PMID- 21605334 OWN - NLM STAT- MEDLINE DCOM- 20120203 LR - 20181201 IS - 1538-7836 (Electronic) IS - 1538-7836 (Linking) VI - 9 IP - 8 DP - 2011 Aug TI - Statins prevent tissue factor induction by protease-activated receptors 1 and 2 in human umbilical vein endothelial cells in vitro. PG - 1608-19 LID - 10.1111/j.1538-7836.2011.04366.x [doi] AB - BACKGROUND: Protease-activated receptors (PARs) are G-protein-coupled receptors that function in hemostasis and thrombosis, as well as in the inflammatory and proliferative responses triggered by tissue injury. We have previously shown that PAR1 or PAR2 occupancy by specific PAR-agonist peptides (PAR-APs) induces tissue factor (TF) expression in human umbilical vein endothelial cells (HUVECs), where TF regulation by PAR1 (but not by PAR2) requires intact endothelial caveolin-enriched membrane microdomains in which PAR1 and caveolin-1 associate. OBJECTIVES: The aim of this study was to determine the effects of cholesterol-lowering agents (statins) and cholesterol-loading lipoprotein on PAR1-AP-mediated and PAR2-AP-mediated TF induction in HUVECs. RESULTS: Statins completely prevented TF induction by PAR-APs in an isoprenoid-independent manner, induced the delocalization of PAR1 from caveolin-enriched membrane microdomains without affecting PAR1 mRNA, and decreased PAR2 mRNA and protein levels. Statins also prevented PAR-AP-mediated extracellular signal-related kinase 1/2 activation, which is crucial for TF induction. The redistribution of PAR1 is accompanied by the relocation of the membrane microdomain-associated G-protein alpha, caveolin-1, and Src, which we previously showed to play a key role in signal transduction and TF induction. Conversely, cholesterol loading potently amplified PAR1-AP-induced TF, probably as a result of the increased abundance of PAR1 and the Src and G-protein alpha signaling molecules in the caveolin-1-enriched fraction, without affecting PAR1 mRNA. CONCLUSIONS: As PARs have important functions in hemostasis, cancer, thrombosis, and inflammatory processes, our findings that statins prevent TF induction by PAR-APs altering the membrane localization of PAR1 and the expression of PAR2 suggest that they may provide health benefits other than reducing atherosclerosis. CI - (c) 2011 International Society on Thrombosis and Haemostasis. FAU - Banfi, C AU - Banfi C AD - Centro Cardiologico Monzino IRCCS, Milan, Italy. cristina.banfi@ccfm.it FAU - Brioschi, M AU - Brioschi M FAU - Lento, S AU - Lento S FAU - Pirillo, A AU - Pirillo A FAU - Galli, S AU - Galli S FAU - Cosentino, S AU - Cosentino S FAU - Tremoli, E AU - Tremoli E FAU - Mussoni, L AU - Mussoni L LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - England TA - J Thromb Haemost JT - Journal of thrombosis and haemostasis : JTH JID - 101170508 RN - 0 (CAV1 protein, human) RN - 0 (Caveolin 1) RN - 0 (Fatty Acids, Monounsaturated) RN - 0 (Fluorobenzenes) RN - 0 (GTP-Binding Protein alpha Subunits) RN - 0 (Hydroxymethylglutaryl-CoA Reductase Inhibitors) RN - 0 (Indoles) RN - 0 (Pyrimidines) RN - 0 (RNA, Messenger) RN - 0 (Receptor, PAR-1) RN - 0 (Receptor, PAR-2) RN - 0 (Sulfonamides) RN - 0 (Terpenes) RN - 4L066368AS (Fluvastatin) RN - 83MVU38M7Q (Rosuvastatin Calcium) RN - 9035-58-9 (Thromboplastin) RN - 97C5T2UQ7J (Cholesterol) RN - EC 2.7.10.2 (src-Family Kinases) RN - EC 2.7.11.24 (MAPK1 protein, human) RN - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1) RN - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3) RN - S5UOB36OCZ (Mevalonic Acid) SB - IM MH - Caveolin 1/metabolism MH - Cells, Cultured MH - Cholesterol/metabolism MH - Enzyme Activation MH - Fatty Acids, Monounsaturated/*pharmacology MH - Fluorobenzenes/*pharmacology MH - Fluvastatin MH - GTP-Binding