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PubMed1991

Increased phagocytic activity of polymorphonuclear leukocytes of chronic granulomatous disease as determined with flow cytometric assay.

Using flow cytometry, we compared the phagocytic activity of polymorphonuclear leukocytes (PMNs) from healthy donors with that of PMNs from 10 patients with chronic granulomatous disease (CGD), eight carriers of X-linked CGD, and one patient with myeloperoxidase deficiency. Ingestion of fluorescent bacteria by CGD and myeloperoxidase-deficient PMNs was significantly increased, that is, about 1.5 times that of normal controls. In CGD carriers, two PMN populations were found: one population consisted of PMNs with enhanced phagocytosis, and the other consisted of PMNs with normal phagocytic activity. With a two-dimensional analysis, we also demonstrated in CGD carriers that phagocytosis of the PMNs that failed to generate hydrogen peroxide was significantly elevated, as was phagocytosis of PMNs in patients with CGD, while on the other hand, the PMNs that normally produced hydrogen peroxide exhibited a normal phagocytic activity. When sodium azide, an inhibitor of myeloperoxidase and catalase, was added to control and carrier PMNs, phagocytic activity was significantly increased, p less than 0.01 in both, but not to the level seen with CGD PMNs. Phagocytosis of CGD and myeloperoxidase-deficient PMNs, however, remained unchanged by the azide treatment. On the basis of above findings, we speculate that phagocytosis of CGD PMNs is increased because the H2O2-myeloperoxidase-halide system, which may modulate phagocytic activity of PMNs, fails to operate.

Adolescent↗

PubMed1989

Intracellular distribution and pharmacokinetics of daunorubicin in anthracycline-sensitive and -resistant HL-60 cells.

Anthracycline-sensitive (HL-60) and -resistant (HL-60/AR) cells, which do not overexpress the P-glycoprotein, each transport and distribute daunorubicin (DNR) into distinct intracellular locations, as visualized by digitized video fluorescence microscopy. At pH 7.4, the fluorescence of DNR in HL-60 cells appears distributed diffusely in both the nucleus and cytoplasm. In contrast, HL-60/AR cells show much less fluorescence in the nucleus and cytoplasm; most of the fluorescence localizes first to the Golgi apparatus and is then gradually shifted to the lysosomes and/or mitochondria. In pharmacokinetic studies, HL-60/AR cells exposed to different extracellular concentrations of [14C]DNR consistently accumulated less radioactive drug than the parent HL-60 cells. Incubation of HL-60/AR cells with sodium azide and deoxyglucose blocked the efflux of [14C]DNR and also prevented the shift of DNR fluorescence from the Golgi apparatus to the lysosomes/mitochondria. The efflux and the intracellular shift of DNR could also be inhibited by lowering the temperature to 18 degrees C, which stops endosomal membrane fusion. When DNR was allowed to accumulate in HL-60 or HL-60/AR cells at pH 5 there was an increase in the proportion of drug fluorescence in the membranes of both HL-60 and HL-60/AR cells; a decrease in the amount of drug retained by HL-60, but not by HL-60/AR cells; and a decrease in the cytostatic effects of DNR on both HL-60 and HL-60/AR cells. These data suggest that DNR resistance is associated with a failure of DNR to pass through membranes and to bind to cytoplasmic and nuclear structures. Instead, most of the drug is taken up by the Golgi apparatus from which it is then shifted to the lysosomes or to mitochondria, or out of the cell.

Antibiotics, Antineoplastic↗

PubMed1985

Transbilayer movement of a fluorescent phosphatidylethanolamine analogue across the plasma membranes of cultured mammalian cells.

The internalization of a fluorescent analogue of phosphatidylethanolamine following its insertion into the plasma membrane of cultured Chinese hamster fibroblasts was examined. When liposomes composed of 50 mol % 1-acyl-2-(N-4-nitrobenzo-2-oxa-1,3-diazole)-aminocaproyl phosphatidylethanolamine (C6-NBD-PE) and dioleoylphosphatidylcholine were incubated with monolayer cell cultures at 2 degrees C, a spontaneous transfer of the fluorescent lipid from liposomes to cells occurred. As long as the cells were kept at 2 degrees C, the fluorescent lipid remained at the plasma membrane. However, if, after removing the fluorescent liposomes, the cultures were warmed to 37 degrees C, the C6-NBD-PE was internalized and resided in the nuclear envelope, mitochondria, and Golgi apparatus in addition to the plasma membrane. Delivery of the fluorescent lipid to the Golgi apparatus could be blocked by the addition of 2-deoxyglucose plus sodium azide to the incubation medium. Evidence is presented suggesting that while delivery of the fluorescent lipid to the Golgi apparatus was mainly dependent on endocytosis, delivery to the nuclear envelope and mitochondria occurred by rapid transbilayer movement of the lipid across the plasma membrane followed by translocation of lipid monomers. Rapid transbilayer movement of C6-NBD-PE across the plasma membrane was found to be a temperature-dependent process that was blocked below 7 degrees C.

