Biomedical subjects

Y Aramaki

Publications and source records attributed to Y Aramaki.

At least 37 records · Page 2Linked to original sources

PubMed1999

Macrosialin may not be involved with the regulation of nitric oxide production from mouse peritoneal macrophages stimulated with LPS.

We reported previously that nitric oxide (NO) production from mouse peritoneal macrophages stimulated with LPS was inhibited by negatively charged liposomes composed of phosphatidylserine (PS-liposomes) or oxidized LDL (Ox-LDL) which have an affinity for scavenger receptors (SRs). In this study, to clarify whether macrosialin, an SR, participates in the inhibitory effects of PS-liposomes or Ox-LDL on NO production, the effects of anti-macrosialin monoclonal antibody (FA/11) on inhibition of NO production by PS-liposomes or Ox-LDL were investigated. FA/11 itself showed no effect on NO production induced by LPS. Binding of FA/11 to macrophages was inhibited by the addition of PS-liposomes or Ox-LDL, indicating that PS-liposomes or Ox-LDL have an affinity for macrosialin. However, the inhibitory effects of these ligands on NO production were not reduced in the presence of FA/11. These findings suggest that macrosialin does not contribute to the inhibitory effects of PS-liposomes or Ox-LDL on NO production from mouse peritoneal macrophages stimulated with LPS.

Animals↗

PubMed1998

Contribution of CR3 to nitric oxide production from macrophages stimulated with high-dose of LPS.

The contribution of the complement receptor type 3 (CR3) to nitric oxide (NO) production from macrophages stimulated by LPS was investigated. When thioglycollate-elicited mouse peritoneal macrophages were stimulated with a high dose of LPS (10 micrograms/ml) in both the presence and absence of fetal calf serum, a source of LPS binding protein (LBP) necessary for the binding of LPS to CD14, NO production was observed. These findings suggest that CD14-dependent and CD14-independent signaling pathways for NO production are present in macrophages. Because binding and phagocytosis of bacteria by macrophages through the CR3 has been previously reported, we investigated whether the CR3 acts in CD14-independent signaling pathway for NO production. By flow cytometric analysis, the binding of FITC-labeled anti-CR3 monoclonal antibody (anti-CR3 mAb) to macrophages was inhibited by LPS. Anti-CR3 mAb induced iNOS protein and produced NO in a dose dependent manner. Further, NO production induced by anti-CR3 mAb was also inhibited by zymocel, beta-glucan with a high affinity to CR3. These results suggest that the CR3 molecule acts in a CD14-independent signaling pathway, and contributes to NO production by macrophages stimulated with high doses of LPS.

Animals↗

PubMed1998

Specific inhibition of interleukin-10 production in murine macrophage-like cells by phosphorothioate antisense oligonucleotides.

The effects of phosphorothioate antisense oligonucleotides (AS-S-oligos) directed against murine interleukin-10 (IL-10) mRNA on IL-10 production in RAW264.7 cells, a murine macrophage-like cell line, when stimulated by lipopolysaccharide (LPS) were examined. Of the six AS-S-oligos used, AS-S-oligos directed against the 3'-untranslated region (3'-UTR) of IL-10 mRNA (AS6-S-oligo) showed the strongest inhibitory effect on IL-10 production, and this inhibition was dose and time dependent. Reverse transcription-polymerase chain reaction (RT-PCR) revealed that the antisense effect originated from a specific reduction of target IL-10 mRNA by hybridization with AS6-S-oligo. In addition, AS6-S-oligo did not affect tumor necrosis factor-alpha (TNF-alpha) production in cells stimulated by LPS, and S-oligos with control sequences did not affect IL-10 production. These findings suggested that AS6-S-oligo most powerfully inhibited IL-10 production in macrophages by an antisense mechanism.

3' Untranslated Regions↗

PubMed1998

Prolonged release of drug from O/w emulsion and residence in rat nasal cavity.

