PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12202492-4 2002 In unpolarized pBCEC, high density lipoprotein, subclass 3 (HDL3)-dependent [3H]cholesterol efflux, was unaffected by 24(S)OH-cholesterol treatment but was enhanced 5-fold in SR-BI overexpressing pBCEC. Tritium 77-79 HDL3 Homo sapiens 22-58 12542695-4 2003 However, the pronounced capacity for specific cell association of [3H]CE-HDL3 and selective [3H]CE-uptake in excess of HDL3-holoparticle association, and cAMP-mediated enhanced cell association of [3H]CE-HDL3 in JAr and Jeg3 suggested the scavenger receptor class B, type I (SR-BI) to be responsible for this pathway. Tritium 67-69 HDL3 Homo sapiens 73-77 12542695-6 2003 Adenovirus-mediated overexpression of SR-BI in all three choriocarcinoma cell lines resulted in an enhanced capacity for cell association of [3H]CE-HDL3 (20-fold in BeWo; fivefold in JAr and Jeg3). Tritium 142-144 HDL3 Homo sapiens 148-152 12907677-4 2003 CETP-mediated CE transfers from [3H]CE VLDL to various lipoproteins, combined on an equal phospholipid basis, ranged 2-fold and followed the order: HDL3 > LDL > HDL2. Tritium 33-35 HDL3 Homo sapiens 148-152 12565706-6 2003 A polyclonal antiserum raised against SR-BI significantly decreased cell-association of [3H]CE-HDL3 in HUH-7 and WRL-68. Tritium 89-91 HDL3 Homo sapiens 95-99 12202492-4 2002 In unpolarized pBCEC, high density lipoprotein, subclass 3 (HDL3)-dependent [3H]cholesterol efflux, was unaffected by 24(S)OH-cholesterol treatment but was enhanced 5-fold in SR-BI overexpressing pBCEC. Tritium 77-79 HDL3 Homo sapiens 60-64 12202492-8 2002 HDL3 was a better promoter of basolateral [3H]cholesterol efflux than lipid-free apoA-I. Tritium 43-45 HDL3 Homo sapiens 0-4 9862176-5 1998 HDL3 (d = 1.125-1.21 g/ml) was radiolabeled in its protein (125I) and in its CE moiety ([3H]cholesteryl oleyl ether, ([3H]CEt)). Tritium 89-91 HDL3 Homo sapiens 0-4 9888879-7 1999 HDL3- and apolipoprotein (apo) A-I-mediated cellular cholesterol and phosphatidylcholine efflux was examined by labeling cells with [3H]cholesterol and [3H]choline, respectively, during growth and cholesterol loading during growth arrest. Tritium 133-135 HDL3 Homo sapiens 0-4 9888879-7 1999 HDL3- and apolipoprotein (apo) A-I-mediated cellular cholesterol and phosphatidylcholine efflux was examined by labeling cells with [3H]cholesterol and [3H]choline, respectively, during growth and cholesterol loading during growth arrest. Tritium 153-155 HDL3 Homo sapiens 0-4 10438151-9 1999 The fate of 3H-CE of the two best CE donors (LDL and HDL3) was followed in HepG2 cells after 3 h of incubation. Tritium 12-14 HDL3 Homo sapiens 53-57 10438151-11 1999 However, when the cells were treated with 100 microM of chloroquine, a lysosomotropic agent, 85 and 40% of 3H-CE hydrolysis was lost for LDL and HDL3, respectively. Tritium 107-109 HDL3 Homo sapiens 145-149 11714843-12 2001 LPL stimulated [3H]cholesteryl oleyl ether uptake from labeled HDL3 by HEK 293 cells substantially, showing that LPL can induce selective CE uptake from HDL3 independent of SR-BI. Tritium 16-18 HDL3 Homo sapiens 63-67 11714843-12 2001 LPL stimulated [3H]cholesteryl oleyl ether uptake from labeled HDL3 by HEK 293 cells substantially, showing that LPL can induce selective CE uptake from HDL3 independent of SR-BI. Tritium 16-18 HDL3 Homo sapiens 153-157 9862176-8 1998 In the absence of HL, the rate of apparent HDL3 particle uptake according to the lipid tracer ([3H]CEt) was in most cases in approximately 10-fold excess on that due to the protein label (125I), indicating selective CE uptake from HDL3. Tritium 96-98 HDL3 Homo sapiens 43-47 9554975-7 1998 A positive correlation was demonstrated between changes in HDL3 binding and changes in [3H]cholesterol efflux. Tritium 88-90 HDL3 Homo sapiens 59-63 9684736-2 1998 Human HDL3 (d 1.125-1.21 g/ml) was radiolabeled with 125I in the protein moiety and with 3H in the CE moiety. Tritium 89-91 HDL3 Homo sapiens 