Protein alpha Subunits/metabolism MH - Human Umbilical Vein Endothelial Cells/*drug effects/metabolism MH - Humans MH - Hydroxymethylglutaryl-CoA Reductase Inhibitors/*pharmacology MH - Indoles/*pharmacology MH - Membrane Microdomains/drug effects/metabolism MH - Mevalonic Acid/metabolism MH - Mitogen-Activated Protein Kinase 1/metabolism MH - Mitogen-Activated Protein Kinase 3/metabolism MH - Phosphorylation MH - Protein Transport MH - Pyrimidines/*pharmacology MH - RNA, Messenger/metabolism MH - Receptor, PAR-1/*drug effects/genetics/metabolism MH - Receptor, PAR-2/*drug effects/genetics/metabolism MH - Rosuvastatin Calcium MH - Signal Transduction/drug effects MH - Sulfonamides/*pharmacology MH - Terpenes/metabolism MH - Thromboplastin/*metabolism MH - Up-Regulation MH - src-Family Kinases/metabolism EDAT- 2011/05/25 06:00 MHDA- 2012/02/04 06:00 CRDT- 2011/05/25 06:00 PHST- 2011/05/25 06:00 [entrez] PHST- 2011/05/25 06:00 [pubmed] PHST- 2012/02/04 06:00 [medline] AID - 10.1111/j.1538-7836.2011.04366.x [doi] PST - ppublish SO - J Thromb Haemost. 2011 Aug;9(8):1608-19. doi: 10.1111/j.1538-7836.2011.04366.x. PMID- 16220532 OWN - NLM STAT- MEDLINE DCOM- 20060327 LR - 20051123 IS - 1615-9853 (Print) IS - 1615-9853 (Linking) VI - 5 IP - 17 DP - 2005 Nov TI - Proteome of endothelial cell-derived procoagulant microparticles. PG - 4443-55 AB - Microparticles (MP) are small membrane vesicles that are released from cells upon activation or during apoptosis. Cellular MP in body fluids constitute a heterogeneous population, differing in cellular origin, numbers, size, antigenic composition and functional properties. MP support coagulation by exposure of tissue factor (TF), the initiator of coagulation in vivo. Moreover, MP may transfer bioactive molecules to other cells, thereby stimulating them to produce cytokines, cell-adhesion molecules, growth factors and TF, and modulate endothelial functions. However, a comprehensive characterization of the antigenic composition of MP has been poorly defined. This study describes the protein composition of endothelial cell (EC)-derived MP (EMP) using a proteomic approach. MS analysis indicated the presence of newly described protein such as metabolic enzymes, proteins involved in adhesion and fusion processes, members of protein folding event, cytoskeleton associated proteins and nucleosome. In conclusion, circulating EMP behave as an actual storage pool, able to disseminate blood-borne TF activity and other bioactive effectors, as confirmed by our experiments showing an increased procoagulant activity of EC exposed to EMP. FAU - Banfi, Cristina AU - Banfi C AD - Department of Pharmacological Sciences, University of Milan, Italy. cristina.banfi@unimi.it FAU - Brioschi, Maura AU - Brioschi M FAU - Wait, Robin AU - Wait R FAU - Begum, Shajna AU - Begum S FAU - Gianazza, Elisabetta AU - Gianazza E FAU - Pirillo, Angela AU - Pirillo A FAU - Mussoni, Luciana AU - Mussoni L FAU - Tremoli, Elena AU - Tremoli E LA - eng PT - Journal Article PL - Germany TA - Proteomics JT - Proteomics JID - 101092707 RN - 0 (Enzymes) RN - 0 (Peptide Fragments) RN - 0 (Proteins) RN - 0 (Tumor Necrosis Factor-alpha) RN - 9035-58-9 (Thromboplastin) SB - IM MH - Amino Acid Sequence MH - Apoptosis MH - Blood Coagulation/*physiology MH - Cell Membrane/*ultrastructure MH - Cells, Cultured MH - Endothelium, Vascular/drug effects/*physiology/ultrastructure MH - Enzymes/chemistry/isolation & purification MH - Humans MH - Molecular Sequence Data MH - Peptide Fragments/analysis/chemistry MH - Proteins/chemistry/isolation & purification MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MH - Thromboplastin/*analysis MH - Tumor Necrosis Factor-alpha/pharmacology MH - Umbilical Veins EDAT- 2005/10/13 09:00 MHDA- 2006/03/28 09:00 CRDT- 2005/10/13 09:00 PHST- 2005/10/13 09:00 [pubmed] PHST- 2006/03/28 09:00 [medline] PHST- 2005/10/13 09:00 [entrez] AID - 10.1002/pmic.200402017 [doi] PST - ppublish SO - Proteomics. 