4-Chloro-7-nitrobenzofurazan↗

PubMed1987

Initial adhesion of murine fibroblasts to collagen and fibronectin occurs by two mechanisms.

The adhesion of Balb/c 3T12 cells to fibronectin (FN) and to denatured (DC) or native (NC) collagen is differentially sensitive to divalent cations and to sodium azide. Short-time adhesion (10 min) to FN requires either Mg2+ or Mn2+, whereas only Mn2+ stimulates attachment to DC and NC. Azide treatment only slightly affects adhesion of cells to FN, but strongly inhibits cell attachment to DC and NC. Attachment to any of these substrata is unaffected by monensin and by treatment of the cells with an intracellular fraction, making unlikely the possibility that molecules released by secretion or cell lysis participate in the adhesive process. Soluble collagen inhibits the adhesion of cells to DC and NC, but does not affect adhesion to FN. Finally, rabbit antiserum against collagen binding proteins inhibits cell attachment to NC and DC; the cells, however, attach normally to FN in presence of this antiserum. Taken together, our results support the view that 3T12 cells attach directly to native or denatured collagens and that FN is not required for this process.

Animals↗

PubMed1988

Organic cation uptake by a cultured renal epithelium.

Several organic cations are actively transported by proximal renal tubules by mediated processes across both the apical and basolateral cell membranes. In order to evaluate this transport system in a cultured renal epithelium, uptake of 3H-tetraethylammonium (TEA) across the apical membrane was measured in LLCPK1 cells, a cell line with several characteristics of proximal tubules. 3H-TEA progressively entered these cells and reached a near-steady state by 30 min. Three-minute uptake was saturable with an apparent Vmax of 1,669 +/- 129 fmoles/micrograms DNA and apparent Km of 34.0 +/- 3.4 microM. 3H-TEA uptake was inhibited by an excess of nonradioactive TEA, other organic cations, sodium azide, and hypothermia. An alkaline external pH was associated with greater 3H-TEA uptake than an acid pH. However, efflux of 3H-TEA from cells was not appreciably affected by changes in external pH. Preincubation of cells in acid or alkaline media did not affect uptake. Alteration of cell pH by ammonium chloride addition or removal had little effect on 3H-TEA uptake. Finally, uptake of 3H-TEA was not accelerated by preloading cells with an excess of nonradioactive TEA. These results indicate that intact LLCPK1 cells possess a mechanism(s) in their apical membranes for the mediated transport of a prototypic organic cation. The mechanism(s) involved in this transport is uncertain. However, neither organic cation/proton nor organic cation/organic cation exchange appears to be the predominant process.

Animals↗

PubMed1986

Comparative uptake, retention and cytotoxicity of daunorubicin by human myeloid cells.

We studied the cellular uptake and retention of daunorubicin (D1) in two human leukemic cell lines (ML1 and K562) and myecloblasts from an untreated patient with acute myelogenous leukemia (AML). The rate of uptake and the steady-state level of D1 were not temperature dependent but increased markedly with increases in the pH of the medium. Also, saturation kinetics were not demonstrable using concentrations of D1 up to 111 microM. Together, these observation suggest a transport mechanism for D1 compatible with passive diffusion. Accumulation of D1 was increased only in cells from the AML patient with addition of sodium azide, whereas drug efflux was not increased significantly in the presence of glucose in MLI or K562 cells. Although the rate of uptake and steady-state levels of D1 were the same in these cells, metabolism and cytotoxicity of D1 differed. Our results indicate that ML1 cells can be used as a pharmacologic model for studying the metabolism and resistance of D1 in vivo.