6-10 9684736-5 1998 Without LPL, apparent HDL3 particle uptake according to the lipid tracer (3H) was in excess of that due to the protein label (125I) indicating selective CE uptake from HDL3. Tritium 74-76 HDL3 Homo sapiens 22-26 9034243-9 1997 Moreover, HDL3 obtained after both diets produced identical [3H] free cholesterol efflux from human monocyte-derived macrophages (29%) and fibroblasts (26%). Tritium 61-63 HDL3 Homo sapiens 10-14 9194766-8 1997 HDL3-mediated [3H]cholesterol efflux was also inhibited in Dex-treated cells; moreover, HDL3 (40 micrograms/mL, 24 hours) had practically no effect on [3H]cholesteryl ester content in Dex-treated SMC but caused a 50% reduction of [3H]cholesteryl esters in the control cells. Tritium 15-17 HDL3 Homo sapiens 0-4 8519599-6 1995 In [3H]-palmitic acid-prelabelled fibroblasts, both HDL3 and LDL were observed to stimulate production of DAG. Tritium 4-6 HDL3 Homo sapiens 52-56 8856073-3 1996 In reconstituted mixtures, all the carboxylated derivatives increased progressively and significantly the transfer of 3H-labeled cholesteryl esters from [3H]CE-HDL3 towards LDL in the 20-100 microM concentration range. Tritium 118-120 HDL3 Homo sapiens 160-164 8856073-3 1996 In reconstituted mixtures, all the carboxylated derivatives increased progressively and significantly the transfer of 3H-labeled cholesteryl esters from [3H]CE-HDL3 towards LDL in the 20-100 microM concentration range. Tritium 154-156 HDL3 Homo sapiens 160-164 8660296-12 1996 The ability of PMN-modified HDL3 to remove 3H-labelled free cholesterol from cells was measured in two cell lines: Fu5AH rat hepatoma cells and J774 mouse macrophages. Tritium 43-45 HDL3 Homo sapiens 28-32 7578801-2 1995 LDL and HDL3 dose-dependently (EC50 values approximately 50 micrograms/ml) stimulated DNA and protein synthesis ([3H]-thymidine and [3H]-leucine incorporation, respectively) in the absence of exogenously added mitogens. Tritium 114-116 HDL3 Homo sapiens 8-12 7578801-2 1995 LDL and HDL3 dose-dependently (EC50 values approximately 50 micrograms/ml) stimulated DNA and protein synthesis ([3H]-thymidine and [3H]-leucine incorporation, respectively) in the absence of exogenously added mitogens. Tritium 133-135 HDL3 Homo sapiens 8-12 8396616-10 1993 When HDL3 binding on phospholipid sites was inhibited by rigid phospholipid particles, the stimulation of [3H]thymidine incorporation related to HDL3 concentration did not show a maximum peak as previously observed but reached a plateau at a concentration as low as 5 micrograms HDL3 protein/ml. Tritium 107-109 HDL3 Homo sapiens 5-9 8003090-3 1994 HDL3 (d = 1.125-1.21 g/ml) was labeled in its apolipoprotein A-I moiety with 125I and in its CE moiety with [3H]cholesteryl oleyl ether. Tritium 109-111 HDL3 Homo sapiens 0-4 8379932-4 1993 In contrast, with an increasing degree of radical-mediated oxidation of labelled HDL3, [3H]cholesteryl linoleate ([3H]Ch18:2) was taken up at an increasingly greater rate than were 125I-apoproteins. Tritium 88-90 HDL3 Homo sapiens 81-85 8379932-5 1993 When [3H]cholesteryl linoleate hydroperoxide ([3H]Ch18:2-OOH was incorporated into unoxidized HDL3 by exchange from donor liposomes, it was taken up at a more than 8-fold higher rate than was incorporated [3H]Ch18:2. Tritium 6-8 HDL3 Homo sapiens 94-98 8379932-5 1993 When [3H]cholesteryl linoleate hydroperoxide ([3H]Ch18:2-OOH was incorporated into unoxidized HDL3 by exchange from donor liposomes, it was taken up at a more than 8-fold higher rate than was incorporated [3H]Ch18:2. Tritium 47-49 HDL3 Homo sapiens 94-98 8379932-6 1993 The same degree of preferential uptake of oxidized CE was observed when HDL3 was used that was doubly labelled with [3H]Ch18:2-OOH and cholesteryl [14C]oleate ([14C]Ch18:1). Tritium 117-119 HDL3 Homo sapiens 72-76 8379932-8 1993 This increased selective uptake of [3H]Ch18:2-OOH from very mildly oxidized HDL3 was accompanied by a parallel increase in the intracellular levels