2005 Nov;5(17):4443-55. doi: 10.1002/pmic.200402017. PMID- 11879189 OWN - NLM STAT- MEDLINE DCOM- 20020419 LR - 20181113 IS - 0264-6021 (Print) IS - 0264-6021 (Linking) VI - 362 IP - Pt 3 DP - 2002 Mar 15 TI - Macrophage metalloproteinases degrade high-density-lipoprotein-associated apolipoprotein A-I at both the N- and C-termini. PG - 627-34 AB - Atheromatous plaques contain various cell types, including macrophages, endothelial cells and smooth-muscle cells. To investigate the possible interactions between secreted matrix metalloproteinases and high-density lipoprotein (HDL) components, we tested the above cell types by culturing them for 24 h. HDL(3) (HDL subfractions with average sizes of between 8.44 nm for HDL(3A) and 7.62 nm for HDL(3C)) were then incubated in their cell-free conditioned media. Proteolytic degradation of apolipoprotein A-I was observed with macrophages, but not with endothelial-cell- or muscle-cell-conditioned supernatant. Absence of calcium or addition of EDTA to incubation media prevented all proteolytic processes. The identified apolipoprotein A-I fragments had sizes of 26, 22, 14 and 9 kDa. Two-dimensional electrophoresis and MS resolved the 26 and the 22 kDa components and identified peptides resulting from both N- and C-terminal cleavage of apolipoprotein A-I. The higher abundance of C- than N-terminally cleaved peptides agrees with data in the literature for a fully structured alpha-helix around Tyr(18) compared with an unstructured region around Gly(185) and Gly(186). The flexibility in the latter region of apolipoprotein A-I may explain its susceptibility to proteolysis. In our experimental set-up, HDL(3C) was more extensively degraded than the other HDL(3) subclasses (HDL(3A) and HDL(3B)). Proteolytic fragments produced by metalloproteinase action were shown by gel filtration and electrophoresis to be neither associated with lipids nor self-associated. FAU - Eberini, Ivano AU - Eberini I AD - Dipartimento di Scienze Farmacologiche, Universita degli Studi di Milano, via G. Balzaretti, 9, I-20133 Milan, Italy. FAU - Calabresi, Laura AU - Calabresi L FAU - Wait, Robin AU - Wait R FAU - Tedeschi, Gabriella AU - Tedeschi G FAU - Pirillo, Angela AU - Pirillo A FAU - Puglisi, Lina AU - Puglisi L FAU - Sirtori, Cesare R AU - Sirtori CR FAU - Gianazza, Elisabetta AU - Gianazza E LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - England TA - Biochem J JT - The Biochemical journal JID - 2984726R RN - 0 (Apolipoprotein A-I) RN - 0 (Culture Media, Conditioned) RN - 0 (Lipoproteins, HDL) RN - 0 (Peptide Fragments) RN - EC 3.4.24.- (Metalloendopeptidases) SB - IM MH - Animals MH - Apolipoprotein A-I/chemistry/*metabolism MH - Cell Line MH - Cells, Cultured MH - Chromatography, Gel MH - Culture Media, Conditioned MH - Endothelium, Vascular MH - Humans MH - Kinetics MH - Lipoproteins, HDL/*metabolism MH - Macrophages, Peritoneal/*enzymology MH - Metalloendopeptidases/*metabolism MH - Peptide Fragments/chemistry MH - Rats MH - Substrate Specificity MH - Umbilical Veins PMC - PMC1222426 EDAT- 2002/03/07 10:00 MHDA- 2002/04/20 10:01 CRDT- 2002/03/07 10:00 PHST- 2002/03/07 10:00 [pubmed] PHST- 2002/04/20 10:01 [medline] PHST- 2002/03/07 10:00 [entrez] PST - ppublish SO - Biochem J. 2002 Mar 15;362(Pt 3):627-34. PMID- 10799307 OWN - NLM STAT- MEDLINE DCOM- 20000613 LR - 20131121 IS - 0006-291X (Print) IS - 0006-291X (Linking) VI - 271 IP - 2 DP - 2000 May 10 TI - Enhanced macrophage uptake of elastase-modified high-density lipoproteins. PG - 386-91 AB - Incubation of human HDL (d = 1.063-1.21 g/ml) with monocyte-derived elastase causes selective proteolysis of apoA-II and apoA-I apolipoproteins. We have found that elastase-digested HDL (ED-HDL) bind to J774-A1 murine macrophages with enhanced affinity and are internalized and degraded at a rate threefold higher than that of native HDL. Unlike oxidized LDL and HDL and proteolytically modified LDL, the uptake of ED-HDL lipoproteins does not affect the cellular lipid biosynthesis nor modify the cell lipid content. The cell surface binding of (125)I-ED-HDL can be competed by native HDL but not by acetylated LDL, consistent with the idea that ED-HDL are recognized by the class B type I scavenger receptor. The liberation of elastase by lipid-engorging macrophages is regarded as an important event during atherogenesis. By enhancing the cellular uptake of HDL this process can lead to a local decrease of antiatherogenic HDL particles. CI - Copyright 2000 Academic Press. FAU - Pirillo, A AU - Pirillo A AD - Department of Pharmacology, Istituto di Scienze Farmacologiche, Milan, Italy. FAU - Ghiselli, G AU - Ghiselli G LA - eng PT - Journal Article PL - United States TA - Biochem Biophys Res Commun JT - Biochemical and biophysical research communications JID - 0372516 RN - 0 (Cholesterol Esters) RN - 0 (Lipoproteins, HDL) RN - 0 (Triglycerides) RN - 97C5T2UQ7J (Cholesterol) RN - EC 3.4.21.37 (Leukocyte Elastase) SB - IM MH - Animals MH - Cells, Cultured MH - Cholesterol/metabolism MH - Cholesterol Esters/metabolism MH - Dose-Response Relationship, Drug MH - Humans MH - Kinetics MH - Leukocyte Elastase/*metabolism MH - Lipid Metabolism MH - Lipoproteins, HDL/blood/chemistry/*metabolism MH - Macrophages/*metabolism MH - Mice MH - Time Factors MH - Triglycerides/metabolism EDAT- 2000/05/09 09:00 MHDA- 2000/06/17 09:00 CRDT- 2000/05/09 09:00 PHST- 2000/05/09 09:00 [pubmed] PHST- 2000/06/17 09:00 [medline] PHST- 2000/05/09 09:00 [entrez] AID - 10.1006/bbrc.2000.2649 [doi] AID - S0006-291X(00)92649-4 [pii] PST - ppublish SO - Biochem Biophys Res Commun. 2000 May 10;271(2):386-91. doi: 10.1006/bbrc.2000.2649. PMID- 8820097 OWN - NLM STAT- MEDLINE DCOM- 19961206 LR - 20181130 IS - 0022-2275 (Print) IS - 0022-2275 (Linking) VI - 37 IP - 1 DP - 1996 Jan TI - Inhibition of acyl-CoA: cholesterol acyltransferase decreases apolipoprotein B-100-containing lipoprotein secretion from HepG2 cells. PG - 1-14 AB - There is evidence that the overproduction of apoB-100-containing lipoproteins by the liver is the underlying event in some forms of dyslipoproteinemia. This metabolic status is associated to an increased risk of developing premature coronary artery disease CAD. The conclusions from previous studies suggested that the availability to the hepatocytes of cholesterol that is readily esterified is an important determinant for VLDL and LDL secretion. In the present study, we set out to investigate the effect of the specific stimulation and inhibition of the rate-limiting enzyme of the cholesterol esterification, acyl-CoA:cholesterol acyltransferase (ACAT, E.C. 2.3.1.26), on the lipid and on the apoB-100 secretion rate from a human hepatoma cell line (HepG2). When the specific ACAT inhibitor FCE 27677 (10-5 M) was added to the cultures, a decrease of the cellular cholesteryl ester content and at the same time a significant reduction of the neutral lipids and of the apoB-100 secretion rate were noticed. The stimulation of ACAT by 25-hydroxycholesterol (20 microgram/ml) caused a 4-fold increase of the cellular cholesteryl ester content and a 2-fold increase of the lipoprotein secretion rate. FCE 27677 (10-5 M to 10-7 M) prevented the effects elicited by the oxysterol. On the contrary, lovastatin (10-6 M) and gemfibrozil (10-6 M) had no effect. The analysis of the lipid and of the apolipoprotein composition of the lipoproteins secreted in the medium revealed that ACAT inhibition had the dual effect of both decreasing the number of apoB-100-containing lipoproteins secreted as well as their cholesteryl ester load. Altogether, these data support the idea of a close relationship between ACAT activation, leading to increased cholesteryl ester availability, and apoB-100-containing lipoprotein secretion. It is speculated that ACAT inhibitors may prove useful for the treatment of human dyslipoproteinemias caused by the hepatic overproduction of apoB-100-containing lipoproteins. FAU - Musanti, R AU - Musanti R AD - Pharmacia Farmitalia Carlo Erba Research Institute, Cardiovascular Department, Milan, Italy. FAU - Giorgini, L AU - Giorgini L FAU - Lovisolo, P P AU - Lovisolo PP FAU - Pirillo, A AU - Pirillo A FAU - Chiari, A AU - Chiari A FAU - Ghiselli, G AU - Ghiselli G LA - eng PT - Comparative Study PT - Journal Article PL - United States TA - J Lipid Res JT - Journal of lipid research JID - 0376606 RN - 0 (Albumins) RN - 0 (Aniline Compounds) RN - 0 (Apolipoprotein B-100) RN - 0 (Apolipoproteins B) RN - 0 (Enzyme Inhibitors) RN - 0 (FCE 27677) RN - 0 (Hydroxycholesterols) RN - 0 (Hypolipidemic Agents) RN - 0 (Lipids) RN - 0 (Phenylurea Compounds) RN - 767JTD2N31 (25-hydroxycholesterol) RN - 9LHU78OQFD (Lovastatin) RN - EC 2.3.1.26 (Sterol O-Acyltransferase) RN - Q8X02027X3 (Gemfibrozil) SB - IM MH - Albumins/metabolism MH - Aniline Compounds/*pharmacology MH - Apolipoprotein B-100 MH - Apolipoproteins B/*metabolism MH - Enzyme Inhibitors/*pharmacology MH - Gemfibrozil/pharmacology MH - Humans MH - Hydroxycholesterols/metabolism MH - Hypolipidemic Agents/pharmacology MH - Lipids/biosynthesis MH - Liver/cytology/*metabolism MH - Lovastatin/pharmacology MH - Phenylurea Compounds/*pharmacology MH - Sterol O-Acyltransferase/*antagonists & inhibitors MH - Tumor Cells, Cultured EDAT- 1996/01/01 00:00 MHDA- 1996/01/01 00:01 CRDT- 1996/01/01 00:00 PHST- 1996/01/01 00:00 [pubmed] PHST- 1996/01/01 00:01 [medline] PHST- 1996/01/01 00:00 [entrez] PST - ppublish SO - J Lipid Res. 1996 Jan;37(1):1-14. PMID- 7541706 OWN - NLM STAT- MEDLINE DCOM- 19950816 LR - 20131121 IS - 1350-6277 (Print) IS - 1350-6277 (Linking) VI - 2 IP - 2 DP - 1995 Apr TI - Oxidized lipoproteins induce long-lasting inhibition of nitric oxide synthase from a murine endothelioma cell line (bEnd.4). PG - 123-30 AB - BACKGROUND: The vascular endothelium produces nitric oxide, which has vasodilatory properties. It has been postulated that some lipoproteins may increase arterial vascular tone by decreasing the availability of endothelium-derived nitric oxide. The mechanism underlying this effect, however, is still poorly understood. METHODS: We investigated the effect of native and oxidized human low- and high-density lipoproteins on the nitric oxide synthetic activity of an endothelioma cell line (bEnd.4). Oxidized lipoproteins were obtained by incubation with CuSO4. The production of nitric oxide by the cells was monitored by quantifying the nitrite concentration in the medium using Greiss reagent. RESULTS: The synthesis of nitric oxide by the bEnd.4 cell line was calcium-dependent and was abolished by a selective inhibitor of the constitutive nitric oxide synthase. Incubation with oxidized lipoproteins caused a time- and dose-dependent inhibition of nitric oxide synthetic activity. At a concentration of 100 micrograms/ml cholesterol, oxidized low- and high-density lipoproteins inhibited the production of nitric oxide by 27 and 51%, respectively, within 6h. The lipid fraction obtained from the native or the oxidized lipoproteins mimicked the effect of the