The inhibition of cell signaling pathways by antitumor ether lipids.
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Animals↗
Biomedical subjects
G Arthur
Publications and source records attributed to G Arthur.
The relationship between a patient's spirituality and health experiences.
BACKGROUND AND OBJECTIVES: The relationship between spirituality and health is a new frontier in medicine. This study is a preliminary investigation into the relationship between a patient's experience of overall health, physical pain, and intrinsic spirituality. METHODS: We used a stratified, random sample of 462 patients at a family practice residency clinic. The Index of Core Spiritual Experiences (INSPIRIT) measured intrinsic spirituality, and Dartmouth Primary Care Cooperative Charts measured overall health and pain. Pearson correlations tested the association between health, pain, and spirituality. Patient scores on the INSPIRIT were then placed into three groups (high, medium, and low levels of intrinsic spirituality). ANOVA tested for significant differences in health and pain. RESULTS: We collected information from 442 of the patients surveyed (95%). We found significant correlation between patient health and spirituality. Significant differences were also found in both overall health and physical pain, based on the three levels of spirituality. Gender differences were only significant for overall health, not for patient pain. CONCLUSIONS: Our results suggest an association between intrinsic spirituality and a patient's experience of health and pain. Assessment of spirituality may be important for family physicians to consider as a supplement to patient interviews.
Adult↗
1-O-Octadecyl-2-O-methylglycerophosphocholine inhibits protein kinase C-dependent phosphorylation of endogenous proteins in MCF-7 cells.
Studies with leukaemic cells, based primarily on in vitro assays, have suggested that antitumour ether lipids have only a moderate effect on protein kinase C (PKC) activity, and, furthermore, inhibition of PKC is unlikely to be involved in the mechanism of inhibition of cell proliferation by these compounds. To determine if this is also the case for epithelial cancer cells, we examined the effect of 1-O-octadecyl-2-O-methylglycerophosphocholine (ET18-OCH3) on PKC-induced phosphorylation of endogenous proteins in MCF-7 cells under incubation conditions where the drug inhibited cell proliferation. As expected, stimulation of quiescent 32P-labelled MCF-7 cells with 1 microM PMA resulted in the phosphorylation of a number of proteins. The PMA-induced phosphorylation of the proteins was abolished by preincubation of the cells with Ro 31-8220 (5 microM) for 20 min, or 10 microg/ml ET18-OCH3 for 3 h before stimulation with PMA. Thus under incubation conditions where ET18-OCH3 inhibited the proliferation of MCF-7 cells, the ether lipid potently inhibited the activity of PKC in intact cells. This inhibition was unlikely to be due to the effect of the compound on PKC translocation since there was little effect of ET18-OCH3 on the translocation of the alpha, gamma and epsilon species of PKC. These results suggest that a role for the inhibition of PKC activity by ET18-OCH3 in the mechanism of inhibition of cell proliferation by ET18-OCH3 cannot yet be discounted in epithelial cancer cells. In addition, we also observed that ET18-OCH3 enhanced the phosphorylation of selected proteins under basal unstimulated conditions. Although some of these proteins were also observed to be phosphorylated in response to PMA stimulation, the phosphorylation induced by ET18-OCH3 was not inhibited by Ro 31-8220, indicating that this was not mediated by PKC.
Biological Transport↗
Enantioselective synthesis and antiproliferative properties of an ilmofosine analog, 2'-(trimethylammonio)ethyl 3-(hexadecyloxy)-2-(methoxymethyl)propyl phosphate, on epithelial cancer cell growth.
An asymmetric synthesis of the 1-alkyloxy analog of the thioether phosphocholine ilmofosine (BM 41.440, rac-1), 2'-(trimethylammonio)ethyl 3-(hexadecyloxy)-2-(methoxymethyl)propyl phosphate (2), is described. Stereoselectivity was obtained in an asymmetric hydroboration-oxidation sequence carried out on a 2,2-disubstituted 1-alkene, 3-(hexadecyloxy)-2-(methoxymethyl)-1-propene (9), which was prepared by starting with either ethyl acrylate or ethyl alpha-(hydroxymethyl)acrylate (3). (R)- and (S)-2 and rac-1 were highly effective in inhibiting the proliferation of the breast adenocarcinoma cell line MCF-7 (IC50, 2 microM), moderately effective against A549 (non-small-cell lung adenocarcinoma) (IC50, 8-10 icroM), and less effective against A427 (large cell lung carcinoma) (IC50, approximately 20 microM). The in vitro cytotoxicity against the three epithelial cancer cell lines was independent of the configuration about C-2 of the glycerol backbone of 2 and was also not altered by substitution of oxygen for sulfur in the sn-1 ether linkage of ilmofosine.
