PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7654760-2 1995 We show that RPE cells secrete a specific set of proteins that includes retinol binding protein (RBP) and transthyretin (TTR), which are both involved in retinol transport in blood. Vitamin A 72-79 retinol binding protein 4 Bos taurus 97-100 9950616-2 1999 METHODS: [3H]all-trans retinol (ROL) was delivered to the basal surface of the cultured RPE by serum retinol-binding protein (RBP). Vitamin A 23-30 retinol binding protein 4 Bos taurus 126-129 10655150-11 2000 IRBP was also markedly superior to RBP and BSA in removing all- trans -retinol from RPE membranes. Vitamin A 59-78 retinol binding protein 4 Bos taurus 1-4 8227049-4 1993 The model of the retinoid-RBP complex is nearly identical to that of bovine retinol-RBP complex; the root mean square deviations between the alpha-carbons in the two proteins is 0.15 A. Vitamin A 76-83 retinol binding protein 4 Bos taurus 26-29 7961949-1 1994 The three-dimensional structures of complexes between bovine plasma retinol-binding protein (RBP) and three retinol analogs with different end groups (fenretinide, all-trans retinoic acid, and axerophthene) have been determined to 1.8-1.9-A resolution. Vitamin A 68-75 retinol binding protein 4 Bos taurus 93-96 7961949-2 1994 Their models are very similar to that of the bovine retinol.RBP complex: the root mean square deviations between equivalent alpha-carbons in the two proteins range from 0.17 to 0.24 A. Vitamin A 52-59 retinol binding protein 4 Bos taurus 60-63 8227049-4 1993 The model of the retinoid-RBP complex is nearly identical to that of bovine retinol-RBP complex; the root mean square deviations between the alpha-carbons in the two proteins is 0.15 A. Vitamin A 76-83 retinol binding protein 4 Bos taurus 84-87 1390692-4 1992 [3H]-all-trans-Retinol (ROL) was delivered to the basal surface of the cells by RBP. Vitamin A 5-22 retinol binding protein 4 Bos taurus 80-83 8373966-8 1993 Expression of RBP in expanding conceptuses, developing extraembryonic membranes, and sites of fetal-maternal attachment suggests that the extraembryonic membranes regulate retinol transport and availability within the conceptus. Vitamin A 172-179 retinol binding protein 4 Bos taurus 14-17 1493174-10 1992 The uterine RBP may play an important role in vitamin A transport between maternal tissues and developing embryos. Vitamin A 46-55 retinol binding protein 4 Bos taurus 12-15 2929489-4 1989 However, serum retinol-binding protein (RBP), which shares structural and conformational similarities with BLG, also enhanced retinol uptake. Vitamin A 15-22 retinol binding protein 4 Bos taurus 40-43 1547313-4 1992 The ultraviolet absorption spectrum and fluorescence excitation and emission spectra of the purified ovine placental RBP indicated the presence of bound retinol. Vitamin A 153-160 retinol binding protein 4 Bos taurus 117-120 1547313-8 1992 Transport, storage, and metabolism of retinol mediated by placental RBP may be essential for normal embryonic development during pregnancy. Vitamin A 38-45 retinol binding protein 4 Bos taurus 68-71 2249622-7 1990 These results suggested that bovine placental membranes secrete RBP into allantoic fluid and that placental RBP may play important roles in vitamin A metabolism in the developing embryo. Vitamin A 140-149 retinol binding protein 4 Bos taurus 108-111 2929489-5 1989 BLG, BLG-retinol, and RBP-retinol all inhibited the uptake of retinol from BLG-[3H]retinol in a concentration-dependent manner. Vitamin A 26-33 retinol binding protein 4 Bos taurus 22-25 3558401-0 1987 Vitamin A uptake from retinol-binding protein in a cell-free system from pigment epithelial cells of bovine retina. Vitamin A 0-9 retinol binding protein 4 Bos taurus 22-45 2739217-3 1989 The major, peak 1 having higher molecular weight corresponded to the retinol peak from human serum which consisted of RBP and prealbumin (PA). Vitamin A 69-76 retinol binding protein 4 Bos taurus 118-121 2739217-7 1989 These