The present study evaluated the usefulness of an o/w emulsion for slowing the release of chlorpheniramine maleate (CM) and prolonging drug residence in the nasal cavity. O/w emulsion formulations of medium chain triglycerides (MCT) were prepared, and their physicochemical properties and drug release kinetics were evaluated using the in vitro dialysis tube method. Drug disappearance from the rat nasal cavity was determined in in situ nasal experiments. CM partitioned in oil droplets by pH, as predicted by pH partition theory. With higher MCT concentration and pH, slower release of CM was observed. CM disappearance (kapp) from the rat nasal cavity was influenced by the amount of drug partitioned in the oil droplets with both the perfusion and deposit methods, and the kapp of CM decreased with increase in MCT concentration and pH. Moreover, with the deposit method, CM remaining in the nasal cavity exhibited a biphasic profile of disappearance, which complied with a saturated process. Because a very small portion of MCT might be adsorbed and formed a pseudooily layer on the mucous membranes, prolongation of CM residence on the mucous membrane was attained. These findings suggest that emulsion containing 30% MCT at pH 8 may be useful for inclusion in controlled-release formulations of CM for intranasal drug delivery in the treatment of allergy.

Administration, Intranasal↗

PubMed1997

Scavenger receptors may regulate nitric oxide production from macrophages stimulated by LPS.

The effects of scavenger receptor (SR) ligands on nitric oxide (NO) production were investigated using mouse peritoneal macrophages stimulated by LPS. Pretreatment of macrophages with oxidized LDL, heparin, maleylated BSA, or liposomes composed of phosphatidylserine (PS-liposomes) inhibited NO production, but native LDL, acetyl LDL dextran sulfate, did not. Immunoblotting analysis suggests that the inhibitory effects could be a result of the inhibition of inducible NO synthase (iNOS) induction, but not enzyme activity. Further, tyrosine phosphorylation of a 41 kDa protein was also inhibited by OxLDL, heparin, maleylated BSA, and PS-liposomes. Chloroquine did not affect the extent of inhibition of NO production induced by these ligands, suggesting that the binding of these ligands to SR generates a signal(s) which is involved in the inhibition of NO production from macrophages stimulated by LPS. SR, which has an affinity to these ligands, may strictly regulate NO production from macrophages, and this inhibitory effect may be due to the inhibition of LPS-induced tyrosine phosphorylation of 41 kDa protein.

Animals↗

PubMed1997

Negatively charged liposomes inhibit tyrosine phosphorylation of 41-kDa protein in murine macrophages stimulated with LPS.

Examination was made of the mechanism of the inhibitory effects of liposomes on NO production using thioglycollate-induced mouse peritoneal macrophages stimulated by LPS. NO production was inhibited dose dependently by negatively charged liposomes containing phosphatidylserine (PS-liposomes) but not neutral liposomes composed with phosphatidylcholine. To clarify this mechanism, the effect of liposomes on protein tyrosine phosphorylation was investigated by Western blot analysis, and tyrosine phosphorylation of protein with 41 kDa was inhibited by PS-liposomes dose dependently. NO production and tyrosine phosphorylation of p41 were also inhibited by herbimycin A, a tyrosine kinase inhibitor. TNF-alpha production was also inhibited by PS-liposomes. The inhibition of tyrosine phosphorylation of protein with 41 kDa by PS-liposomes may thus lead to the suppression on NO and TNF-alpha productions from macrophages stimulated by LPS.

Animals↗

PubMed1997

Effects of oligodeoxynucleotides on the physicochemical characteristics and cellular uptake of liposomes.

We studied the effects of a phosphodiester oligodeoxynucleotide (ODN), which is antisense to the site in the neighborhood of the AUG initiation codon of the mouse tumor necrosis factor alpha gene (TNF-alpha), on the physicochemical characteristics and the cellular association of three types of liposomes with different surface charges. The physicochemical characteristics of the liposomes changed after adding ODN. When the ODN/lipid molar ratio was approximately 0.15 in cationic (TMAG) liposomes [consisting of N-(alpha-trimethylammonioacetyl)didodecyl-D-glutamate chloride (TMAG), dilauroylphosphatidylcholine (DLPC), and dioleolylphosphatidylethanolamine (DOPE) in a 1:2:2 ratio], but not in neutral and negatively charged liposomes, then the liposomes aggregated and fused. At higher molar ratios, these changes in TMA liposomes were not evident. In addition, ODN inverted the zeta-potential of TMAG liposomes from positive to negative at an ODN/lipid molar ratio of approximately 0.15. Therefore, the aggregation and fusion induced by ODN could be explained by a lower surface charge repulsion between TMAG liposomes. On the other hand, the association of ODN with RAW264.7 cells, a mouse macrophage-like cell line, was very slight. The cellular association of ODN was significantly enhanced compared with neutral and negatively charged liposomes by encapsulation in TMAG liposomes. The ODN added to liposome suspensions did not affect the rate and extent of TMAG liposome cellular association, even at an ODN/lipid molar ratio of approximately 0.15. These results indicate that the lipid composition and ODN/lipid molar ratio are critical for the physicochemical characteristics of cationic liposomes. However, the changes had less influence on the cellular uptake properties of cationic liposomes.