Antineoplastic Agents↗
Heterogeneity of polyclonal IgE characterized by differential charge, affinity to protein A, and antigenicity.
Functional and physical heterogeneity of polyclonal IgE has been reported. Extremely low serum concentrations of IgE have limited the study of these important differences. We have purified polyclonal dog IgE and developed polyclonal and monoclonal (mAb C2) anti-dog IgE antibodies. In this study chromatofocusing of dog IgE revealed two biologically active IgE fractions: IgE1 eluted at pH 5.0, and IgE2 eluted at pH 4.7. The two IgE subforms (IgEs) exhibited typical IgE characteristics: positive in the 48-hour passive cutaneous anaphylaxis response, heat-labile, identical molecular weight, and reactive to polyclonal anti-dog IgE. However, the two IgEs were found to be significantly heterogeneous. IgE1 bound to protein A and did not react with mAb C2 in ELISA and isoelectric focusing-immunoblotting, whereas IgE2 did not bind to protein A and reacted with mAb C2. Further, in sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting, IgE2, but not IgE1, reacted with seven well-defined mAb anti-human IgE antibodies and an mAb anti-mouse IgE antibody, even though both IgE1 and IgE2 reacted with polyclonal anti-human and anti-mouse IgE. Neuraminidase or endoglycosidase treatment did not abolish the differential antigenicity and charge of IgE1 and IgE2, although the antigenicity of IgE2 was significantly reduced after incubation with endoglycosidase. These data suggest that carbohydrate moieties are not involved in the observed differences in antigenicity and charge and that the two IgE molecules represent distinct isotypes. In studies with seven purified IgE fractions obtained from different ragweed-allergic dogs, the distribution of ragweed IgE2 varied 200-fold, whereas ragweed total IgE levels varied only fourfold. This raises the possibility of a relationship between different IgEs and the allergic response.
Animals↗
1-O-octadecyl-2-O-methyl-glycerophosphocholine inhibits the transduction of growth signals via the MAPK cascade in cultured MCF-7 cells.
1-O-Octadecyl-2-O-methyl-glycerophosphocholine (ET18-OCH3) is an ether lipid with selective antiproliferative properties whose mechanism of action is still unresolved. We hypothesized that since ET18-OCH3 affects a wide variety of cells, its mechanism of action was likely to involve the inhibition of a common widely used pathway for transducing growth signals such as the mitogen-activated protein kinase (MAPK) cascade. To test this, we established conditions whereby quiescent MCF-7 cells took up ET18-OCH3 in sufficient quantities that inhibited cell proliferation subsequent to the addition of growth medium and examined the activation of components of the MAPK cascade under these conditions. ET18-OCH3 inhibited the sustained phosphorylation of MAPK resulting in a decrease in the magnitude and duration of activation of MAPK in cells stimulated with serum or EGF. ET18-OCH3 had no effect on the binding of EGF to its receptors, their activation, or p21ras activation. However, an interference in the association of Raf-1 with membranes and a resultant decrease in Raf-1 kinase activity in membranes of ET18-OCH3-treated cells was observed. ET18-OCH3 had no direct effect on MAPK or Raf-1 kinase activity. A direct correlation between ET18-OCH3 accumulation, inhibition of cell proliferation, Raf association with the membrane, and MAPK activation was also established. These results suggest that inhibition of the MAPK cascade by ET18-OCH3 as a result of its effect on Raf-1 activation may be an important mechanism by which ET18-OCH3 inhibits cell proliferation.
Calcium-Calmodulin-Dependent Protein Kinases↗
Synthesis and evaluation of the antiproliferative effects of 1-O-hexadecyl-2-O-methyl-3-O-(2'-acetamido-2'-deoxy-beta-D- glucopyranosyl)-sn-glycerol and 1-O-hexadecyl-2-O-methyl-3-0- (2'-amino-2'-deoxy-beta-D-glucopyranosyl)-sn-glycerol on epithelial cancer cell growth.