results suggested that, in cow, retinol was transported by the complex of RBP and another protein, presumably PA, but in calf, mainly by RBP alone. Vitamin A 38-45 retinol binding protein 4 Bos taurus 80-83 2739217-7 1989 These results suggested that, in cow, retinol was transported by the complex of RBP and another protein, presumably PA, but in calf, mainly by RBP alone. Vitamin A 38-45 retinol binding protein 4 Bos taurus 143-146 3558401-1 1987 Retinol transfer from plasma retinol-binding protein to cytoplasmic retinol-binding protein with retinyl-ester formation as the intermediate step. Vitamin A 0-7 retinol binding protein 4 Bos taurus 29-52 3558401-2 1987 We have investigated the steps by which retinol, released from plasma retinol-binding protein (RBP), enters the cells and is accumulated for the most part as a retinyl-ester, only a small fraction of it being present as a complex with cytoplasmic retinol-binding protein (CRBP). Vitamin A 40-47 retinol binding protein 4 Bos taurus 70-93 3558401-2 1987 We have investigated the steps by which retinol, released from plasma retinol-binding protein (RBP), enters the cells and is accumulated for the most part as a retinyl-ester, only a small fraction of it being present as a complex with cytoplasmic retinol-binding protein (CRBP). Vitamin A 40-47 retinol binding protein 4 Bos taurus 95-98 3558401-3 1987 For this purpose, we have developed a cell-free system composed of plasma membrane-enriched fractions from bovine retinal pigment epithelium which selectively incorporates exogenous vitamin A when presented as a retinol-RBP complex. Vitamin A 182-191 retinol binding protein 4 Bos taurus 220-223 3558401-4 1987 Upon incubation in the presence of [3H]retinol-RBP, isolated plasma membrane fractions take up and esterify retinol. Vitamin A 39-46 retinol binding protein 4 Bos taurus 47-50 3558401-4 1987 Upon incubation in the presence of [3H]retinol-RBP, isolated plasma membrane fractions take up and esterify retinol. Vitamin A 108-115 retinol binding protein 4 Bos taurus 47-50 943148-1 1976 By means of autoradiographic techniques the specific plasma carrier of retinol, namely retinol binding protein (RBP) in a radioactive form (retinol-125I.RBP), bound specifically in vivo to the choroidal surface of intact, isolated bovine pigment epithelial cells. Vitamin A 71-78 retinol binding protein 4 Bos taurus 87-110 943148-1 1976 By means of autoradiographic techniques the specific plasma carrier of retinol, namely retinol binding protein (RBP) in a radioactive form (retinol-125I.RBP), bound specifically in vivo to the choroidal surface of intact, isolated bovine pigment epithelial cells. Vitamin A 71-78 retinol binding protein 4 Bos taurus 112-115 943148-1 1976 By means of autoradiographic techniques the specific plasma carrier of retinol, namely retinol binding protein (RBP) in a radioactive form (retinol-125I.RBP), bound specifically in vivo to the choroidal surface of intact, isolated bovine pigment epithelial cells. Vitamin A 71-78 retinol binding protein 4 Bos taurus 153-156 943148-1 1976 By means of autoradiographic techniques the specific plasma carrier of retinol, namely retinol binding protein (RBP) in a radioactive form (retinol-125I.RBP), bound specifically in vivo to the choroidal surface of intact, isolated bovine pigment epithelial cells. Vitamin A 87-94 retinol binding protein 4 Bos taurus 112-115 943148-1 1976 By means of autoradiographic techniques the specific plasma carrier of retinol, namely retinol binding protein (RBP) in a radioactive form (retinol-125I.RBP), bound specifically in vivo to the choroidal surface of intact, isolated bovine pigment epithelial cells. Vitamin A 87-94 retinol binding protein 4 Bos taurus 153-156 943148-2 1976 The retinol-125I.RBP did not bind to the retinal surface of the pigment epithelial cells nor did not bind to photoreceptors. Vitamin A 4-11 retinol binding protein 4 Bos taurus 17-20 943148-4 1976 Retinol metabolism might be deranged in some diseases through