PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 4335797-9 1972 Inhibition of plasma lecithin:cholesterol acyltransferase reduced the exchange of sphingomyelin but had no effect on lecithin exchange. Sphingomyelins 82-95 lecithin-cholesterol acyltransferase Homo sapiens 21-57 7407066-0 1980 Interaction of lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in the transport of cholesteryl ester into sphingomyelin liposomes. Sphingomyelins 134-147 lecithin-cholesterol acyltransferase Homo sapiens 15-51 16319418-4 2006 Analysis of LCAT kinetics parameters (V(max) and K(m)) revealed that either LpA-I or plasma HDL from NPD-B, as well as reconstituted HDL enriched with SM, exhibited severely decreased LCAT-mediated cholesterol esterification. Sphingomyelins 151-153 lecithin-cholesterol acyltransferase Homo sapiens 12-16 16605271-0 2006 Regulation of the activity and fatty acid specificity of lecithin-cholesterol acyltransferase by sphingomyelin and its metabolites, ceramide and ceramide phosphate. Sphingomyelins 97-110 lecithin-cholesterol acyltransferase Homo sapiens 57-93 16605271-1 2006 Sphingomyelin (SM), the second most abundant phospholipid in plasma lipoproteins, was previously shown to be a physiological inhibitor of the lecithin-cholesterol acyltransferase (LCAT) reaction. Sphingomyelins 0-13 lecithin-cholesterol acyltransferase Homo sapiens 142-178 16605271-1 2006 Sphingomyelin (SM), the second most abundant phospholipid in plasma lipoproteins, was previously shown to be a physiological inhibitor of the lecithin-cholesterol acyltransferase (LCAT) reaction. Sphingomyelins 0-13 lecithin-cholesterol acyltransferase Homo sapiens 180-184 16605271-1 2006 Sphingomyelin (SM), the second most abundant phospholipid in plasma lipoproteins, was previously shown to be a physiological inhibitor of the lecithin-cholesterol acyltransferase (LCAT) reaction. Sphingomyelins 15-17 lecithin-cholesterol acyltransferase Homo sapiens 142-178 16605271-1 2006 Sphingomyelin (SM), the second most abundant phospholipid in plasma lipoproteins, was previously shown to be a physiological inhibitor of the lecithin-cholesterol acyltransferase (LCAT) reaction. Sphingomyelins 15-17 lecithin-cholesterol acyltransferase Homo sapiens 180-184 8702592-0 1996 Sphingomyelin inhibits the lecithin-cholesterol acyltransferase reaction with reconstituted high density lipoproteins by decreasing enzyme binding. Sphingomyelins 0-13 lecithin-cholesterol acyltransferase Homo sapiens 27-63 9507105-4 1998 Increasing Lp2A-I POPC or SPH content also significantly inhibits cholesterol esterification by LCAT. Sphingomyelins 26-29 lecithin-cholesterol acyltransferase Homo sapiens 96-100 8702592-3 1996 In order to clarify the role of sphingomyelin in the regulation of the LCAT reaction and its effects on the structure of apolipoprotein A-I, we prepared reconstituted HDL (rHDL) containing egg phosphatidylcholine, cholesterol, apolipoprotein A-I, and up to 22 mol % sphingomyelin. Sphingomyelins 32-45 lecithin-cholesterol acyltransferase Homo sapiens 71-75 8702592-5 1996 The reaction kinetics of LCAT with the rHDL particles revealed no significant change in the apparent Vmax but showed a concentration-dependent increase in slope of the reciprocal plots and in the apparent Km values with sphingomyelin content. Sphingomyelins 220-233 lecithin-cholesterol acyltransferase Homo sapiens 25-29 8702592-6 1996 The dissociation constant (Kd) for LCAT with these particles increased linearly with sphingomyelin content up to 22 mol %, changing in parallel with the apparent Km values. Sphingomyelins 85-98 lecithin-cholesterol acyltransferase Homo sapiens 35-39 8702592-8 1996 On the other hand, the proteoliposome substrates also had increased Kdvalues for LCAT at high sphingomyelin contents but compared with the rHDL particles had a 6-10-fold lower affinity for LCAT binding and exhibited kinetics consistent with competitive inhibition by sphingomyelin at the active site. Sphingomyelins 94-107 lecithin-cholesterol acyltransferase Homo sapiens 81-85 8702592-8 1996 On the other hand, the proteoliposome substrates also had increased Kdvalues for LCAT at high sphingomyelin contents but compared with the rHDL particles had a 6-10-fold lower affinity for LCAT binding and exhibited kinetics consistent with competitive inhibition by sphingomyelin at the active site. Sphingomyelins 267-280 lecithin-cholesterol acyltransferase Homo sapiens 81-85 8702592-9 1996 These results show conclusively that the dominant mechanism for the inhibition of LCAT activity with rHDL particles by sphingomyelin is the impaired binding of the enzyme to the interface. Sphingomyelins 119-132 lecithin-cholesterol acyltransferase Homo sapiens 82-86 8702592-2 1996 Sphingomyelin, an important constituent of HDL, may regulate the activity of LCAT at any of the key steps of the enzymatic reaction: binding of LCAT to the interface, activation by apo A-I, or inhibition at the catalytic site. Sphingomyelins 0-13 lecithin-cholesterol acyltransferase Homo sapiens 77-81 8702592-2 1996 Sphingomyelin, an important constituent of HDL, may regulate the activity of LCAT at any of the key steps of the enzymatic reaction: binding of LCAT to the interface, activation by apo A-I, or inhibition at the catalytic site. Sphingomyelins 0-13 lecithin-cholesterol acyltransferase Homo sapiens 144-148 8376375-6 1993 The lysolecithin acyltransferase and phospholipase reactions carried out by LCAT were also inhibited by SPH. Sphingomyelins 104-107 lecithin-cholesterol acyltransferase Homo sapiens 76-80 8376375-7 1993 Kinetic studies suggested that: 1) LCAT binds better to substrate vesicles which contain SPH; 2) SPH competes with PC in binding to the active site of the enzyme; and 3) SPH is a more powerful competitive inhibitor than a diether analog of PC. Sphingomyelins 89-92 lecithin-cholesterol acyltransferase Homo sapiens 35-39 8376375-7 1993 Kinetic studies suggested that: 1) LCAT binds better to substrate vesicles which contain SPH; 2) SPH competes with PC in binding to the active site of the enzyme; and 3) SPH is a more powerful competitive inhibitor than a diether analog of PC. Sphingomyelins 97-100 lecithin-cholesterol acyltransferase Homo sapiens 35-39 8376375-7 1993 Kinetic studies suggested that: 1) LCAT binds better to substrate vesicles which contain SPH; 2) SPH competes with PC in binding to the active site of the enzyme; and 3) SPH is a more powerful competitive inhibitor than a diether analog of PC. Sphingomyelins 97-100 lecithin-cholesterol acyltransferase Homo sapiens 35-39 8376375-8 1993 The ability of various lipoproteins to act as substrates for purified LCAT varied inversely with the SPH/PC ratio. Sphingomyelins 101-104 lecithin-cholesterol acyltransferase Homo sapiens 70-74