Two ether glucosyl diglyceride analogs were synthesized, and their antiproliferative activity against four epithelial cancer cell lines was evaluated. 1-O-Hexadecyl-2-O-methyl-3-O-(2'-acetamido-2'-deoxy-beta-D- glucopyranosyl)-sn-glycerol (4) was synthesized by reaction of 2-acetamido-2-deoxy-3,4,6-tri-O-acetyl-alpha-D-glucopyranosyl chloride with 1-O-hexadecyl-2-O-methyl-sn-glycerol followed by deacetylation by methanolic hydrolysis. The N-acetyl group of 4 was removed by hydrolysis with ethanolic potassium hydroxide to form 1-O-hexadecyl-2-O-methyl-3-O-(2'-amino-2'-deoxy-beta-D-glucopyranosyl)- sn-glycerol (5). Compounds 4 and 5 inhibited the proliferation of MCF-7, A549, A427, and T84 cancer cell lines. The IC(50) values for 5 ranged from 6.5 to 12.2 microM, whereas 4 was more effective against A549 cells (IC(50) 9 microM) than against MCF-7 (IC(50) 17 microM) and A427 (IC(50) 25 microM) cells and was inactive against T84 cells. Under identical incubation conditions, compounds 4 and 5 were potent inhibitors of the proliferation of OVCAR-3 cells with IC(50) values of 12 and 4 microM, respectively, whereas ET-18-OCH(3), hexadecylphosphocholine, and erucylphosphocholine had IC(50) values of 24, >30, and >30 microM, respectively. The cell-inhibitory profile of these ether-linked glucosyl diglycerides strengthens the hypothesis that such glycolipids represent a distinct group of antitumor ether lipids, having antineoplastic activities that differ from the well-known alkylphosphocholines and alkyllysophospholipids.
Antineoplastic Agents↗
Evidence for receptor and G-protein regulation of a phosphatidylethanolamine-hydrolysing phospholipase A1 in guinea-pig heart microsomes: stimulation of phospholipase A1 activity by DL-isoprenaline and guanine nucleotides.
While evidence has been presented for the receptor-mediated activation of phospholipases A2, C and D, the activation of phospholipase A1 subsequent to receptor activation has not been established. Phospholipase A1-catalysed hydrolysis of 1-palmitoyl-2-linoleoyl-glycerophosphoethanolamine (GPE) by guinea-pig heart microsomes was stimulated 40-60% by isoprenaline. This isoprenaline-mediated increase in activity was blocked by propranolol and butoxamine, a specific beta 2-adrenergic antagonist, but not by atenolol, a specific beta 1-adrenergic antagonist. Neither clonidine nor phenylephrine, alpha 1- and alpha 2-adrenergic agonists respectively, had a stimulatory effect on the hydrolysis of the PE substrate. Guanosine 5'(-)[gamma-thio]triphosphate (GTP[S]) and guanosine 5'(-)[beta,gamma-imido]triphosphate, but not guanosine 5'(-)[beta-thio]diphosphate (GDP[S]) or adenosine 5'(-)[gamma-thio]triphosphate, stimulated the hydrolysis of 1-palmitoyl-2-linoleoyl-GPE by phospholipase A1. GDP[S] inhibited the isoprenaline-mediated stimulation of phospholipase A1 activity. Phospholipase A1 hydrolysis of 1-palmitoyl-2-linoleoyl-GPE was not dependent on cations; however, the stimulatory effects of isoprenaline and GTP[S] on the hydrolytic activity were abolished by cation chelators. The above data suggest that phospholipase A1 activity in guinea-pig heart microsomes is activated by the binding of isoprenaline to beta 2-adrenergic receptors. Furthermore the stimulation of phospholipase A1 activity by the agonist may be mediated via activation of G-proteins.
Adrenergic beta-Agonists↗
Effect of 1-O-octadecyl-2-O-methyl-glycerophosphocholine on phosphatidylcholine and phosphatidylethanolamine synthesis in MCF-7 and A549 cells and its relationship to inhibition of cell proliferation.
