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PubMed1984

Different enzyme classes associated with human natural killer cells may mediate disparate functions.

Previous studies have shown that degradation of the acute phase reactant serum amyloid A (SAA) is mediated by enzymes on the plasma membrane of lymphocytes and monocytes. The responsible enzymes had properties of neutral elastases. The present investigations were conducted to explore whether human NK cells enriched by Percoll gradient centrifugation have similar activity and if so, whether the same or different enzyme classes are responsible for proteolysis as well as for tumor cell lysis. Accordingly, human NK cells were enriched on discontinuous Percoll gradients after which the cells were incubated either with SAA or with [3H] proline-labeled melanoma cells at various effector to target cell ratios. When SAA degradation was followed by SDS-polyacrylamide gel electrophoresis, NK fractions proved to be as effective in digesting the protein as unfractionated mononuclear leukocytes. To characterize the enzymes that may be involved in cytotoxicity on the one hand, and SAA degradation on the other, the NK fractions were treated with the following inhibitors: diisopropylfluorophosphate (DFP), soybean trypsin inhibitor, N-p-tosyl-L-lysine chloromethylketone (TLCK), the elastase inhibitors elastatinal, Ac-Ala-Ala-Pro-Val-CH2Cl, Meo-Suc-Ala-Ala-Pro-Val-CH2Cl, and an inhibitor of aryl sulfatase, Na2SO4. Preincubation of the cells with DFP or elastase inhibitors abolished their ability to hydrolyze SAA but did not affect their ability to kill tumor cells. On the other hand TLCK, a potent inhibitor of cytotoxicity, did not bring about any reduction in the proteolysis of SAA. DFP and Na2SO4 diminished cytotoxicity partially. Elimination of NK cells by sorting after incubation of lymphocytes with the monoclonal antisera Leu-7 and Leu-11 abolished cytotoxicity as well as proteolysis. The observations are compatible with the concept that NK cells carry several enzymes with different substrate specificities that may be involved in disparate cellular functions.

Arylsulfatases↗

PubMedDate not supplied

[Effect of the medium on the functional and structural properties of serum albumins. I. Effect of ionic strength on N-variant of human serum albumin].

The effect of ionic strength on the 1-anilino-8- naphtalene sulfonate (ANS) binding sites of the N-form of human serum albumin (HSA) was studied by means of the protein and ligand fluorescence. The parameters of the binding of ANS to HSA (the number of sites and the binding constants) were determined by two methods: by measuring the ANS fluorescence either (i) at increasing protein concentrations and constant ANS concentration, or (ii) at increasing ANS concentration and two constant protein concentrations (9.6 and 2.53 microM). An increase in the NaCl concentration results in a monotonous decrease of the ANS fluorescence yield of HSA-ANS complex, which could be interpreted in terms of two different effects: first, the direct collisional quenching interaction of Cl-ions with bound ANS located on the surface of HSA and, second, the ca. 10 per cent decrease of the number of bound ANS molecules due to the lowering of the ANS-HSA association constant values. The fluorimetric titration showed that at low ionic strength (0.008 M NaCl) HSA molecule has one strong ( lgKaI = 6.75-7.25) and two secondary sites with lower affinity ( lgKaII = 6.35). The increase in the NaCl concentration results in a decrease of the affinity for both kinds of binding sites (in 0.2 NaCl lgKaI = 6.3-6.7; lgKaII = 5.6-5.9). In contrast with NaCl, Na2SO4 induces only a limited decrease of the ANS fluorescence occurring within a narrow concentration range (from ca. 0.02 to 0.05 M Na2SO4, e. i. at ionic strengths from 0.07 to 0.15) and which can be described as a cooperative interaction of six SO4(2)-ions with a HSA molecule.(ABSTRACT TRUNCATED AT 250 WORDS)

Anilino Naphthalenesulfonates↗

PubMed1983

Cold injury-induced swelling of brain and other tissues: its molecular mechanism.