Animals↗

PubMed1997

Contribution of trypsin-sensitive proteins to binding of cationic liposomes to the mouse macrophage-like cell line RAW264.7.

We studied the binding of cationic liposomes, including didodecyl N-(alpha-(trimethylammonio)acetyl)-D-glutamate chloride (TMAG), to a mouse macrophage-like cell line RAW264.7 to clarify which molecules contribute to the binding of TMAG liposomes to the cell surface. Several types of TMAG liposomes encapsulating [3H]inulin, intra-aqueous markers of liposomes, were prepared and their binding characteristics were compared with those of neutral and negatively charged liposomes. The binding of TMAG liposomes to cells was superior to those of neutral and negatively charged liposomes and increased with increasing TMAG content. Scatchard plots for the binding of TMAG liposomes to the cells were approximately linear, indicating a single class of binding sites. Pretreatment of the cell surface with heparinase, heparitiase, chondroitinase ABC, or neuraminidase did not reduce the binding of TMAG liposomes. These results suggested that neuraminic acid and glycosaminoglycan on the cell surface have little contribution to TMAG liposome binding. Pretreatment of the cells with trypsin reduced the binding of TMAG liposomes in a concentration-dependent manner but did not detach the cells from the culture plates. In addition, alpha-chymotrypsin pretreatment had no effect even up to 5 micrograms/mL. Post-treatment with trypsin enhanced the release of TMAG liposomes from the cell surface in a concentration-dependent manner. These results demonstrated that TMAG liposomes bind to trypsin-sensitive proteins on the cell surface.

Animals↗

PubMed1997

Specific inhibition of nitric oxide production in macrophages by phosphorothioate antisense oligonucleotides.

The effects of antisense oligonucleotides (ODNs) on nitric oxide (NO) production induced by lipopolysaccharide (LPS) were investigated using thioglycollate-induced mouse peritoneal macrophages. Antisense phosphorothioate ODNs (S-oligo) corresponding to a sequence in the neighborhood of the AUG initiation codon of a mouse inducible nitric oxide synthase (iNOS) mRNA, which has a G-quartet motif in its antisense sequence, inhibited NO induction in a dose-dependent manner. Antisense phosphodiester ODNs (D-oligo), 5'- and 3'-terminal phosphorothioate-modified antisense ODNs and control scramble and missense S-oligos had no such effect. In addition, control nonsense and two mismatched S-oligos, which include G-quartet motif in their sequences, inhibited NO induction to approximately 50% of those in the control. Antisense S-oligo showed the inhibitory effect on NO production by exposure of macrophages to various concentrations of LPS. Western blot analysis using anti-mouse inducible nitric oxide synthase (iNOS) antibody revealed that antisense S-oligo specifically removed an immunoreactive band at 130 kDa. In addition, the results of reverse transcription-polymerase chain reaction (RT-PCR) revealed that the antisense effect originated from a specific reduction of the targeted iNOS mRNA by hybridization with the antisense S-oligo. Furthermore, no ODNs affected beta-actin mRNA and tumor necrosis factor alpha (TNF-alpha) expression in macrophages stimulated by LPS. These findings demonstrated that antisense S-oligo inhibited NO production derived from iNOS expression in macrophages by an antisense mechanism, including the aptameric effect partially mediated by the G-quartet motif.

Animals↗

PubMed1996

Efficient gene transfer to EGF receptor overexpressing cancer cells by means of EGF-labeled cationic liposomes.