The role of perturbation of lipid synthesis in the inhibition of cell proliferation by OctMeGroPCho was investigated with sensitive (MCF-7) and resilient (A549) cell lines. It inhibited de novo synthesis of phosphatidylcholine in both cells but increased triacylglycerol synthesis in A549 cells and phosphatidylethanolamine, phosphatidic acid and diacylglycerol synthesis in MCF-7 cells. The inhibition of synthesis of CDP-choline metabolites in MCF-7 cells and phosphatidylcholine biosynthetic enzyme activities in vitro by OctMeGroPCho suggests that direct inhibition of phosphocholine cytidylyltransferase may contribute to the observed inhibition of phosphatidylcholine synthesis. The activation of phosphoethanolamine cytidylyltransferase and ethanolamine phosphotransferase activities by OctMeGroPCho in vitro and increased production of CDP-ethanolamine suggest that stimulation of the above enzymes by OctMeGroPCho in the cells is responsible for the increased phosphatidylethanolamine synthesis. The apparent effect of OctMeGroPCho on intracellular lipid-metabolising enzymes is a strong indication that it may be widely distributed intracellularly and not just confined to the plasma membrane. The decrease in phosphatidylcholine synthesis by OctMeGroPCho in MCF-7 cells was prevented by co-incubation with oleic acid without any effect on the inhibition of cell growth. Although OctMeGroPCho resulted in similar decreases in phosphatidylcholine content in both cells, this did not affect the proliferation of A549 cells. The above results indicate that, although OctMeGroPCho has profound effects on lipid metabolism, these changes are not responsible for the inhibition of proliferation observed in MCF-7 cells.
Antineoplastic Agents↗
Calcium-supported calpain degradation rates for cardiac myofibrils in diabetes. Sulfhydryl and hydrophobic interactions.
OBJECTIVE: The purpose was to investigate the calcium required for calpain-mediated degradation of selected cardiac myofibril proteins modified by diabetes, sulfhydryl (SH) and hydrophobic reagents. METHODS: After 20 weeks of streptozotocin-induced (55 mg.kg-1) diabetes, calcium sensitive calpain (1.5 U.ml-1) degradation rates of purified cardiac myofibrillar proteins (1 mg.ml-1) were measured, in vitro, and compared to degradation rates for N-ethylmaleimide (NEM) and 2-p-toluidinylnapthalene-6-sulfonate (TNS) treated samples. RESULTS: Diabetes (blood glucose of 550 +/- 32 mg.dl-1) reduced the yield of purified myofibrillar protein with minimal change in fibril protein composition. Total SH group reactivities (nmol.mg-1.30min) were 220 +/- 21, 163 +/- 17 and 156 +/- 24 for control, diabetic and NEM-treated (0.5 mM) myofibrils (p < or = 0.05). Calpain degradation rates were faster for all diabetic and SH modified myofibrillar proteins (p < or = 0.05), with a 45 and 35% reduction in the pCa50 for a 37 kDa protein of diabetic and NEM-treated fibril complexes. For control myofibrils, both 100 and 200 uM TNS, reduced calpain degradation rates to a similar extent for all substrate proteins. In contrast, diabetic and NEM-treated samples showed a further reduction in calpain degradation rates with increasing TNS from 100 to 200 uM. CONCLUSION: Our results support the hypothesis that in diabetes the calcium requirements for calpain degradation rates are reduced and dependent upon sulfhydryl group status and Ca(2+)-induced hydrophobic interactions, implicating a 37 kDa myofbillar-complexed protein.
Animals↗
Krypton fluoride excimer laser ablation of tooth tissues: precision tissue machining.
A variety of lasers using different wavelengths have been used to remove dental hard tissue. The infrared lasers produce their effects photothermally whereas ultraviolet excimer lasers remove tissue in a controlled and precise manner by photoablation. This study investigates the use of 248 nm laser radiation in the precision removal of both enamel and dentine using diffraction limited ultraviolet optics. The data showed that enamel and dentine were machined to a high level of precision (1-2 micron tolerances). The rate of removal was greater in dentine than enamel at a range of energy densities between 1.15 and 2.2 J/cm2. The method of removal of both tissues appears to be by the preferential ablation of the organic phases of each, exposing the anatomical details of their structure. An explanation of the possible method of ablation is proposed for these tissues.
Dental Enamel↗
Complementary therapies used by people with HIV infection.
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Complementary Therapies↗
Wedge factors for rectangular fields.