of labelled free cholesterol. Tritium 36-38 HDL3 Homo sapiens 76-80 8241097-4 1993 Results obtained showed that American HDL3, irrespective of the plasma HDL-C level, had higher activity in stimulating both [3H]cholesterol and cholesterol mass efflux from cholesterol-loaded fibroblasts and in suppressing cellular cholesterol esterification when compared with Russian HDL3. Tritium 125-127 HDL3 Homo sapiens 38-42 8318513-5 1993 HDL3 isolated after the monounsaturated fatty acid diet induced the greatest cellular [3H]free cholesterol efflux, reduced the content of intracellular cholesterol, and enhanced 125I-LDL degradation. Tritium 87-89 HDL3 Homo sapiens 0-4 8318513-6 1993 Univariate regression analyses suggested that the increased capacity of HDL3 to promote cellular [3H]free cholesterol efflux was in part due to its greater fluidity, higher cholesteryl ester content, elevated linoleic to linolenic acid ratio in phospholipids, and its smaller size. Tritium 98-100 HDL3 Homo sapiens 72-76 8396616-10 1993 When HDL3 binding on phospholipid sites was inhibited by rigid phospholipid particles, the stimulation of [3H]thymidine incorporation related to HDL3 concentration did not show a maximum peak as previously observed but reached a plateau at a concentration as low as 5 micrograms HDL3 protein/ml. Tritium 107-109 HDL3 Homo sapiens 145-149 8396616-10 1993 When HDL3 binding on phospholipid sites was inhibited by rigid phospholipid particles, the stimulation of [3H]thymidine incorporation related to HDL3 concentration did not show a maximum peak as previously observed but reached a plateau at a concentration as low as 5 micrograms HDL3 protein/ml. Tritium 107-109 HDL3 Homo sapiens 145-149 1333103-2 1992 In (3H) PC prelabelled platelets, phosphocholine is released into the medium during HDL3 induced PC turnover with a 1.5 to 2 fold increment, indicating that HDL3 stimulated DAG generation in platelets is likely due to phospholipase C (PLC). Tritium 4-6 HDL3 Homo sapiens 84-88 8443247-11 1993 With both types of membrane, apparent HDL3 particle association according to [3H]cholesteryl oleate-labeled HDL3 was in significant excess on that due to 125I-HDL3. Tritium 78-80 HDL3 Homo sapiens 38-42 8443247-11 1993 With both types of membrane, apparent HDL3 particle association according to [3H]cholesteryl oleate-labeled HDL3 was in significant excess on that due to 125I-HDL3. Tritium 78-80 HDL3 Homo sapiens 108-112 8443247-11 1993 With both types of membrane, apparent HDL3 particle association according to [3H]cholesteryl oleate-labeled HDL3 was in significant excess on that due to 125I-HDL3. Tritium 78-80 HDL3 Homo sapiens 108-112 8418891-8 1993 Efflux of [3H]cholesterol from plasma membranes was stimulated to similar extents by Lp A-I and Lp A-I/A-II isolated from either HDL2, HDL3 or plasma. Tritium 11-13 HDL3 Homo sapiens 135-139 1333103-2 1992 In (3H) PC prelabelled platelets, phosphocholine is released into the medium during HDL3 induced PC turnover with a 1.5 to 2 fold increment, indicating that HDL3 stimulated DAG generation in platelets is likely due to phospholipase C (PLC). Tritium 4-6 HDL3 Homo sapiens 157-161 2397248-1 1990 Apo E-free human high-density lipoprotein (HDL3) was labeled with 125I in apoprotein and with 3H in cholesteryl linoleyl ether (a non-hydrolyzable analogue of cholesteryl ester). Tritium 94-96 HDL3 Homo sapiens 43-47 2175955-1 1990 Low concentrations of HDL3 stimulate a transient biphasic increase in 1,2-diacylglycerol (DAG), with an early phase peaking at 30 seconds and a late phase at 60 seconds in (3H)-phosphatidylcholine prelabelled platelets. Tritium 173-176 HDL3 Homo sapiens 22-26 2400395-8 1990 More 3H radioactivity, but not the cholesterol, was precipitated from HDL2 or HDL3 by the reagent, demonstrating that 3H-labelled HDL2 and HDL3 behave like their fraction C, which becomes labelled to the highest specific radioactivity despite having the smallest mass. Tritium 5-7 HDL3 