Isolated mouse brain, kidney, and other tissues were incubated for from one to several days at 4 degrees C in isotonic solutions containing varying mixtures of sucrose and NaCl (or Na2SO4, LiCl, Li2SO4, MgSO4). The ischemic, cold-injured tissues swelled in proportion to the concentration of NaCl or LiCl. They swelled less in Na2SO4 and Li2SO4 and they swelled even less and/or shrank in MgSO4 or sucrose. It was shown that in the presence of about 100 mM NaCl, the degree of swelling follows inversely the level of ATP present in the cells. The data were interpreted using the theory of cell swelling based on the association-induction hypothesis: NaCl- and LiCl-induced swelling in injured tissues and KCl-induced swelling in normal tissues, were both explained as the consequence of the dissociation of the volume-restraining effects of salt linkages among cell proteins. The depletion of ATP and the consequent increase of electron density or c-value of the fixed anionic groups turns NaCl (ineffective in causing swelling of normal tissues) into a fully effective agent for causing swelling of the injured tissues.

Adenosine Triphosphate↗

PubMed1981

Rapid screening method for aflatoxin M1 in milk.

A rapid screening method for detecting aflatoxin M1 in milk has been developed, based on minicolumn chromatography and requiring 8-10 min for each test. The minicolumn is packed with dry Florisil (100-200 mesh) on the bottom, anhydrous Na2SO4 as the next layer, topped with neutral alumina (70-200 mesh) to which 8% water (wet basis) has been added. A blue fluorescent band at the Florisil-Na2SO4 interface indicates the presence of aflatoxin M1. The limit of detection is estimated to be about 0.2 microgram/kb. Because several items are disposable, both the time to maintain glassware and the cost per determination are reduced.

Aflatoxin M1↗

PubMed1980

The effect of osmotic pressure on the intestinal absorption of sulfafurazol and ethanol in the rat.

The aim of the present study was to extend our earlier research into the effect of osmotic pressure on the intestinal absorption of drugs. In the experiments rats and an in situ technique were used. Sulfafurazol and ethanol were test substances and osmotic pressure was adjusted by NaCl, KNO3 or Na2SO4. From the results it was concluded that if all other factors are excluded the effect of the osmotic pressure of the vehicle is such that an isotonic solution has the best extent of bioavailability. Bioavailability decreases both when osmotic pressure decreases and when it increases. However, the decreasing effect of hypertonic solutions is stronger than that of hypotonic solutions. Although NaCl, KNO3 and Na2SO4, are often mentioned as alternative salts for adjusting osmotic pressure they are not equal in respect of their ability to alter the absorption of a drug.

Animals↗

PubMed1996

Stability and folding of the SH3 domain of Bruton's tyrosine kinase.

Bruton's tyrosine kinase (BTK) plays an important role in B cell development. Deletion of C-terminal 14 amino acids of the SH3 domain of BTK results in X-linked agammaglobulinemia (XLA), an inherited disease. We report here on the stability and folding of SH3 domain of BTK. Peptides corresponding to residues 216-273 (58 residues) and 216-259 (44 residues) of BTK SH3 domain were synthesized by solid phase methods; the first peptide constitutes the entire SH3 domain of BTK while the latter peptide lacks 14 amino acid residues of the C-terminal. The 58 amino acid peptide forms mainly a beta-barrel type folding unit. Although small and lacking disulfide bonds, this peptide is extremely stable to thermal denaturation. Based on circular dichroism measurements, its melting temperature was found to be high, 82 degrees C at pH 6.0. However, the Gibbs free energy (delta GH2O) of the intrinsic stability and thermodynamic spontaneity of unfolding were found to be low, 2.6 kcal/mol by Gdn.HCl denaturation experiments, as compared to 12 kcal/mol obtained for larger single domain proteins, indicating poor stability of SH3 domain. Addition of 500 mM of Na2SO4 increased the free energy change delta GH2O to 4.0 kcal/mol, suggesting an ionic strength effect. The truncated peptide fails to fold correctly and adopts random coil conformation in contrast to 58 amino acid beta-barrel peptide, which exhibits high thermal stability but normal or low stability at ambient temperature. These results, to our knowledge the first to delineate the importance of C-terminal in structural integrity of SH3 domains, indicate also that improper folding and/or poor stability of mutant SH3 domain in BTK likely causes XLA.