Epidermal growth factor (EGF)-labeled cationic liposomes (EGF-liposomes) were prepared for efficient gene transfer vector to EGF receptor expressing cells. Transfection activity of EGF-liposomes associating plasmid PGV-C which encodes luciferase showed a 2-fold increase in EGF receptor expressing cells, HEC-1-A, compared to that of EGF-non-labeled liposomes (N-liposomes). In EGF receptor deficient HRA cells, however, both EGF- and N-liposomes exhibited low transfection efficiency and no difference was observed between them. Furthermore, by the addition of anti EGF receptor antibody, transfection efficiency of EGF-liposomes was suppressed, suggesting EGF receptor-mediated endocytosis of EGF-liposomes. Transfection activity of EGF-liposomes was strongly dependent on the concentrations of fusogenic lipid, dioleoylphospha-tidylethanolamine in liposomes. By X-gal staining 6-8% of GCH-1(m) cells which also had EGF receptor expressed beta-galactosidase activity following the transfection by EGF-liposomes associating pSV-beta-galactosidase. These findings indicate that EGF-liposomes could be a preferable vector for EGF-receptor expressing cells.

1,2-Dipalmitoylphosphatidylcholine↗

PubMed1996

Inhibitory effects of negatively charged liposomes on nitric oxide production from macrophages stimulated by LPS.

The effects of liposomes on nitric oxide (NO) productions induced by lipopolysaccharide were investigated using thioglycollate-induced mouse peritoneal macrophages. Negatively charged liposomes composed of phosphatidic acid (PA-liposomes) and phosphatidylserine (PS-liposomes) showed inhibitory effect on NO production in a dose dependent manner, but not in liposomes composed of phosphatidylcholine (PC-liposomes). Pretreatment of macrophages with liposomes was required in order to observe the inhibitory effect on NO production. NO production induced by IFN-gamma was also inhibited by negatively charged liposomes. To clarify the mechanism of inhibitory effect of liposomes, immune blotting was performed using anti mouse inducible nitric oxide synthase (iNOS) antibody. An immunoreactive band at 130 kDa was observed in the extract of control and PC-liposome- treated macrophages, whereas a faint or no band was observed in PS- and PA-liposome-treated ones. These finding revealed that the inhibition of NO production by negatively charged liposomes could be a result in the inhibition of iNOS induction, but not enzyme activity.

Animals↗

PubMed1996

Effects of fusogenic and DNA-binding amphiphilic compounds on the receptor-mediated gene transfer into hepatic cells by asialofetuin-labeled liposomes.

Effects of fusogenic and DNA-binding amphiphilic compounds on the receptor-mediated gene transfer using asialofetuin-labeled liposomes (AF-liposomes) were examined with HepG2 cells and rat hepatocytes in primary culture. AF-liposomes were sufficiently taken up by both types of cells through the asialoglycoprotein receptor-mediated endocytosis. In HepG2 cells, bacterial beta-galactosidase (beta-Gal) gene expression was observed by transfection using AF-liposomes encapsulating plasmid pCMV beta DNA (AF-liposome-pCMV beta). By addition of dioleoylphosphatidylethanolamine (DOPE) to the liposomal lipid composition (AF-liposome(DOPE)-pCMV beta), the transfection efficiency was clearly increased. The effects of DOPE were more conspicuous in the presence of chloroquine in the medium throughout the transfection. When pCMV beta complexed with gramicidin S (pCMV beta (GrS)) was encapsulated (AF-liposome(DOPE)-pCMV beta (GrS) and was transfected to HepG2 cells, an significantly high beta-Gal activity in the cells was observed as compared with that in the cells transfected with AF-liposome(DOPE)-pCMV beta. No effects of GrS were found in the transfection using AF-non-labeled control liposomes. In primary culture of rat hepatocytes, no beta-Gal gene expression was observed even though AF-liposome(DOPE)-pCMV beta was introduced into the cells prepared from adult rats. However, following the transfection with AF-liposome(DOPE)-pCMV beta, the beta-Gal activity was expressed in the cells from immature rats cultured in the medium supplemented with epidermal growth factor and insulin, and the transfection efficiency was 2-fold higher than that transfected with pCMV beta encapsulated in AF-non-labeled control liposomes. By the complex formation of pCMV beta with GrS, the transfection efficiency of AF-liposome(DOPE)-pCMV beta (GrS) increased according to the increase of GrS in the complex. It was shown that AF-liposome(DOPE)-pCMV beta (GrS) did efficiently introduce and express beta-Gal gene in both HepG2 cells and primary hepatocytes in the receptor mediated manner.

Animals↗

PubMed1996

Liposomal induction of a heat-stable macrophage priming factor to induce nitric oxide in response to LPS.