Homo sapiens 78-82 2400395-8 1990 More 3H radioactivity, but not the cholesterol, was precipitated from HDL2 or HDL3 by the reagent, demonstrating that 3H-labelled HDL2 and HDL3 behave like their fraction C, which becomes labelled to the highest specific radioactivity despite having the smallest mass. Tritium 118-120 HDL3 Homo sapiens 78-82 2400395-8 1990 More 3H radioactivity, but not the cholesterol, was precipitated from HDL2 or HDL3 by the reagent, demonstrating that 3H-labelled HDL2 and HDL3 behave like their fraction C, which becomes labelled to the highest specific radioactivity despite having the smallest mass. Tritium 118-120 HDL3 Homo sapiens 139-143 2400395-13 1990 Kinetics of the transfer of HDL [3H]cholesteryl oleate to VLDL showed a greater apparent Vmax for fractions A than for fractions B from either HDL2 or HDL3, whereas the apparent Km values were very similar, which suggest that this transfer process is influenced by the apoprotein composition of the donor lipoprotein. Tritium 33-35 HDL3 Homo sapiens 151-155 2271659-1 1990 The transfer of [3H]cholesterol in low-density lipoprotein (LDL) to different high-density lipoprotein (HDL) species in native human plasma was determined by using nondenaturing two-dimensional electrophoresis. Tritium 17-19 HDL3 Homo sapiens 104-107 2397248-4 1990 Both 125I and 3H labels from control HDL3 were cleared from rat blood monoexponentially, but 3H at a faster rate than 125I (3H t1/2 = 3.0-4.1 h; 125I t1/2 = 7.0-7.7 h). Tritium 14-16 HDL3 Homo sapiens 37-41 2322573-9 1990 A prior phospholipase treatment of HDL3 stimulated by 2-5-fold the uptake of [3H]cholesteryl ether, whereas the transfer of free [14C]cholesterol was minimally increased. Tritium 77-81 HDL3 Homo sapiens 35-39 2322573-10 1990 The uptake of 3H/14C-labelled sterols from HDL2 was 2-3-times higher than from HDL3. Tritium 14-16 HDL3 Homo sapiens 79-83 2322573-15 1990 Competition experiments showed that 12-times more unlabelled HDL3 were required to half reduce the uptake of HDL3 [3H]cholesteryl ether than to impede similarly the HDL 125I-apolipoprotein recovered in cells. Tritium 115-118 HDL3 Homo sapiens 61-65 2322573-15 1990 Competition experiments showed that 12-times more unlabelled HDL3 were required to half reduce the uptake of HDL3 [3H]cholesteryl ether than to impede similarly the HDL 125I-apolipoprotein recovered in cells. Tritium 115-118 HDL3 Homo sapiens 109-113 3803386-1 1987 Human high-density lipoproteins HDL2 (d = 1.068-1.125) and HDL3 (d = 1.125-1.210) doubly labelled with [3H]cholesterol/cholesteryl ester and with [acyl-14C]phosphatidylcholine were further incubated with phospholipases. Tritium 104-106 HDL3 Homo sapiens 59-63 2820959-4 1987 HDL3 and TNM-HDL3 were found to be equally effective in causing efflux of plasma membrane cholesterol radiolabeled with [3H]cholesterol. Tritium 121-123 HDL3 Homo sapiens 0-4 2820959-4 1987 HDL3 and TNM-HDL3 were found to be equally effective in causing efflux of plasma membrane cholesterol radiolabeled with [3H]cholesterol. Tritium 121-123 HDL3 Homo sapiens 13-17 2820959-5 1987 However, HDL3 was much more effective than TNM-HDL3 in causing efflux of [3H]cholesterol associated with intracellular membranes. Tritium 74-76 HDL3 Homo sapiens 9-13 2820959-5 1987 However, HDL3 was much more effective than TNM-HDL3 in causing efflux of [3H]cholesterol associated with intracellular membranes. Tritium 74-76 HDL3 Homo sapiens 47-51 2820959-6 1987 By measuring movement of endogenously synthesized [3H]cholesterol to the plasma membrane, and into the medium, we found that HDL3 induced a rapid movement of [3H]cholesterol from a preplasma membrane compartment to the plasma membrane that preceded [3H]cholesterol efflux. Tritium 51-53 HDL3 Homo sapiens 125-129 2820959-6 1987 By measuring movement of endogenously synthesized [3H]cholesterol to the plasma membrane, and into the medium, we found that HDL3 induced a rapid movement of [3H]cholesterol from