Agammaglobulinaemia Tyrosine Kinase↗

PubMed1998

UV resonance Raman spectroscopy of DNA and protein constituents of viruses: assignments and cross sections for excitations at 257, 244, 238, and 229 nm.

Ultraviolet resonance Raman (UVRR) spectra of H2O and D2O solutions of the nucleoside (dA, dG, dC, dT) and aromatic amino acid (Phe, Trp, Tyr) constituents of DNA viruses have been obtained with laser excitation wavelengths of 257, 244, 238, and 229 nm. Using the 981 cm-1 marker of Na2SO4 as an internal standard, Raman frequencies and scattering cross sections were evaluated for all prominent UVRR bands at each excitation wavelength. The results show that UVRR cross sections of both the nucleosides and amino acids are strongly dependent on excitation wavelength and constitute sensitive and selective probes of the residues. The results provide a library of UVRR marker bands for structural analysis of DNA viruses and other nucleoprotein assemblies.

DNA Viruses↗

PubMed1999

Thymic epithelial cells synthesize a heparan sulfate with a highly sulfated region.

Epithelial cells are important components of the thymus microenvironment and are involved in thymocyte differentiation. The production and secretion of sulfated glycosaminoglycans by these cells grown in culture were investigated using labeling with radioactive 35S-Na2SO4 and 3H-glucosamine. The major glycosaminoglycans synthesized by these cells are heparan sulfate and hyaluronic acid. The structure of the heparan sulfate was investigated by the pattern of degradation products formed by deaminative cleavage with nitrous acid. The ratio 35S-sulfate/ H-glucosamine is high in the segments of the heparan sulfate released during the deaminative cleavage with nitrous acid but low in the resistant portion of the molecule. Thus, the heparan sulfate synthesized by the thymic epithelial cells contains a highly sulfated region. Digestion with heparitinase reveals that this highly sulfated region is a heparin-like segment of the molecule. The heparan sulfate is rapidly incorporated into the cell surface but its secretion to the extracellular medium requires a longer incubation period. Finally, heparin was used to mimic the possible effect of this heparan sulfate with a highly sulfated region, as ascertained by its ability to modulate thymocyte adhesion to thymic epithelial cells. Since heparin actually enhanced thymocyte adhesion, it is suggested that the heparan sulfate described herein, secreted by the thymic epithelium, may play a role upon intrathymic heterotypic cellular interactions.

Animals↗

PubMed2001

Durability of sodium sulfate-treated polylysine-alginate microcapsules.

Chelated hollow microcapsules are unstable under in vitro conditions because of their hygroscopic nature. Nongel inducing cations, such as Na+, stabilize the outer membrane of the alginate-polylysine-alginate microcapsules leading to more stable beads. We made different batches of empty capsules with a mean +/- SEM diameter of 607+/-11 microns, and found that within 1 week of incubating these capsules in normal saline at 37 degrees C, they increased to 718+/-10 microns (p < 0.05, n = 5). In initial experiments, we made different batches of capsules and divided them into two groups. One group was left untreated (control) whereas the other was treated with 6 mM Na2SO4 for 30 min, before incubation in saline at 37 degrees C. Control capsules increased in weight and size, before beginning to melt in less than 1 week. In contrast, treated capsules rapidly lost weight and remained intact during 1 month of follow-up. In perifusion experiments, we found no deleterious effect of sodium sulfate treatment on the function of islets enclosed in the capsules.