PURPOSE: The effects of liposomes on nitric oxide (NO) production from mouse peritoneal macrophages following intraperitoneal injection of liposomes were investigated. METHODS: Mouse peritoneal macrophages were collected following intraperitoneal injection of liposomes and cultured with and without lipopolysaccharide (LPS). Peritoneal washing fluid was also collected from the mice injected with liposomes. NO production was evaluated by measuring the concentration of nitrite in the macrophage culture supernatant by Griess reagent. RESULTS: NO production stimulated by LPS was observed in peritoneal macrophages obtained from the liposome-treated mice, but liposomes did not active macrophages directly to induce NO in response to LPS. NO production was higher in the liposomes composed of phosphatidylcholine than that of negatively charged liposomes composed of phosphatidylserine. Peritoneal washing fluid obtained from mice injected with liposomes has a capacity to induce NO production in the macrophages from naive mice. This capacity was not diminished by heat-treatment at 100 degrees C for 5 min. CONCLUSIONS: Peritoneal macrophages were activated to produce NO in response to LPS following intraperitoneal injection of liposomes. They did not activate macrophages directly, and the induction of heat-stable macrophage priming factor, but not cytokines, is suggested.

Animals↗

PubMed1996

alpha 2-macroglobulin stimulation of protein tyrosine phosphorylation in macrophages via the mannose receptor for Fc gamma receptor-mediated phagocytosis activation.

Macrophage phagocytic activity has previously been shown to be increased by binding of modified alpha 2-macroglobulin (alpha 2M) with mannose residues at termini of sugar chains to mannose receptors on macrophages, with a subsequent increase in the number of Fc gamma receptors at the cell surface. In the present study, an examination was made of the association of protein tyrosine kinase with the increase in number of Fc gamma receptors following binding of modified alpha 2M to mannose receptors. The phagocytosis of IgG-opsonized sheep red blood cells through the action of the Fc gamma receptor by modified alpha 2M was inhibited by mannose and herbimycin A and slightly so by genistein. The mannose receptor would thus appear to be associated with tyrosine kinase activity. By Western blotting, tyrosine phosphorylated proteins with molecular weights of 32000, 34000, 36000, 65000, 85000 and 110000 appeared or increased upon treating macrophages with modified alpha 2M. The degree of tyrosine phosphorylated proteins was the same for control macrophages following incubation in the presence of mannose and herbimycin A. Genistein treatment affected only tyrosine phosphorylated proteins of 65000 and 110000. The binding of modified alpha 2M to mannose receptors was demonstrated by the inducement of tyrosine kinase activation that was sensitive to herbimycin A, followed by an increase in Fc gamma receptors and consequently greater phagocytosis.

Animals↗

PubMed1996

Free radicals from 1-palmitoyl-2-arachidonoylphosphatidylcholine liposomes in Fe2+/ascorbic acid solution.

The generation of free radicals during the lipid peroxidation of liposomes composed of 1-palmitoyl-2-arachidonoylphosphatidylcholine (PAPC-liposome) in Fe2+/ascorbic acid (AsA) solution was studied by the ESR spin trapping technique. A carbon-centered radical adduct was observed using alpha-(4-pyridyl-1-oxide)-N-tert-butyl-nitorone (4-POBN) and 5,5-dimethyl-1-pyrroline-N-oxide (DMPO), but no oxygen-centered radicals such as .OH, LO., and LOO. were observed. The lipid peroxidation evaluated as 2-thiobarbituric acid reactive substances was inhibited by the addition of 4-POBN. The intensity of this inhibitory effect was dependent on the time when 4-POBN was added to the mixture of PAPC-liposomes and Fe2+/AsA solution, and no inhibitory effect could be observed after 4 min. The signal intensity of the carbon-centered radical adduct was dependent on the lipid concentration of PAPC-liposomes. These results suggest that the alkyl radicals generated from PAPC-liposome peroxidation induced by Fe2+/AsA were trapped by DMPO or 4-POBN at an earlier stage of lipid peroxidation.

Ascorbic Acid↗

PubMed1995

Receptor-mediated transfer of pSV2CAT DNA to a human hepatoblastoma cell line HepG2 using asialofetuin-labeled cationic liposomes.