Azides↗

PubMed1982

A new combined assay of phagocytosis and intracellular killing of Escherichia coli by polymorphonuclear leukocytes.

A new combined radiometric assay is described in which adherence, and phagocytosis and killing of Escherichia coli by human polymorphonuclear leucocytes (PMN) are simultaneously measured in the same sample. Pure monolayers of PMN in Petri dishes are allowed to ingest [14C]phenylalanine labelled E. coli and excess bacteria are removed by washing. A period of incubation allows intracellular killing to occur while polymyxin-B is added to half the dishes to kill extracellular bacteria. The remaining viable bacteria in all dishes are labelled with [3H]thymidine. The number of ingested bacteria and the percentage of intracellular organisms killed is determined from the 14C and 3H counts by a simple subtraction technique. By performing protein assays on representative monolayers, the number of PMN adhered in the monolayers and hence the mean bacterial uptake per PMN is estimated. The assay detected killing efficiencies reduced below the normal range, in monolayers treated with sodium azide, phenylbutazone, in polymorphonuclear leukocytes from patients with chronic granulomatous disease, and in immature neutrophils from the promyelocytic leukaemic cell line, HL60. The assay was adapted to measure phagocytosis and killing by cells in suspension.

Azides↗

PubMed1995

Induction of thermotolerance by chemical agents in Lactococcus lactis subsp. lactis IL1403.

Like in other organisms tested to date, adapted cells of Lactococcus lactis subsp. lactis IL1403 pretreated at 42 degrees C for 30 min develop a thermotolerant state, i.e. an increased ability to survive subsequent exposure to a lethal challenge temperature (52 degrees C for 15 or 30 min). In different cellular systems, chemicals as diverse as divalent metal salts, natural or synthetic compounds trigger the development of thermotolerance. Yet, in L. lactis subsp. lactis IL1403, among the 17 chemicals tested, only four induced this transient increased tolerance to heat: cadmium chloride, mercury chloride, sodium azide and beta-mercaptoethanol. Intriguingly, none of these four compounds induced the synthesis of three major heat shock proteins (DnaK, GroEL and hsp104-analogue), which are believed to be responsible for thermotolerance in most organisms. It is suggested that: (i) the lesions produced by these various 'proteotoxic' agents are fundamentally different from those produced by heat; (ii) heat shock protein synthesis and transient induced tolerance to heat are not tightly correlated phenomena in L. lactis subsp. lactis as they are in Escherichia coli and some other organisms.

Adaptation, Physiological↗

PubMed1986

Intracellular site of "Ca reversal": inhibition of uterine smooth muscle contraction in Ca-free medium by a minute amount of Ca ion released from mitochondria by drugs.

Sodium azide (NaN3) and dinitrophenol (DNP) at low concentrations caused "Ca reversal", i.e. inhibition of oxytocin-induced tonic contraction of estrogen-dominated rat uterine smooth muscle in Ca-free solution. This inhibition was not due to depletion of ATP by NaN3 or DNP. Higher concentrations of NaN3 and DNP caused additional contraction. NaN3 and DNP dose-dependently released Ca ion from mitochondria isolated from the estrogen-dominated rat uterine smooth muscle in vitro. Electron microscopic studies have shown that in estrogen-dominated rat uterine smooth muscle cells, cytoplasmic membranes proliferate, resulting in compartmentalization of the myofilament-sarcoplasmic system and its separation from the receptor-effector system in the surface folds of the plasma membranes, which also contain some mitochondria. It is proposed that low concentrations of NaN3 and DNP release a small amount of Ca ion from these outer mitochondria and this Ca ion acts on the intracellular "site of Ca reversal" to induce reversal, i.e. inhibition. Higher concentrations of NaN3 and DNP are proposed to release a large amount of Ca ion from the central mitochondria near myofilaments and so induce contraction. The "site of Ca reversal" was shown to be intracellular as our previous postulation.

Animals↗

PubMed1989

Reorganization and stabilization of acetylcholine receptor aggregates on rat myotubes.