Absorbable Implants↗

PubMed2005

Adsorption of biopolymers at hydrophilic cellulose-water interface.

The extent of adsorption (Gamma2(1)) of bovine serum albumin (BSA), beta-lactoglobulin, lysozyme, gelatin, and DNA from aqueous solution onto the hydrophilic surface of cellulose has been measured as function of biopolymer concentration at different temperatures, pHs, and ionic strengths, and in the presence of a high concentration of inorganic salts and denaturants. In all cases, the value of Gamma2(1) increases with the increase of biopolymer concentration (X2) in bulk and it attains a maximum value at a critical mole fraction concentration X2m. The value of Gamma2m depends upon the nature of protein, temperature, pH, and ionic strength, as well as the nature of neutral salts present in excess. Gamma2m for proteins at a fixed physicochemical condition stands in the following order: Gelatin>betalactoglobulin>lysozyme>BSA. The isotherms for adsorption of DNA nucleotides on cellulose surface at pH 4.0 have been compared at different temperatures and ionic strengths, and in the presence of high concentration of inorganic salts LiCl, NaCl, KCl, and Na2SO4. Values of Gamma2m for different systems have been evaluated and critically compared. At pH 6.0 and 8.0, Gamma2(1) values of DNA nucleotides on cellulose are all negative due to the excess positive hydration of cellulose. At pH 4.0, adsorption of nucleotides of acid, alkali, and heat-denatured DNA widely differ from each other and in the presence of excess concentration of urea becomes negative. The probable mechanisms of biopolymer-cellulose adsorption in terms of polymer hydration, steric interaction, London-van der Waals, hydrophobic, and other types of interactions have been discussed qualitatively. The standard free energy change for the adsorption of protein and DNA nucleotides on the cellulose surface at the state of adsorption saturation has been calculated in kJ per kg of cellulose using an integrated form of the Gibbs adsorption equation. The relation between DeltaG degrees and maximum affinities between biopolymers and the polysaccharide interface have been discussed for various systems.

Adsorption↗

PubMed2006

Synthesis of DL-alanine hollow tubes and core-shell mesostructures.

Three double hydrophilic block copolymers were used as crystal-growth modifiers of DL-alanine to generate amorphous precursor nanoparticles that undergo subsequent mesoscopic transformation to core-shell mesostructures and hollow tubes with quadratic cross-sections. The growth sequence can be stopped at various stages so that a series of intermediates between amorphous core- and crystalline-shell particles and tubes can be obtained. Time-dependent conductivity, TEM, SEM, and environmental scanning electron microscopy (ESEM) measurements were used to obtain a better understanding of the crystallization process, and a formation mechanism for the generation of the tubes is proposed. Na2SO4, NaCl, and NaNO3 as salts differ in their influence on the crystallization behavior of alanine by changing the solubility of alanine and by decreasing the stability of the intermediate particles. Core-shell mesostructures that formed in the dissolution-recrystallization process were captured as the transformation rate was decreased by the addition of copolymers or salts. Hollow tubes with quadratic cross-sections are the final product of the transformation process.

Alanine↗

PubMed1994

Complex intermolecular interactions maintain a stable linkage between the photoreceptor connecting cilium axoneme and plasma membrane.