Asialofetuin-labeled liposomes (AF-lps) were developed as a vector for gene transfer to hepatocytes. Plasmid pSV2CAT DNA which encodes bacterial chloramphenicol acetyltransferase (CAT) was associated with (meaning, in this report, the sum of 'to be adsorbed on the surface of' and 'to be encapsulated into the internal phase of') AF-lps (AF-lps-pSV2CAT) prepared by a tandem combination of the detergent removal and freeze-thaw methods. Ninety-six percent of input pSV2CAT was associated with AF-lps containing N-(alpha-trimethylammonioacetyl)-didodecyl-D-glutamate chloride, and approx. two-thirds of the associated DNA was encapsulated into the internal phase. The uptake of AF-lps by the cultured human hepatoblastoma cell line HepG2, having asialoglycoprotein receptors (AGPR) on their plasma membrane, was decreased by the addition of free AF and cytochalasin B. AF-lps bound to HepG2 cells through specific interaction with AGPR, and were internalized into the cells by the receptor-mediated endocytotic pathway. HepG2 cells transfected by AF-lps-pSV2CAT showed a significantly higher CAT activity than those transfected by pSV2CAT associated with non-labeled control lps (N-lps-pSV2CAT) or a mixture of pSV2CAT and empty AF-lps. Pretreatment with EDTA-encapsulated AF-lps increased the transfection efficiency of AF-lps-pSV2CAT. The CAT activity in A431 and Swiss/3T3 cells transfected with AF-lps-pSV2CAT was low and almost the same as those transfected with N-lps-pSV2CAT. Since DNA encapsulated in lps is likely to be protected against digestion by nucleases in the blood circulation, AF-lps could be used as a gene transfer vector targeting the hepatocytes in vivo.

Asialoglycoprotein Receptor↗

PubMed1995

Contribution of mannose receptor to signal transduction in Fc gamma receptor-mediated phagocytosis of mouse peritoneal macrophages induced by liposomes.

The contribution of mannose receptors on the cell surface of mouse peritoneal macrophages to the process of liposome-induced phagocytosis of immunoglobulin G-opsonized sheep red blood cells (SRBCs) through Fc gamma receptor has been investigated. Fc gamma receptor-mediated phagocytosis of opsonized SRBCs was activated by modified alpha 2-macroglobulin, which was produced in the incubation mixture of alpha 2-macroglobulin and liposome-treated splenic B cells. The phagocytosis was specifically inhibited by the addition of D-mannose, and the inhibition was dependent on the D-mannose concentration. The binding of modified alpha 2-macroglobulin to macrophages was also reduced by the addition of D-mannose. The activation effect of modified alpha 2-macroglobulin was not inhibited when in the presence of alpha 2-macroglobulin-trypsin and -methylamine complexes. In the presence of cycloheximide, activated phagocytosis was reduced to the control level. By Scatchard plot analysis of IgG binding studies, the number of Fc gamma receptors of a macrophage had been increased to 4.6-fold that of a control macrophage by treatment with modified alpha 2-macroglobulin. These findings suggest that macrophage mannose receptors are involved in activating the process of Fc gamma receptor-mediated phagocytosis of opsonized SRBCs induced by modified alpha 2-macroglobulin. Lectins may participate in a signal transduction in macrophage activation by liposomes.

Animals↗

PubMed1995

Interferon-gamma inductive effect of liposomes as an immunoadjuvant.

Adjuvant effect of liposomes was compared to that of aluminium hydroxide (Alum) using ovalbumin (OVA) as a model antigen, and the difference in adjuvanticity of liposomes from Alum has been evaluated on the basis of cytokine production. Both adjuvants enhanced the IgG levels, but a remarkable difference was observed in the production of IgG subclass; Alum enhanced IgG1 levels, and liposomes enhanced IgG2a, IG2b, and IG3 levels. Further, Alum enhanced antigen-specific IgE levels, whereas liposomes did not. To clarify the difference in adjuvant effect of these adjuvants, secretion of cytokines, especially interferon-gamma (IFN-gamma) and interleukin-4 (IL-4) which regulate IgE production, was estimated ex vivo. Overnight culture of splenic cells obtained from mice immunized with liposomes encapsulating OVA elicits IFN-gamma secretion, but not IL-4 secretion. On the other hand, the production of both cytokines was elevated by the immunization with OVA-Alum complex. The results indicate that the difference of adjuvant activity between liposomes and Alum may come from the difference in the secretion of IL-4 and that, consequently, a different class of antibody response is developed. More importantly, negatively charged liposomes containing phosphatidylserine remarkably promoted IFN-gamma secretion compared to neutral liposomes.

Adjuvants, Immunologic↗