Aggregation of acetylcholine receptors (AChRs) is an important early feature of the postsynaptic development of the vertebrae neuromuscular junction. At later stages of differentiation, aggregates are remodeled and stabilized. Aggregation of AChRs can be induced on rat myotubes in culture within 4 hr by treatment with embryonic pig brain extract (EBX). In this study, further sequential changes in the distribution of AChRs were followed by video-intensified fluorescence microscopy. These studies have revealed that groups of AChR aggregates that have formed after 4 hr in EBX are reorganized during the exposure to EBX for 20 additional hr to form a smaller number of larger, oval-shaped aggregates. We have named these two types of aggregates "4-hr aggregates" and "24-hr aggregates". This reorganization occurs by the expansion and merging of individual aggregates within a group, and by the incorporation of newly inserted AChRs. The 24-hr aggregates are an average of 15 times greater in area than 4-hr aggregates, and contain regions with an apparent AChR site density (fluorescence intensity) that is more than twice that of 4-hr aggregates. Electron microscopy of mapped 24-hr aggregates revealed that folded plasma membrane is associated with these regions, probably accounting for the elevated fluorescence. The 24-hr aggregates are more stable than 4-hr aggregates, as determined by their significantly slower disassembly after removal of EBX, elevation of temperature (38 degrees C), reduction of extracellular calcium levels (0.1 mM), or the addition of sodium azide (7 mM). This was determined by following disassembly both statistically (using fixed cultures) and by direct observations of living myotubes. These findings were confirmed by measuring the sequential changes in relative AChR site density over time in individual living myotubes. Thus, 24-hr aggregates form by the reorganization of 4-hr aggregates; exhibit a more regular, compact shape; and are more stable than 4-hr aggregates. These changes in AChR organization and aggregate stability resemble the changes occurring after the initial formation of junctional AChR aggregates during embryonic development, demonstrating additional similarities between this model system and the developing neuromuscular junction.

Animals↗

PubMed2001

Synthesis of cyclic sulfates by halocyclization.

[reaction: see text]. We report the synthesis of cyclic sulfates by halocyclization. The resulting cyclic sulfate products can be opened selectively with sodium azide to transform them into highly functionalized compounds that contain azide, alcohol, and halide groups.

Cyclization↗

PubMed1997

Rapid Ca2+ influx induced by the action of dibutylhydroquinone and glucagon in the perfused rat liver.

Glucagon induces a slight Ca2+ efflux when administered to the perfused rat liver. However, the hormone promotes rapid and significant Ca2+ influx after the prior administration of 2, 5-di(t-butyl)-1,4-hydroquinone (BHQ), an agent that promotes Ca2+ release from the endoplasmic reticulum (ER). The concentrations of glucagon that promote Ca2+ influx are similar to those that promote glycogenolysis and gluconeogenesis in isolated hepatocytes. The permeable analogue of cAMP, but not that of cGMP, is able to duplicate the Ca2+-mobilizing effects of glucagon. The influx of Ca2+ into liver is blocked by Ni2+. Administration of sodium azide, an inhibitor of mitochondrial electron transport, also blocks the BHQ plus glucagon-induced Ca2+ influx and this is reversed when azide administration is terminated. The actions of azide are evident within 60 s after administration or withdrawal, and also occur when either oligomycin or fructose is co-administered; this provides evidence for an effect of azide independent of cellular ATP depletion. Measurement of total calcium in mitochondria that were isolated rapidly from perfused livers after the combined administration of glucagon and BHQ confirmed that large quantities of extracellular Ca2+ had entered these organelles. These experiments provide evidence that in the perfused rat liver the artificial emptying of the ER Ca2+ pool allows glucagon to promote rapid and sustained Ca2+ influx that seems to terminate in mitochondria.

Animals↗

PubMed1997

Endocytotic uptake of small unilamellar liposomes by human trophoblast cells in culture.

We evaluated the mechanism of uptake of carboxyfluorescein-containing small unilamellar liposomes of different surface charge by trophoblast cells in culture. Carboxyfluorescein-encapsulated neutral liposomes were prepared by using equimolar concentrations of lecithin and cholesterol. Anionic and cationic liposomes were prepared by adding dicetylphosphate and stearylamine. Trophoblast cells from human term placenta were cultured and incubated on the first day at 37 degrees C with liposome-encapsulated carboxyfluorescein or 500 nM of free carboxyfluorescein. The mechanism of uptake was determined by pre-treating the cells with metabolic inhibitors: 2 mM of sodium azide and 25 mM of deoxyglucose for 30 min. The uptake of liposomes was also evaluated both qualitatively under fluorescent microscope and quantitatively by measuring carboxyfluorescein fluorometrically. The uptake of free carboxyfluorescein and cationic liposomes was comparable. The anionic liposomes were taken up by the trophoblast cells more avidly than the neutral (13.2 +/- 1.6 versus 9.5 +/- 1.4%; P <0.01), cationic (2.9 +/- 0.4%; P <0.001) and the free carboxyfluorescein (2.1 +/- 0.9%; P <0.01). When cells were pre-treated with metabolic inhibitors, the uptake of anionic (5.9 +/- 1.8%; P <0.001) and neutral liposomes (4.0 +/- 0.8%; P <0.01) was significantly reduced, whereas uptake of cationic and free carboxyfluorescein remained unaltered. This study indicates that small unilamellar liposomes are internalized by the trophoblast cells in culture by an energy-dependent pathway; most probably by endocytosis. The neutral and anionic liposomes are internalized more avidly than cationic liposomes.

