues and fluids from unmated or pregnant rabbits during the first half of gestation. 2. Compartmental analysis was used to find the simplest mathematical model that simulated satisfactorily tracer behaviour. Models were fitted to experimental results by a numerical procedure using a computer. 3. The kinetics of zinc exchange in most tissues investigated could adequately be described by a three-compartment model, in which total tissue zinc content was divided into a rapidly exchanging pool, with a turnover time of about 1h, and a slowly exchanging pool, the turnover time of which was in liver 15h, in peak-stage corpus luteum 8h, and in the other tissues 30-70h. 4. In rabbit endometrium zinc transport varied with hormonal conditions, the turnover rate being higher in non-pregnant than pregnant endometrium. 5. Uptake of (65)Zn by uterine fluid was slow, and in the free-lying embryos (blastocysts) slower still, in keeping with uterine fluid acting as carrier of zinc into the unimplanted embryos. 6. In placental tissue zinc transport varied with gestational stage. Foetal placenta exchanged zinc with blood plasma four times faster than maternal placenta. In foetuses zinc turnover time and flux equalled that of the slow zinc compartment in foetal placenta. 7. Corpus luteum on days 5-6 of gestation showed peak specific radioactivity and zinc flux values, which exceeded those of all other tissues. 8. In liver the slow zinc compartment had a higher rate of turnover than corresponding compartments in tissues other than peak-stage corpus luteum, but no hormone-dependent changes were observed. 9. Zinc uptake by erythrocytes was the slowest of all examined.

Animals↗

PubMed2006

Zinc binding to a regulatory zinc-sensing domain monitored in vivo by using FRET.

We have generated probes of metal binding to zinc fingers (ZFs) that provide tools to study zinc trafficking in vivo. In this study, we used these probes to examine zinc binding by the Zap1 transcription factor of Saccharomyces cerevisiae. Zap1 contains two zinc-regulated activation domains (ADs), AD1 and AD2. AD2 is located within two C2H2 ZFs, ZF1 and ZF2. Studies have indicated that apoAD2 activates transcription and zinc binding to ZF1 and that ZF2 forms an interacting-finger-pair structure that is necessary to inhibit AD function. A related structural finger pair, ZF3 and ZF4, is found in the Zap1 DNA binding domain. In vitro studies indicated that, although the ZF1/2 and ZF3/4 finger pairs bind zinc with similar affinities, zinc that was bound to ZF1/2 was much more labile. We examined the properties of Zap1 ZFs in vivo by FRET. ZF pairs were flanked by enhanced yellow fluorescent protein and enhanced cyan fluorescent protein, allowing detection of zinc-induced conformation changes by FRET. By using these reporters, we found that ZF1/2 and ZF3/4 showed similar responses to zinc under steady-state conditions in vivo. In contrast, ZF1/2 zinc binding was significantly more labile than was ZF3/4. Also, ZF1/2 accumulated in an apo form that could rapidly bind zinc, whereas the ZF3/4 pair did not. Last, we show that these properties are evolutionarily conserved indicating their importance to Zap1 function. These results indicate that the kinetic lability of ZF1/2 in vivo is a key component of Zap1 zinc responsiveness.

Amino Acid Sequence↗

PubMed2001

A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity.

Zinc is essential for many cellular processes, including DNA synthesis, transcription, and translation, but excess can be toxic. A zinc-induced gene, smtA, is required for normal zinc-tolerance in the cyanobacterium Synechococcus PCC 7942. Here we report that the protein SmtA contains a cleft lined with Cys-sulfur and His-imidazole ligands that binds four zinc ions in a Zn(4)Cys(9)His(2) cluster. The thiolate sulfurs of five Cys ligands provide bridges between the two ZnCys(4) and two ZnCys(3)His sites, giving two fused six-membered rings with distorted boat conformations. The inorganic core strongly resembles the Zn(4)Cys(11) cluster of mammalian metallothionein, despite different amino acid sequences, a different linear order of the ligands, and presence of histidine ligands. Also, SmtA contains elements of secondary structure not found in metallothioneins. One of the two Cys(4)-coordinated zinc ions in SmtA readily exchanges with exogenous metal ((111)Cd), whereas the other is inert. The thiolate sulfur ligands bound to zinc in this site are buried within the protein. Regions of beta-strand and alpha-helix surround the inert site to form a zinc finger resembling the zinc fingers in GATA and LIM-domain proteins. Eukaryotic zinc fingers interact specifically with other proteins or DNA and an analogous interaction can therefore be anticipated for prokaryotic zinc fingers. SmtA now provides structural proof for the existence of zinc fingers in prokaryotes, and sequences related to the zinc finger motif can be identified in several bacterial genomes.