a preplasma membrane compartment to the plasma membrane that preceded [3H]cholesterol efflux. Tritium 159-161 HDL3 Homo sapiens 125-129 2820959-6 1987 By measuring movement of endogenously synthesized [3H]cholesterol to the plasma membrane, and into the medium, we found that HDL3 induced a rapid movement of [3H]cholesterol from a preplasma membrane compartment to the plasma membrane that preceded [3H]cholesterol efflux. Tritium 159-161 HDL3 Homo sapiens 125-129 3607054-1 1987 Membranes isolated from bovine adrenal cortex, incubated with human high-density lipoproteins (HDL3), labeled with 125I and [3H]cholesteryl linoleyl ether, showed preferential binding of [3H]cholesteryl linoleyl ether. Tritium 124-128 HDL3 Homo sapiens 95-99 3607054-1 1987 Membranes isolated from bovine adrenal cortex, incubated with human high-density lipoproteins (HDL3), labeled with 125I and [3H]cholesteryl linoleyl ether, showed preferential binding of [3H]cholesteryl linoleyl ether. Tritium 125-127 HDL3 Homo sapiens 95-99 3111539-6 1987 The uptake of HDL cholesteryl ester by intact adipocytes as monitored by [3H]cholesteryl ether labeled HDL3, was also significantly reduced (about 35% reduction, P less than 0.005) by substituting apolipoprotein A-II for A-I in HDL3. Tritium 74-76 HDL3 Homo sapiens 103-107 2918251-4 1989 However, in macrophages that were not loaded with cholesterol, HDL3 stimulated net movement of 3H-labeled sterol from the plasma membrane into intracellular compartments, the opposite direction from that seen for cholesterol-loaded cells. Tritium 95-97 HDL3 Homo sapiens 63-67 3572251-1 1987 In this study we determined in vivo conversions of human 3H-labeled cholesteryl ester-labeled HDL3 [( 3H]CE-HDL3) in male rats and the effects of partially purified lipid transfer protein on the conversion processes. Tritium 57-59 HDL3 Homo sapiens 94-98 3572251-1 1987 In this study we determined in vivo conversions of human 3H-labeled cholesteryl ester-labeled HDL3 [( 3H]CE-HDL3) in male rats and the effects of partially purified lipid transfer protein on the conversion processes. Tritium 57-59 HDL3 Homo sapiens 108-112 3572251-1 1987 In this study we determined in vivo conversions of human 3H-labeled cholesteryl ester-labeled HDL3 [( 3H]CE-HDL3) in male rats and the effects of partially purified lipid transfer protein on the conversion processes. Tritium 102-104 HDL3 Homo sapiens 94-98 3572251-1 1987 In this study we determined in vivo conversions of human 3H-labeled cholesteryl ester-labeled HDL3 [( 3H]CE-HDL3) in male rats and the effects of partially purified lipid transfer protein on the conversion processes. Tritium 102-104 HDL3 Homo sapiens 108-112 3572251-2 1987 Zonal centrifugation techniques were used to prepare the [3H]CE-HDL3 and to follow the conversion processes. Tritium 58-60 HDL3 Homo sapiens 64-68 3572251-5 1987 In vitro incubation of [3H]CE-HDL3 in rat plasma reproduced in part the HDL3----HDL2 conversion, but no movement of radioactivity to HDL1 was observed. Tritium 24-26 HDL3 Homo sapiens 30-34 3572251-5 1987 In vitro incubation of [3H]CE-HDL3 in rat plasma reproduced in part the HDL3----HDL2 conversion, but no movement of radioactivity to HDL1 was observed. Tritium 24-26 HDL3 Homo sapiens 72-76 6793575-8 1981 Direct incubation of HDL3 or human serum with 3H-glycosphingolipid dispersions did not yield a glycolipid . Tritium 46-48 HDL3 Homo sapiens 21-25 7126623-2 1982 [3H]Cholesteryl esters were formed by endogenous HDL3/VHDL enzyme (d greater than 1.125 g/ml) following incubation with mixed vesicles of phosphatidylcholine, unesterified cholesterol and 3H-labelled unesterified cholesterol. Tritium 1-3 HDL3 Homo sapiens 49-53 7126623-2 1982 [3H]Cholesteryl esters were formed by endogenous HDL3/VHDL enzyme (d greater than 1.125 g/ml) following incubation with mixed vesicles of phosphatidylcholine, unesterified cholesterol and 3H-labelled unesterified cholesterol. Tritium 188-190 HDL3 Homo sapiens 49-53