Microtubule-membrane cross-linkers in motile and nonmotile cilia are supramolecular structures, held together by strong interactions between the constituent molecules. We have characterized these interactions in the photoreceptor connecting cilium, where cross-linkers co-fractionate and maintain their in situ location after Triton X-100 extraction of axonemes. In bovine photoreceptor cells, the transmembrane assemblage that is cross-linked to the connecting cilium axoneme contains three high molecular mass glycoconjugates of 425, 600, and 700 kDa (Horst et al., 1987). The relative amounts of the three glycoconjugates, as judged from band intensity in electrophoretograms, depend strongly on sample treatment prior to electrophoresis. The electrophoretic pattern was reproducible after several weeks of storage of the axoneme fraction in extraction buffer containing 50% sucrose. Removal of sucrose from the buffer by dialysis eliminated the 600 kDa and 700 kDa, and decreased the detected amount of the 425 kDa glycoconjugate. When samples were incubated in Laemmli sample buffer at increasing temperatures (23 degrees, 60 degrees, 95 degrees C), a gradual reduction in the intensity of the three bands was observed. The quantitative reduction of high molecular mass glycoconjugates was accompanied by the appearance of novel protein species of lower molecular mass, as detected by lectin and antibody overlays of axonemal transblots. These results suggest that the previously characterized cross-linker glycoconjugates are complex, SDS-resistant multi-molecular conglomerates. We have further used fluorescent lectins to monitor the presence of glycoconjugates on whole-mounted axonemes, in conditions aimed to selectively solubilize the cross-linkers. The cross-linker complexes could not be dissociated from the axoneme by incubation with buffers containing 1 M of either Na2SO4 or NaI. The results indicate that the connecting cilium-specific cross-linker complexes are bound via high-affinity interactions to both axoneme and overlying plasma membrane.

Animals↗

PubMed1988

Immobilized pH gradients: effect of salts, added carrier ampholytes and voltage gradients on protein patterns.

Salts formed from strong acids and bases (e.g. NaCl, Na2SO4, Na2HPO4), present in a protein sample applied to an immobilized pH gradient (IPG) gel, induce protein modification (oxidation of iron moiety in hemoglobin) already at low levels (5 mM) and irreversible denaturation (precipitation) at higher levels (greater than 50 mM). This effect is due to production of strongly alkaline cationic and strongly acidic anionic boundaries formed by the splitting of the salt's ion constituents, as the protein zone is not and can not be buffered by the surrounding gel until it physically migrates into the gel matrix. Substitution of "strong" salts in the sample zone with salts formed by weak acids and bases, e.g.. Tris-acetate, Tris-glycinate, Good's buffers such as (N-[2-acetamido]-2-iminodiacetic acid (ADA), (2-[(2-amino-2-oxoethyl)-amino] ethanesulfonic acid (ACES), (3-[N-morpholino]propane sulfonic acid (MOPS), essentially abolishes both phenomena, oxidation and irreversible denaturation. Suppression of "strong" salt's effects is also achieved by adding, to the sample zone, carrier ampholytes in amounts proportional to the salt present (e.g. by maintaining a salt: carrier ampholytes molar ratio of at least 1:1). This suppression is due to the strong buffering power of the added carrier ampholytes, able to counteract drastic pH changes in the two moving boundaries. A reduction of these deleterious effects of strong salts is also achieved when the IPG run is performed at low voltage for a prolonged time (4 h at 500 V instead of only 1 h at 500 V, before switching to high-voltage settings). Guidelines are given for trouble-free IPG operations.

Ampholyte Mixtures↗

PubMed2004

Effect of acetylation and succinylation on solubility profile, water absorption capacity, oil absorption capacity and emulsifying properties of mucuna bean (Mucuna pruriens) protein concentrate.