The variation of wedge factor with field size was measured for a range of square and rectangular fields for 45 degrees and 60 degrees wedges. Measurements were performed on accelerators with both externally mounted wedges, the Varian 600C of nominal energy 6MV and internally mounted wedges, the Philips SL75/5 of nominal energy 6MV and the Philips SL25 of nominal energy 25MV. Analysis of the results confirm previous investigations reported in the literature of the variation of wedge factor with field size and in particular the significantly greater variation for internally mounted wedges. A wedge factor for a rectangular field based on the wedge factor of the open field equivalent square gives a maximum error of 1.5%. A wedge factor for a rectangular field based on the wedge factor of the square field of equal area reduces the maximum error to 0.5% for all three accelerators. Analysis of results reported in the literature show a similar reduction.
Particle Accelerators↗
The ethanolamine requirement of keratinocytes for growth is not due to defective synthesis of ethanolamine phosphoacylglycerols by the decarboxylation pathway.
We have investigated whether the growth requirement of keratinocytes for ethanolamine is due to defective synthesis of ethanolamine phosphoacylglycerols (EPG) via decarboxylation of serine phosphoacylglycerols. Proliferating keratinocytes readily incorporated [3H]ethanolamine into phosphatidylethanolamine (PE) and [3H]serine into phosphatidylserine (PS) and PE. Non-proliferating keratinocytes in ethanolamine-free medium incorporated [3H]glycerol into phosphatidylcholine (PC), PS and PE in decreasing order of label incorporated. The order of decreasing incorporation of glycerol after addition of ethanolamine to the medium was PC > PE > PS. Incubation of non-proliferating keratinocytes with [3H]serine resulted in incorporation of label into PS and PE. The extent of incorporation of [3H]serine into PS in non-proliferating keratinocytes was not less than that in proliferating cells. Addition of ethanolamine to the medium of non-proliferating keratinocytes did not change the quantity of label incorporated into PS, but resulted in a decrease of label incorporated into PE. When cells were prelabelled overnight with [3H]serine and subsequently incubated in medium containing ethanolamine, the loss of label from PS was inhibited relative to that of control cells incubated in medium without ethanolamine. The activity of PS decarboxylase activity in keratinocyte mitochondria was inhibited by phosphoethanolamine and PE, but not by ethanolamine or CDP-ethanolamine. Both proliferating and non-proliferating keratinocytes incorporated [3H]serine into ether-linked ethanolamine phospholipids. Taken together, the above results suggest that (1) both proliferating and non-proliferating keratinocytes are able to synthesize PE and ether-linked ethanolamine phospholipids from serine, and therefore the ethanolamine-requirement of the cells is not due to a defective decarboxylase pathway; (2) any inability of the decarboxylase pathway to meet cellular EPG requirement is not due to decreased synthesis of serine phospholipids; (3) synthesis of PE via decarboxylation, the major route in nonproliferating keratinocytes, appears to decrease when ethanolamine is made available and the CDP-ethanolamine pathway is functioning; (4) phosphoethanolamine and increased PE produced from the CDP-ethanolamine pathway may inhibit PS decarboxylase activity in the cells and provide a means of coordinating the synthesis of PE by the two pathways to prevent excess production.
Cell Division↗
Effect of delta 9-tetrahydrocannabinol and merthiolate on acyltransferase activities in guinea pig liver microsomes.