Antimetabolites↗

PubMed1986

The mechanisms by which haemoglobin inhibits the relaxation of rabbit aorta induced by nitrovasodilators, nitric oxide, or bovine retractor penis inhibitory factor.

The mechanisms by which haemoglobin and methaemoglobin inhibit the vasodilator actions of glyceryl trinitrate, sodium azide, nitric oxide, and the bovine retractor penis inhibitory factor (IF) were studied on rabbit endothelium-denuded aortic rings. Methaemoglobin was less effective than haemoglobin against each vasodilator, it was more effective at inhibiting the relaxation to azide than that to glyceryl trinitrate. Glyceryl trinitrate was neither bound nor inactivated when passed through columns of haemoglobin-agarose or methaemoglobin-agarose. Azide was reversibly bound but less by haemoglobin-agarose than by methaemoglobin-agarose. Inhibition of the vasodilator actions of glyceryl trinitrate is not attributable therefore to a direct interaction with the haemoproteins, although a small part of the inhibition of azide-induced relaxation by methaemoglobin is likely to be due to a direct interaction. Columns of haemoglobin-agarose were more effective than columns of methaemoglobin-agarose in removing nitric oxide from solution. The greater ability of haemoglobin, compared to methaemoglobin, to inhibit vasodilatation induced by nitrovasodilators may therefore reflect the greater ability of haemoglobin to bind nitric oxide which is the active principle of the nitrovasodilators. Neither the acid-activated nor the inactive forms of IF were bound or inactivated when passed through columns of methaemoglobin-agarose. Neither form of IF was retained on passage through columns of haemoglobin-agarose, but the resulting activity in the eluates was less than control, was unstable and, unlike the original activity, decayed rapidly on ice. The greater ability of haemoglobin, compared to methaemoglobin, to inhibit vasodilatation induced by IF might therefore reflect the greater ability of haemoglobin to interact with this vasodilator and inactivate it.

Animals↗

PubMed1982

Manganese binding and oxidation by spores of a marine bacillus.

Mature, dormant spores of a marine bacillus, SG-1, bound and oxidized (precipitated) manganese on their surfaces. The binding and oxidation occurred under dormant conditions, with mature spores suspended in natural seawater. These heat-stable spores were formed in the absence of added manganese in the growth medium. The rate and amount of manganese bound by SG-1 spores was a function of spore concentration. Temperatures greater than 45 degrees C, pH values below 6.5, or the addition of EDTA or the metabolic inhibitors sodium azide, potassium cyanide, and mercuric chloride inhibited manganese binding and oxidation. However, SG-1 spores bound and oxidized manganese after treatment with glutaraldehyde, formaldehyde, ethylene oxide gas, or UV light, all of which killed the spores. Manganese oxidation never occurred in the absence of manganese binding to spores. The data suggest that Mn2+ was complexed by a spore component, perhaps an exosporium or a spore coat protein: once bound, the manganese was rapidly oxidized.

Azides↗

PubMed1983

Somatomedin synthesis by a subclone of Buffalo rat liver cells: characterization and evidence for immediate secretion of de novo synthesized hormone.