a defect in the pigment epithelial receptor for RBP. Vitamin A 0-7 retinol binding protein 4 Bos taurus 110-113 1171864-2 1975 Purified bovine retinol-RBP formed tight complexes with purified human and chicken prealbumin in physiological ionic strength buffers as judged by gel filtration chromatography, hyperchromic effect on the absorption spectrum of retinol-RBP, and changes in the circular dichroism spectrum. Vitamin A 16-23 retinol binding protein 4 Bos taurus 24-27 1171864-2 1975 Purified bovine retinol-RBP formed tight complexes with purified human and chicken prealbumin in physiological ionic strength buffers as judged by gel filtration chromatography, hyperchromic effect on the absorption spectrum of retinol-RBP, and changes in the circular dichroism spectrum. Vitamin A 228-235 retinol binding protein 4 Bos taurus 24-27 1171864-4 1975 It was concluded from this series of experiments that bovine serum lacks a protein with the binding properties of prealbumin and that bovine retinol-RBP has the normal potential binding to human, chicken, and presumably other prealbumins. Vitamin A 141-148 retinol binding protein 4 Bos taurus 149-152 1171864-5 1975 Bovine retinol-RBP has a molecular weight, amino acid composition, absorption, and fluorescence spectra which are indistinguishable from that of human retinol-RBP, although the magnitude of the optical rotatory strength of the induced circular dichroism signal at 330 nm was 50% larger in the bovine than in the human material (1.65 and 1.1 Debye-Bohr magnetons, respectively). Vitamin A 7-14 retinol binding protein 4 Bos taurus 15-18 1171864-5 1975 Bovine retinol-RBP has a molecular weight, amino acid composition, absorption, and fluorescence spectra which are indistinguishable from that of human retinol-RBP, although the magnitude of the optical rotatory strength of the induced circular dichroism signal at 330 nm was 50% larger in the bovine than in the human material (1.65 and 1.1 Debye-Bohr magnetons, respectively). Vitamin A 151-158 retinol binding protein 4 Bos taurus 15-18 1171864-6 1975 About 12 liters of bovine and human urine were concentrated by pressure dialysis and a search was made for retinol-RBP using gel filtration and ion exchange chromatography. Vitamin A 107-114 retinol binding protein 4 Bos taurus 115-118 31147589-1 2019 Retinol binding protein 4 (RBP4) facilitates the transport of retinol in the body but is also an adipokine and fatty acid transporter. Vitamin A 62-69 retinol binding protein 4 Bos taurus 0-25 1092676-7 1975 The specific binding of both human and bovine retinol-125I-RBP was a linear function of the number of binding sites (number of cells) and was saturable with respect to retinol-125I-RBP. Vitamin A 46-53 retinol binding protein 4 Bos taurus 59-62 1092676-7 1975 The specific binding of both human and bovine retinol-125I-RBP was a linear function of the number of binding sites (number of cells) and was saturable with respect to retinol-125I-RBP. Vitamin A 46-53 retinol binding protein 4 Bos taurus 181-184 1092676-7 1975 The specific binding of both human and bovine retinol-125I-RBP was a linear function of the number of binding sites (number of cells) and was saturable with respect to retinol-125I-RBP. Vitamin A 168-175 retinol binding protein 4 Bos taurus 59-62 1092676-7 1975 The specific binding of both human and bovine retinol-125I-RBP was a linear function of the number of binding sites (number of cells) and was saturable with respect to retinol-125I-RBP. Vitamin A 168-175 retinol binding protein 4 Bos taurus 181-184 1092676-8 1975 Bound iodinated retinol-RBP was rapidly displaced by the addition of unlabeled retinol-RBP, indicating that the specific binding process was a surface phenomenon and was not due to endocytosis. Vitamin A 16-23 retinol binding protein 4 Bos taurus 24-27 1092676-8 1975 Bound iodinated retinol-RBP was rapidly displaced by the addition of unlabeled retinol-RBP, indicating that the specific binding process was a surface phenomenon and