intact lipoproteins. CONCLUSION: These results support the involvement of oxidized lipoproteins in the modulation of endothelial functions relevant to the pathogenesis of cardiovascular disease. FAU - Fogliatto, G AU - Fogliatto G AD - Pharmacia Farmitalia Carlo Erba Research Institute, Milan, Italy. FAU - Musanti, R AU - Musanti R FAU - Pirillo, A AU - Pirillo A FAU - Ghiselli, G AU - Ghiselli G LA - eng PT - Journal Article PL - England TA - J Cardiovasc Risk JT - Journal of cardiovascular risk JID - 9436980 RN - 0 (Calmodulin-Binding Proteins) RN - 0 (Lipoproteins, HDL) RN - 0 (Lipoproteins, LDL) RN - 0 (Nitrites) RN - 31C4KY9ESH (Nitric Oxide) RN - 789U1901C5 (Copper) RN - 97C5T2UQ7J (Cholesterol) RN - EC 1.14.13.39 (Nitric Oxide Synthase) RN - EC 1.4.- (Amino Acid Oxidoreductases) RN - EC 1.6.99.1 (NADPH Dehydrogenase) RN - LRX7AJ16DT (Copper Sulfate) RN - SY7Q814VUP (Calcium) SB - IM MH - Amino Acid Oxidoreductases/*antagonists & inhibitors MH - Animals MH - Calcium/pharmacology MH - Calmodulin-Binding Proteins/*antagonists & inhibitors MH - Cholesterol/administration & dosage/pharmacology MH - Chromatography, High Pressure Liquid MH - Copper/chemistry MH - Copper Sulfate MH - Dose-Response Relationship, Drug MH - Endothelium, Vascular/metabolism MH - Hemangioendothelioma/*enzymology/metabolism MH - Humans MH - Lipoproteins, HDL/administration & dosage/chemistry/*pharmacology MH - Lipoproteins, LDL/administration & dosage/chemistry/*pharmacology MH - Mice MH - Muscle, Smooth, Vascular/metabolism MH - NADPH Dehydrogenase/*antagonists & inhibitors MH - Nitric Oxide/antagonists & inhibitors/metabolism MH - Nitric Oxide Synthase MH - Nitrites/antagonists & inhibitors/metabolism MH - Oxidation-Reduction MH - Tumor Cells, Cultured EDAT- 1995/04/01 00:00 MHDA- 1995/04/01 00:01 CRDT- 1995/04/01 00:00 PHST- 1995/04/01 00:00 [pubmed] PHST- 1995/04/01 00:01 [medline] PHST- 1995/04/01 00:00 [entrez] PST - ppublish SO - J Cardiovasc Risk. 1995 Apr;2(2):123-30. PMID- 8101992 OWN - NLM STAT- MEDLINE DCOM- 19930902 LR - 20141120 IS - 0031-7144 (Print) IS - 0031-7144 (Linking) VI - 48 IP - 6 DP - 1993 Jun TI - Astragalosides from Egyptian Astragalus spinosus Vahl. PG - 452-4 AB - Four cycloartane triterpene oligoglycosides were isolated from the n-butanol extract of the aerial parts of Astragalus spinosus Vahl. (Leguminosae). They were identified as astragaloside I (1), isoastragaloside I (2), astragaloside IV (4) and cycloastragenol 6-O-glucoside (5) on the basis of comparing their m.p.'s, 1H NMR and 13C NMR spectra and chromatographic patterns with the data given in the literature. The results of AIDS antiviral and antitumor screening of the major component, astragaloside II (3), are dealt with. FAU - Abdallah, R M AU - Abdallah RM AD - Faculty of Pharmacy, University of Alexandria, Egypt. FAU - Ghazy, N M AU - Ghazy NM FAU - El-Sebakhy, N A AU - El-Sebakhy NA FAU - Pirillo, A AU - Pirillo A FAU - Verotta, L AU - Verotta L LA - eng PT - Journal Article PL - Germany TA - Pharmazie JT - Die Pharmazie JID - 9800766 RN - 0 (Antineoplastic Agents, Phytogenic) RN - 0 (Antiviral Agents) RN - 0 (Glucosides) SB - IM SB - X MH - Antineoplastic Agents, Phytogenic/*pharmacology MH - Antiviral Agents/*pharmacology MH - CD4-Positive T-Lymphocytes/drug effects/microbiology MH - Drug Screening Assays, Antitumor MH - Egypt MH - Glucosides/isolation & purification/*pharmacology MH - HIV/drug effects MH - Humans MH - In Vitro Techniques MH - Magnetic Resonance Spectroscopy MH - Plants, Medicinal/*chemistry EDAT- 1993/06/01 00:00 MHDA- 1993/06/01 00:01 CRDT- 1993/06/01 00:00 PHST- 1993/06/01 00:00 [pubmed] PHST- 1993/06/01 00:01 [medline] PHST- 1993/06/01 00:00 [entrez] PST - ppublish SO - Pharmazie. 1993 Jun;48(6):452-4.