Amino Acid Sequence↗

PubMed2005

The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus.

It has been suggested that ZIP7 (Ke4, Slc39a7) belongs to the ZIP family of zinc transporters. Transient expression of the V5-tagged human ZIP7 fusion protein in CHO cells led to elevation of the cytoplasmic zinc level. However, the precise function of ZIP7 in cellular zinc homeostasis is not clear. Here we report that the ZIP7 gene is ubiquitously expressed in human and mouse tissues. The endogenous ZIP7 was associated with the Golgi apparatus and was capable of transporting zinc from the Golgi apparatus into the cytoplasm of the cell. Moreover, by using the yeast mutant strain Deltazrt3 that was defective in release of stored zinc from vacuoles, we found that ZIP7 was able to decrease the level of accumulated zinc and in the meantime to increase the nuclear/cytoplasmic labile zinc level in the ZIP7-expressing zrt3 mutant. We showed that the protein expression of ZIP7 was repressed under zinc-rich condition, whereas there were no effects of zinc on ZIP7 gene expression and intracellular localization. Neither did zinc deficiency affect the intracellular distribution of ZIP7 in mammalian cells. Our study demonstrates that ZIP7 is a functional zinc transporter that acts by transporting zinc from the Golgi apparatus to the cytoplasm of the cell.

Animals↗

PubMed1989

Zinc, copper and iron utilisation by chicks fed various concentrations of zinc.

1. Zinc, iron and copper interactions were examined in chicks (New Hampshire X Single Comb White Leghorn) grown individually in stainless steel cages and fed on purified diets with three concentrations of zinc: control (37 mg Zn/kg), moderate (100 mg Zn/kg) and excess (2000 mg Zn/kg) in three studies. 2. Chicks given either moderate or excess zinc excreted more than twice as much 65Zn from a test diet as those fed on the control diet. Thus chicks given the moderate amount of zinc had concentrations of zinc in tissues similar to those of controls but chicks given excess zinc accumulated zinc in their tissues. 3. The specific activity of 65Zn in the tissues, especially in the bursa of Fabricius, of chicks given excess zinc was not reduced as much as would be predicted. Thus, ingestion of excess zinc appeared to reduce tissue turnover of 65Zn, especially in the bursa. However, humoral immune responses, as measured by antibody titres to sheep red blood cells, were not affected. 4. Chicks given excess zinc or pair-fed on the control diet retained less 59Fe from a test diet than chicks given control or moderate concentrations of zinc ad libitum. The iron concentrations in tibiae of chicks given excess zinc were depressed.

Animal Feed↗

PubMed2006

Predicting bioavailable zinc from lower phytate forms, folic Acid and their interactions with zinc in vegetarian meals.

OBJECTIVE: To develop a statistical model for predicting zinc bioavailability from cereal-based vegetarian meals using relative proportion of nutrients, non-nutrients and their interactive effects. METHODS: A database on in vitro zinc dialysability (by isotopic tracer, 65Zn) of vegetarian meals (266 out of 326) from Asia, Africa, Europe /US and Latin America was used to develop a model for estimating zinc bioavailability. A multiple regression analysis adjusted for energy content was carried out for net bioavailable zinc from a meal with the predictor variables as meal contents of iron, zinc, copper, ascorbic acid, beta-carotene, riboflavin, thiamine, folic acid, tannic acid, fiber, phytate degradation products (IP6 to IP1), along with their interaction terms. Reproducibility of the model was tested with remaining 60 meals. Validation of the model was done with zinc absorption data of i) 12 young adults on 24 meals and ii) 5 adults with ileostomy on 7 meals. RESULTS: Folic acid, IP3 and IP5 were significant influencing factors for bioavailable zinc. Weighted multiple regression equation was: ln (bioavailable zinc in mg) = -1.701 + 1.285 x ln [(IP5 in mg] x (Zn in mg)] -1.222 x ln(IP5 in mg) -0.0078 x folic acid in microg -0.137 x ln [(IP3 in mg) x (Zn in mg)] with adjusted R--[2] = 0.64, p = 0.0001. The correlation between predicted and observed dialysability of meals was found to be 0.96 (p < 0.01). A significant correlation between observed and predicted amount of absorbed zinc (r = 0.85, p < 0.01) was obtained for the human data of zinc absorption in 12 healthy and 5 subjects with ileostomy. CONCLUSIONS: Bioavailable amount of zinc from vegetarian meals was influenced by IP3, IP5 and folic acid content and their interactive effect with zinc content.

Adult↗

PubMed1985

Does the oral zinc tolerance test measure zinc absorption?