was not due to endocytosis. Vitamin A 16-23 retinol binding protein 4 Bos taurus 87-90 1092676-8 1975 Bound iodinated retinol-RBP was rapidly displaced by the addition of unlabeled retinol-RBP, indicating that the specific binding process was a surface phenomenon and was not due to endocytosis. Vitamin A 79-86 retinol binding protein 4 Bos taurus 24-27 1092676-8 1975 Bound iodinated retinol-RBP was rapidly displaced by the addition of unlabeled retinol-RBP, indicating that the specific binding process was a surface phenomenon and was not due to endocytosis. Vitamin A 79-86 retinol binding protein 4 Bos taurus 87-90 1092676-10 1975 The dissociation constant for the binding between retinol-125I-RBP and pigment epithelium receptor was estimated to be about 5 times 10-minus 12 M. Addition of human prealbumin (thyroxine-binding prealbumin) did not affect the binding of either human or bovine retinol-125I-RBP to pigment epithelium cells. Vitamin A 50-57 retinol binding protein 4 Bos taurus 63-66 1092676-10 1975 The dissociation constant for the binding between retinol-125I-RBP and pigment epithelium receptor was estimated to be about 5 times 10-minus 12 M. Addition of human prealbumin (thyroxine-binding prealbumin) did not affect the binding of either human or bovine retinol-125I-RBP to pigment epithelium cells. Vitamin A 261-268 retinol binding protein 4 Bos taurus 63-66 1092676-11 1975 Retinol-125I-RBP did not bind specifically to isolated bovine rod photoreceptor outer segments. Vitamin A 0-7 retinol binding protein 4 Bos taurus 13-16 1092676-12 1975 Human apo-RBP was less effective in displacing bound retinol-125I-RBP than either native or reconstituted human retinol-RBP. Vitamin A 53-60 retinol binding protein 4 Bos taurus 66-69 1092676-13 1975 These results suggest a mechanism whereby, after delivering its retinol to the cell, apo-RBP is displaced from the specific receptor on pigment epithelium cell by another retinol-RBP molecule. Vitamin A 64-71 retinol binding protein 4 Bos taurus 89-92 1092676-13 1975 These results suggest a mechanism whereby, after delivering its retinol to the cell, apo-RBP is displaced from the specific receptor on pigment epithelium cell by another retinol-RBP molecule. Vitamin A 171-178 retinol binding protein 4 Bos taurus 89-92 1092676-13 1975 These results suggest a mechanism whereby, after delivering its retinol to the cell, apo-RBP is displaced from the specific receptor on pigment epithelium cell by another retinol-RBP molecule. Vitamin A 171-178 retinol binding protein 4 Bos taurus 179-182 1092676-14 1975 This postulated mechanism makes it possible to control the delivery of retinol to the target cell by the relative plasma concentrations of apo- and retinol-RBP and their relative affinities for the specific receptor binding site. Vitamin A 71-78 retinol binding protein 4 Bos taurus 156-159 31147589-1 2019 Retinol binding protein 4 (RBP4) facilitates the transport of retinol in the body but is also an adipokine and fatty acid transporter. Vitamin A 62-69 retinol binding protein 4 Bos taurus 27-31 19785912-9 2010 These results suggest that RBP4 and retinol levels are independently regulated under physiological and pathophysiological conditions and that RBP4, like retinol, is transferred from maternal stores to calves through colostrum. Vitamin A 153-160 retinol binding protein 4 Bos taurus 142-146 23040032-1 2012 Retinol-binding protein (RBP) is the main transport system for retinol in circulation, is a relatively small protein with one binding site for retinol in the all-trans form, and is bound to transthyretin. Vitamin A 63-70 retinol binding protein 4 Bos taurus 0-23 23040032-1 2012 Retinol-binding protein (RBP) is the main transport system for retinol in circulation, is a relatively small protein with one binding site for retinol in the all-trans form, and is bound to transthyretin. Vitamin A 63-70 retinol binding protein 4 Bos taurus 25-28 23040032-1 2012 Retinol-binding protein (RBP) is the main transport