Previous studies have reported that cultured Buffalo rat liver (BRL-3A) cells synthesize and release a somatomedin called multiplication-stimulating activity, a major component of which is rat insulin-like growth factor-II (rIGF-II). We have isolated a subclone of hepatocytes (BRL-3SC) from these cells, which release rIGF-II into serum-free medium at a similar but considerably more uniform rate than BRL-3A cells, and have described their morphology and defined some of the conditions regulating the rate of synthesis and secretion of rIGF-II. Time-course experiments indicate that after a 2-h lag, rIGF-II is released at a nearly constant rate of 70 microU insulin-like activity/ml . 24 h for 5 days. These cells demonstrate considerable resistance to variations in environmental pH, with extremes of pH 6.8-8.0 in the initial culture medium causing a negligible effect on rIGF-II release. We found no evidence for the existence of an appreciable amount of intracellular rIGF-II, consistent with the lack of secretion granules in these cells. Moreover, at concentrations not causing irreversible cell damage, inhibitors of protein synthesis, cycloheximide and actinomycin D, produced 87% and 76% reductions, respectively, in rIGF-II release in 24 h, and inhibitors of oxidative phosphorylation, dinitrophenol and sodium azide, reduced rIGF-II release by 72% and 78%, respectively. We conclude from these studies that BRL-3A cells, and particularly those of the subclone BRL-3SC herein described, may provide an excellent model for investigations of somatomedin synthesis and release and that such studies are facilitated by the fact that rIGF-II released into serum-free medium appears to be the immediate product of de novo peptide synthesis.

Animals↗

PubMed1986

The properties of arginine transport in vacuolar membrane vesicles of Neurospora crassa.

We have measured the uptake of arginine into vacuolar membrane vesicles from Neurospora crassa. Arginine transport was found to be dependent on ATP hydrolysis, Mg2+, time, and vesicle protein with transported arginine remaining unmodified after entry into the vesicles. The Mg2+ concentration required for optimal arginine transport varied with the ATP concentration so that maximal transport occurred when the MgATP2- concentration was at a maximum and the concentrations of free ATP and Mg2+ were at a minimum. Arginine transport exhibited Michaelis-Menten kinetics when the arginine concentration was varied (Km = 0.4 mM). In contrast, arginine transport did not follow Michaelis-Menten kinetics when the MgATP2-concentration was varied (S0.5 = 0.12 mM). There was no inhibition of arginine transport when glutamine, ornithine, or lysine were included in the assay mixture. In contrast, arginine transport was inhibited 43% when D-arginine was present at a concentration 16-fold higher than that of L-arginine. Measurements of the internal vesicle volume established that arginine is concentrated 14-fold relative to the external concentration. Arginine transport was inhibited by dicyclohexylcarbodiimide, carbonyl cyanide m-chlorophenyl-hydrazone, and potassium nitrate (an inhibitor of vacuolar ATPase activity). Inhibitors of the plasma membrane or mitochondrial ATPase such as sodium vanadate or sodium azide did not affect arginine transport activity. In addition, arginine transport had a nucleoside triphosphate specificity similar to that of the vacuolar ATPase. These results suggest that arginine transport is dependent on vacuolar ATPase activity and an intact proton channel and proton gradient.

Adenosine Triphosphate↗

PubMed1996

Use of four-colour flow cytometry to evaluate conjugate formation between human peripheral blood mononuclear cells and tumour target cells.

A four-colour flow cytometry technique is described for the determination of the number and phenotype of conjugate-forming mononuclear effector cells from human blood. The discriminatory power of previously described techniques was improved by labelling the effector cells with antibodies that simultaneously identified natural killer (NK), T, and myeloid cells and by labelling the tumour target cells with fluorescein octadecyl ester (FOE), so that cell conjugates could be differentiated from nonbinding effector cells more effectively than by the use of light scatter. The simultaneous characterisation of the three classes of conjugate-forming cells within a heterogeneous human peripheral blood mononuclear cell (PBMC) population made it possible to investigate conjugate formation by each subpopulation without purification, or semipurification (e.g., by monocyte removal), of the subpopulations. The binding of PBMCs to K562 and RPMI 1788 targets was examined. Binding for all three PBMC subpopulations was optimal at 37 degrees C and was negligible at 0 degree C (except for some T cell binding to RPMI 1788 cells). At 37 degrees C, maximum binding was essentially achieved by 10 min. Sodium azide inhibited the majority of the conjugation by NK and T cells, and that inhibition could be removed by washing the cells prior to conjugation, whereas azide had a negligible effect on the binding by monocytes. It appears that effective conjugation by human peripheral blood NK and T lymphocytes requires the operation of an energy-dependent process, differentiating it from conjugation by monocytes.

Azides↗