Increases in plasma zinc concentration were compared with radiozinc absorption after oral test doses. Ten healthy, fasting subjects were each given 385 mumol zinc chloride (25 mg Zn) labelled with 0.5 muCi 65ZnCl2 and a non-absorbed marker, 51CrCl3, dissolved in 100 ml of water; another 10 persons were given 354 mumol zinc chloride and 125 g of minced turkey containing 31 mumol zinc also labelled with 65Zn and 51Cr. Measurements were made of plasma zinc concentration at hourly intervals for 5 hours, radiozinc absorption by stool counting of unabsorbed radioactivity 12-36 hours later, and radiozinc retention by whole body counting at 7 days. The mean percentage of radiozinc absorbed and retained in the body from the two test meals was found to be identical (42%). In contrast the increased area under the plasma zinc curve up to 5 hours after the turkey meal, 28 +/- 9 mumol/L (mean +/- SD) was significantly less than that for zinc chloride alone, 47 +/- 15 mumol/L, p less than 0.005. Despite this difference, a good correlation was found between the area under the plasma zinc curve and 65Zn absorption in individual subjects after each meal. The discrepancy between the results of zinc absorption derived from the plasma zinc curve and 65Zn absorption for the liquid and solid test meals was most likely explained by binding of zinc to food and delayed gastric emptying of the solid meal. With a test meal of turkey meat at least this dampened the plasma appearance of zinc but did not affect its overall absorption.

Administration, Oral↗

PubMed2006

Molecular cloning and functional characterization of novel zinc transporter rZip10 (Slc39a10) involved in zinc uptake across rat renal brush-border membrane.

Previously, in our laboratory a 40-kDa zinc transporter protein was purified and functionally reconstituted in proteoliposomes (Kumar R, Prasad R. Biochim Biophys Acta 1419: 23-32, 1999). Furthermore, we now report the identification of Slc39a10 cDNA encoding the 40-kDa zinc transporter protein by isolating a cloned DNA complementary to zinc transporter mRNA. cDNA was constructed from immunoenriched mRNA encoding the zinc transporter. cDNA was inserted into pBR322 using poly(dC)- poly(dG) tailing. Escherichia coli DH5alpha cells were transformed, and colonies were screened for zinc transporter cDNA by insertional inactivation. Plasmid DNA was purified from the ampicillin-sensitive clones, and the cDNA was sequenced from both strands. A basic local alignment research tool (BLAST) search of cDNA revealed that it belongs to the Slc39 gene family of zinc transporters and was designated as Slc39a10. Zinc transporter protein deduced on the basis of cDNA sequence was named rZip10 and consists of 385 amino acids with 9 predicted transmembrane domains. The Slc39a10 gene was abundantly expressed in both rat and human tissues. Increased extracellular zinc concentration resulted in upregulation of Slc39a10 in LLC-PK(1) cells expressing rZip10, which was downregulated at higher zinc concentrations. These cells accumulated more zinc than control cells. rZip10-mediated zinc uptake activity was time-, temperature-, and concentration-dependent and saturable which followed Michaelis-Menten kinetics with a K(m) of 19.2 microM and V(max) of 50 pmol x min(-1) x mg protein(-1). This activity was competitively inhibited by cadmium with K(i) of 91 microM. rZip10-mediated zinc uptake was inhibited by COOH group-modifying agents such as DCC. Immunofluorescence studies showed that rZip10 localizes to the plasma membrane of LLC-PK(1) cells.

Amino Acid Sequence↗

PubMed1982

Maternal essential fatty acid supplementation increases zinc absorption in neonatal rats: relevance to the defect in zinc absorption in acrodermatitis enteropathica.

Pregnant zinc deficient and zinc adequate rats were injected subcutaneously with evening primrose oil throughout gestation and for 3 days post partum. The nursing pups were injected intragastrically with zinc-65 on day 3 of live and sacrifices 4 h later. The % of the total injected zinc recovered in the carcass (minus the gut and gut contents) was significantly increased in those pups nursed by mothers injected with evening primrose oil, regardless of their dietary zinc intake. The fatty acid composition of the total lipid extract of the gut and gut contents of the neonates with increased zinc-65 absorption indicated that these pups had higher proportions of arachidonic acid and other metabolites of linoleic acid than did those with lower zinc-65 absorption. In other 3-day-old rat pups, intragastric injection of linoleic, gamma-linolenic or dihomo-gamma-linolenic acids along with the dose of zinc-65 very significantly increased zinc-65 absorption in a dose-related manner. Arachidonic acid however had no significant effect on zinc-65 absorption. Prostaglandin E1 caused a significant increase in zinc-65 absorption but prostaglandin E2 had no consistent effect. Indomethacin caused a dose-related inhibition of zinc-65 absorption.

Acrodermatitis↗