system for retinol in circulation, is a relatively small protein with one binding site for retinol in the all-trans form, and is bound to transthyretin. Vitamin A 143-150 retinol binding protein 4 Bos taurus 0-23 23040032-1 2012 Retinol-binding protein (RBP) is the main transport system for retinol in circulation, is a relatively small protein with one binding site for retinol in the all-trans form, and is bound to transthyretin. Vitamin A 143-150 retinol binding protein 4 Bos taurus 25-28 19785912-1 2010 Retinol-binding protein 4 (RBP4) is a plasma protein involved in retinol transportation, and recent evidence in rodents suggests that RBP4 is also a metabolic regulator that modifies insulin sensitivity. Vitamin A 65-72 retinol binding protein 4 Bos taurus 0-25 19785912-1 2010 Retinol-binding protein 4 (RBP4) is a plasma protein involved in retinol transportation, and recent evidence in rodents suggests that RBP4 is also a metabolic regulator that modifies insulin sensitivity. Vitamin A 65-72 retinol binding protein 4 Bos taurus 27-31 12787682-3 2003 RBP is a plasma transport protein which delivers specifically retinol from its store sites to target cells. Vitamin A 62-69 retinol binding protein 4 Bos taurus 0-3 17255476-0 2007 A membrane receptor for retinol binding protein mediates cellular uptake of vitamin A. Vitamin A 76-85 retinol binding protein 4 Bos taurus 24-47 17255476-2 2007 It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. Vitamin A 117-126 retinol binding protein 4 Bos taurus 49-72 17255476-2 2007 It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. Vitamin A 117-126 retinol binding protein 4 Bos taurus 74-77 17255476-2 2007 It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. Vitamin A 117-126 retinol binding protein 4 Bos taurus 167-170 17255476-2 2007 It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. Vitamin A 157-166 retinol binding protein 4 Bos taurus 74-77 17255476-2 2007 It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. Vitamin A 157-166 retinol binding protein 4 Bos taurus 167-170 17255476-4 2007 STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. Vitamin A 53-62 retinol binding protein 4 Bos taurus 98-101 17255476-4 2007 STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. Vitamin A 88-97 retinol binding protein 4 Bos taurus 98-101 17255476-6 2007 The RBP receptor represents a major physiological mediator of cellular vitamin A uptake. Vitamin A 71-80 retinol binding protein 4 Bos taurus 4-7 12787682-9 2003 All these changes, which reveal a substantially lowered conformational stability of RBP, presumably occur at the initial stages of the acidic denaturation of RBP and are possibly associated with a facilitated release of the retinol molecule from its carrier protein. Vitamin A 224-231 retinol binding protein 4 Bos taurus 158-161 12787682-7 2003 At this pH, most significant are the alteration of the arrangement of salt bridges and of the network of water molecules/H-bonds that participates in the retinol-RBP interaction, an appreciable increase of the volume of the beta-barrel cavity, a considerably higher degree of mobility of the RBP-bound ligand and of several protein regions and the disorder of a large number of solvent molecules that are ordered at neutral pH. Vitamin A 154-161 retinol binding protein 4 Bos taurus 162-165 12787682-9 2003 All these changes, which reveal a substantially lowered conformational stability of RBP, presumably occur at the initial stages of the acidic denaturation of RBP and are possibly associated with a facilitated release of the retinol molecule from its carrier protein. Vitamin A 224-231 retinol binding protein 4 Bos taurus 84-87 12548658-2 2003 Retinol is transported systemically and intercellularly by retinol-binding protein (RBP). Vitamin A 0-7 retinol binding protein 4 Bos taurus 59-82 12548658-2 2003 Retinol is transported systemically and intercellularly by retinol-binding protein (RBP). Vitamin A 0-7 retinol binding protein 4 Bos taurus 84-87