delta 9-Tetrahydrocannabinol (THC) and merthiolate have been utilized as lysophospholipid acyltransferase inhibitors in metabolic studies. However, their effects on acyltransferases other than lysophosphatidylcholine:acyl-CoA acyltransferase (LPCAT) are not known. We have therefore investigated the effectiveness of THC and merthiolate in inhibiting the acylation of lysophosphatidylcholine, lysophosphatidylethanolamine, lysophosphatidylserine, lysophosphatidylinositol (LPI) and lysophosphatidic acid (LPA) in guinea pig liver microsomes using oleoyl-CoA and arachidonoyl-CoA as acyl donors. THC inhibited LPCAT and lysophosphatidylethanolamine:acyl-CoA acyltransferase (LPEAT) by 40-50%, but had no effect or only slightly increased the activities of the other acyltransferases when assayed with oleoyl-CoA as the acyl donor. The results obtained with arachidonoyl-CoA were similar to those with oleoyl-CoA, with the exception of a 40% inhibition of lysophosphatidylserine:acyl-CoA acyltransferase (LPSAT) at concentrations of 50 microM or higher. At similar concentrations, merthiolate was more effective than THC in inhibiting the acyltransferases examined. Selective effects on the acyltransferases were observed at low concentrations of merthiolate (20 microM or less). Thus, LPCAT was most susceptible, followed by LPI acyltransferases, LPSAT, LPEAT and lysophosphatidic acid:acyl-CoA acyltransferases (LPAAT). The presence of LPA did not affect the inhibition of LPCAT by merthiolate. Thus the resilience of LPAAT to merthiolate inhibition was not due to chelation of the compound by the acidic lysolipid. Thiol reagents including N-ethyl-maleiamide, 5,5'-dithio-bis-nitrobenzoic acid, iodoacetate, beta-mercaptoethanol and dithiothreitol had little or no effect on the acyltransferases relative to equimolar concentrations of merthiolate.(ABSTRACT TRUNCATED AT 250 WORDS)
Acyl Coenzyme A↗
3-Deazaadenosine and MDL29350 differentially affect the methylation of serine-and ethanolamine-derived phosphatidylethanolamine in Hep G2 cells.
The effect of 3-deazaadenosine (DZA) and the hypolipidemic drug MDL29350 (2-[3,5-di(t-butyl-4-hydroxyphenyl)thio]hexanoic acid) on the synthesis and methylation of phosphatidylethanolamine (PE) originating from the cytidine diphosphate (CDP) ethanolamine pathway and PE originating from decarboxylation of phosphatidylserine (PS) was investigated. DZA and MDL29350 did not affect the synthesis of PE by either pathway; however, methylation of ethanolamine-derived PE was inhibited by 80% and methylation of serine-derived PE was inhibited by 36% by 20 mumol/LDZA or MDL29350. The differential inhibition of the methylation of PE synthesized via serine or ethanolamine suggests that in Hep G2 cells PE-N-methyltransferase (PENMT) may be segregated into distinct compartments that are differentially accessible to the drugs.
Caproates↗
Binding of dog immunoglobulins G, A, M, and E to concanavalin A.
The binding of dog immunoglobulins G, A, M and E to concanavalin A (Con A) has been investigated. A passive cutaneous anaphylaxis test was used for measurement of dog IgE, and enzyme-linked immunosorbent assay was used for measurement of dog IgG, IgA and IgM. After the dog serum fraction was applied to a Con A-Sepharose column, sequential elution with different buffers was performed; 100% of IgE and IgM, 60% of IgG and 58% of IgA bound to the Con A-Sepharose. IgE was eluted by mannose, methylglucose, and methylmannoside. IgG was eluted by glucose, mannose, methylglucose, and methylmannoside. IgA and IgM were eluted by methylmannoside only. This provides a useful technique in the purification of dog immunoglobulins, especially dog IgE.
Animals↗
Purification and identification of polyclonal IgE antibodies from ragweed-sensitized dog sera.
We have purified and characterized polyclonal dog IgE. Serum IgE was precipitated by (NH4)2SO4 and then purified by two different procedures. Ion exchange on DEAE-Sephacel, followed by HPLC using Tonen hydroxylapatite and then Protein G-Sepharose, produced a highly purified IgE fraction (No. 1) free of IgG, IgA and IgM as measured by ELISA, but recovery of IgE as measured by passive cutaneous anaphylaxis was low. Gel filtration on Sephacryl S-300, Con A-Sepharose and Protein G-Sepharose recovered 18% of initial IgE, 0.02% IgG, 0.4% IgM and 0.3% IgA. This IgE fraction (No. 2) was used to induce antibody production in rabbits. Western blot analysis was then performed for dog IgE fractions No. 1 and 2. Using the rabbit anti-dog IgE, a prominent IgE band with an apparent molecular mass of 226 kD was identified in fractions No. 1 and 2 subjected to nonreducing SDS-PAGE. This band also reacted with anti-human IgE, but not with anti-dog IgG or anti-dog IgA. Under reducing conditions the approximate molecular mass for the IgE & chain, estimated by Western blot using rabbit anti-dog IgE, was 73 kD, providing a molecular mass of 196 kD for dog IgE.
Allergens↗