Mucuna protein concentrate was acylated with succinic and acetic anhydride. The effects of acylation on solubility, water absorption capacity, oil absorption capacity and emulsifying properties were investigated. The pH-dependent solubility profile of unmodified mucuna protein concentrate (U-mpc) showed a decrease in solubility with decrease in pH and resolubilisation at pH values acidic to isoelectric pH (pH 4). Apart from pH 2, both acetylated mucuna protein concentrates (A-mpc) and succinylated mucuna protein concentrate (S-mpc) had improved solubility over the unmodified derivative. Acylation increased the water absorption capacity (WAC) at all levels of ionic strength (0.1-1.0 M). WAC of the protein samples increased with increase in ionic strength up to 0.2 M after which a decline occurred with increase in ionic strength from 0.4-1.0 M. When protein solutions were prepared in salts of various ions, increase in WAC followed the Hofmeister series in the order: NaSCN < NaClO4 < NaI < NaBr < NaCl < Na2SO. Acetylation improved the oil absorption capacity while the lipophilic tendency reduced the following succinylation. Emulsifying capacity increased with increase in concentration up to 2, 4 and 5% w/v for U-mpc, A-mpc and S-mpc, respectively, after which an increase in concentration reduced the emulsifying capacity. Both acetylation and succinylation significantly (P < 0.05) improved the emulsifying capacity at pH 4-10. Initial increase in ionic strength up to 0.4 M for U-mpc and 0.4 M for A-mpc and S-mpc increased the emulsion capacity progressively. Further increase in ionic strength reduced emulsion capacity (EC). Contrary to the effect of various salts on WAC, increase in EC generally follows the series Na2SO4 < NaCl < NaBr < NaI < NaClO4 < NaSCN. At all levels of ionic strength studied, S-mpc had a better emulsifying activity (EA) than both A-mpc and U-mpc. EA and emulsifying stability (ES) were pH-dependent. Maximum EA and ES were recorded at pH 10. ES of protein derivatives were higher than those of U-mpc in the range of pH 4-10 but lower at pH 2. Studies revealed that both A-mpc and S-mpc had better ES and EA than the unmodified derivative when protein solutions were prepared in salts of various anions.

Absorption↗

PubMed1992

Biglycan and decorin gene expression in normal and fibrotic rat liver: cellular localization and regulatory factors.

The expression of genes encoding the core proteins of the novel small chondroitin/dermatan sulfate proteoglycans decorin and biglycan was studied in the livers of normal rats and in liver tissue during fibrogenesis induced by prolonged bile-duct ligation and thioacetamide poisoning. The cell types responsible for the expression of these transcripts and some key regulatory factors were identified. Both biglycan and decorin messenger RNAs were detected in normal liver tissue. Their relative abundance increased strongly during liver fibrogenesis, reaching highest levels in cirrhotic tissue 8 wk after common bile-duct ligation and after 12 wk of peroral thioacetamide administration, respectively. Specific proteoglycan transcripts were almost absent in hepatocytes from normal and regenerating liver, and only trace amounts were observed in freshly isolated and cultured Kupffer cells. Fat-storing cells clearly expressed both biglycan and decorin transcripts. The steady-state levels of their messenger RNAs increased threefold (biglycan) and fourfold (decorin) during primary culture. Myofibroblastlike cells (transformed fat-storing cells after the second passage) contained dramatically reduced levels of decorin messenger RNA and also lower levels of biglycan messenger RNA compared with primary cultures. These changes of core protein messenger RNA expression were not reflected by the synthesis rates of medium proteoglycans labeled with 35S as Na2SO4, in particular that of medium chondroitin sulfate. Transiently acidified (but not native) conditioned media from Kupffer cells and myofibroblastlike cells and transforming growth factor-beta 1 enhanced the relative abundances of biglycan and decorin messenger RNAs up to five times in primary-cultured fat-storing cells. Biglycan and decorin in myofibroblastlike cells did not respond to these stimuli.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed2005

Electrochemical studies on zirconium and its biocompatible alloys Ti-50Zr at.% and Zr-2.5Nb wt.% in simulated physiologic media.

Different electrochemical studies were carried out for Zr and its biocompatible alloys Ti-50Zr at.% and Zr-2.5Nb wt.% in solutions simulating physiologic media, Ringer and PBS (phosphate buffered saline) solutions. The results from rest-potential measurements showed that the three materials are spontaneously passivated in both solutions and that the Ti-50Zr alloy has the greatest tendency for spontaneous oxide formation. Some corrosion parameters (such as the pitting and repassivation potentials) were obtained via cyclic voltammetry in both solutions, revealing that the Ti-50Zr has the best corrosion protection while Zr has the worst. On the other hand, the pre-anodization (up to 8 V vs. SCE) of the alloys in a 0.15 mol/L Na2SO4 solution led to a significant improvement in their protection against pitting corrosion when exposed to the Ringer solution. Elemental analyses by EDX showed that during pitting corrosion, there is no preferential corrosion of any of the alloying elements (Zr, Ti, Nb).

Alloys↗

PubMed1980

Cell-surface glycosaminoglycans: turnover in cultured human embryo fibroblasts (IMR-90).

As constituents of both extracellular matrix and the cell surface, glycosaminoglycans are in a strategic position to influence several basic cell features. The localization and turnover of glycosaminoglycans was investigated in cultured normal human embryo fibroblasts of lung origin (IMR-90). Attention was directed particularly toward that compartment of the culture which could be released by gentle proteolysis (trypsin, 0.1 mg/ml, 15 min) and is considered to represent the cell surface. In the presence of NA2SO4, sulfated glycosaminoglycans (S-GAGs) of the cell surface were labeled rapidly, but within 30 min some 35S-GAG appeared in the extracellular medium. The intracellular pool of S-GAGs labeled during a 10-min period was lost during the first hr of chase with a half-life of 18 min, compared with 16 hr for S-GAGs labeled over a 48-hr period. Pulse-labeled S-GAGs of the surface turned over with an initial half-life of 60 min, compared with 7 hr for surface material labeled over a 48-hr period. These rapid movements of the early chase period were followed by similar movement at a much slower rate. The results are consistent with a model in which most of the S-GAGs synthesized in the cell move rapidly to the surface. The surface GAGs are then released immediately to the medium or accumulate at the membrane to be shed more slowly at a later time or to be degraded. The S-GAG which left the cell layer most rapidly during chase was dermatan sulfate, while heparan sulfate made up an increasing percentage of the cell layer as chase progressed. These cultures produce a fibrillar matrix of fibronectin, but the kinetics of this study suggest that the S-GAGs of the surface are membrane-bound, and an extracellular glycosaminoglycan matrix does not form.

Cell Line↗

PubMed1980

Effect of changes in the ionic environment of reticulocytes on the uptake of transferrin-bound iron.

Rabbit reticulocytes were incubated with rabbit transferrin labelled with 59Fe and 125I in media in which the NaCl was replaced by other electrolytes or sucrose. Iron and transferrin uptake by the cells was affected by changes in the pH, ionic strength, ionic composition, and the osmolarity of the medium. Uptake was maximal at pH 7.4. A reduction in ionic strength produced by replacing NaCl with sucrose inhibited the uptake in a concentration-dependant manner, greatest inhibition occurring at lowest salt concentration. Similar results were obtained when KCl, LiCl, RbCl, Na2SO4, or K2SO4 were used instead of NaCl. Low ionic strength was found to inhibit the endocytotic uptake of transferrin labelled with colloidal gold, but had only a small effect on transferrin binding to cell membrane receptors. It was concluded that low ionic strength inhibits iron uptake primarily by blocking the endocytosis of transferrin. Three salts, NH4Cl, CaCl2, and MgCl2, produced different results from the above. NH4Cl inhibited iron uptake at all concentrations used. This action was due to an effect on the release of iron from transferrin, which appeared to be taken up by the cells in a normal manner. When the ionic strength of the sucrose medium was increased by adding low concentrations of CaCl2, iron uptake was greater than with equivalent concentrations of NaCl. However, with CaCl2 concentrations above 10 mM, iron uptake was inhibited, due to inhibition of transferrin uptake, possibly by blocking endocytosis. By contrast, MgCl2 stimulated iron uptake at all concentrations used. The results are discussed in terms of the possible effects of ionic strength, pH, and ionic composition of the extracellular fluid on the three main steps involved in iron uptake by immature erythroid cells: transferrin-receptor interaction, endocytosis, and iron release from transferrin.

Ammonium Chloride↗