PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12832282-5 2004 Serum-free, exogenous ATRA-free medium conditioned by LICs rich in retinol storage granules caused a 10-fold greater increase of CRBP-I mRNA in PMVCs than media conditioned by LICs with few retinol storage granules. Vitamin A 67-74 retinol binding protein 1 Rattus norvegicus 129-135 15950969-5 2005 We found that combinations of Crbp, eRoldh, Aldh1a2 or Aldh1a3, and Crabp2 were present in all vitamin A sensitive tissues examined. Vitamin A 95-104 retinol binding protein 1 Rattus norvegicus 30-34 12500946-4 2002 This study aimed to investigate in PAV-1 and in primary HSC (i) the incorporation of retinol and its esterification, (ii) the cellular retinol-binding protein (CRBP) content, (iii) the acid retinyl ester hydrolase activity (aREH), (iv) the thermal susceptibility and (v) the lipid composition of the membranes, which may play a crucial role in retinol transport across cellular membrane. Vitamin A 135-142 retinol binding protein 1 Rattus norvegicus 160-164 14642897-9 2004 Our results provide evidence of a functional retinol esterifying enzyme in cultured RCS RPE cells and suggest that CRBP-I could play a role in the uptake and esterification of ROL in the RPE cells. Vitamin A 45-52 retinol binding protein 1 Rattus norvegicus 115-121 12850148-1 2003 Cellular retinol-binding protein I (CRBP I) and cellular retinol-binding protein II (CRBP II) are closely homologous proteins that play distinct roles in the maintenance of vitamin A homeostasis. Vitamin A 173-182 retinol binding protein 1 Rattus norvegicus 0-34 12850148-1 2003 Cellular retinol-binding protein I (CRBP I) and cellular retinol-binding protein II (CRBP II) are closely homologous proteins that play distinct roles in the maintenance of vitamin A homeostasis. Vitamin A 173-182 retinol binding protein 1 Rattus norvegicus 36-42 12850148-4 2003 Intraligand NOE cross-peaks were detected for the hydroxyl proton in the NOESY spectrum of CRBP I-bound retinol, but not for CRBP II-bound retinol, indicating that the conformational dynamics of retinol binding are different for these two proteins. Vitamin A 104-111 retinol binding protein 1 Rattus norvegicus 91-97 12850148-7 2003 Thus binding of retinol markedly reduced conformational flexibility in both CRBP I and CRBP II on the micro- to millisecond timescale. Vitamin A 16-23 retinol binding protein 1 Rattus norvegicus 76-82 12500946-6 2002 Retinol pre-treatment doubled this esterification rate (10.7%) and the CRBP content in PAV-1. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 71-75 7499345-7 1995 RoDH(II) recognized the physiological form of retinol as substrate, CRBP, with a Km of 2 mM. Vitamin A 46-53 retinol binding protein 1 Rattus norvegicus 68-72 11032179-6 2000 Additionally, cellular retinol binding protein one (CRBPI) null lungs are more sensitive than wild type lungs to the pan-RAR antagonist-induced stimulation of branching. Vitamin A 23-30 retinol binding protein 1 Rattus norvegicus 52-57 10828080-10 2000 Addition of retinol (10(-8)-10(-5) m) or all-trans-retinoic acid (10(-10)-10(-6) m) rapidly up-regulates CRBP expression. Vitamin A 12-19 retinol binding protein 1 Rattus norvegicus 105-109 7588278-0 1995 Gene expression of retinoic acid receptors, retinoid-X receptors, and cellular retinol-binding protein I in bone and its regulation by vitamin A. Vitamin A 135-144 retinol binding protein 1 Rattus norvegicus 44-104 7588278-4 1995 These results indicated that in bone, the actions of vitamin A are exerted through these nuclear receptors by regulating target gene expression, and through CRBP-I by modulating the intracellular transport of vitamin A. Vitamin A 53-62 retinol binding protein 1 Rattus norvegicus 157-163 7588278-4 1995 These results indicated that in bone, the actions of vitamin A are exerted through these nuclear receptors by regulating target gene expression, and through CRBP-I by modulating the intracellular transport of vitamin A. Vitamin A 209-218 retinol binding protein 1 Rattus norvegicus 157-163 7588278-5 1995 Moreover, using rats of various retinoid status, we investigated whether the expression of target genes for vitamin A (RAR beta and CRBP-I) is regulated by retinoic acid (RA) in the adult rat tibia. Vitamin A 108-117 retinol binding protein 1 Rattus norvegicus 132-138 11165018-3 2001 Interaction with cellular retinol-binding protein (CRBP), the major physiological form of retinol, led to the identification and cDNA cloning of RoDH1. Vitamin A 26-33 retinol binding protein 1 Rattus norvegicus 51-55 11165018-12 2001 The ability of some these SDRs to access retinol bound with CRBP provides specificity in retinoid metabolism and allows retinoic acid biosynthesis and retinol esterification to continue, as CRBP protects retinol from the general cellular milieu. Vitamin A 41-48 retinol binding protein 1 Rattus norvegicus 60-64 11165018-12 2001 The ability of some these SDRs to access retinol bound with CRBP provides specificity in retinoid metabolism and allows retinoic acid biosynthesis and retinol esterification to continue, as CRBP protects retinol from the general cellular milieu. Vitamin A 41-48 retinol binding protein 1 Rattus norvegicus 190-194 11165018-12 2001 The ability of some these SDRs to access retinol bound with CRBP provides specificity in retinoid metabolism and allows retinoic acid biosynthesis and retinol esterification to continue, as CRBP protects retinol from the general cellular milieu. Vitamin A 151-158 retinol binding protein 1 Rattus norvegicus 60-64 11165018-12 2001 The ability of some these SDRs to access retinol bound with CRBP provides specificity in retinoid metabolism and allows retinoic acid biosynthesis and retinol esterification to continue, as CRBP protects retinol from the general cellular milieu. Vitamin A 151-158 retinol binding protein 1 Rattus norvegicus 190-194 11165018-12 2001 The ability of some these SDRs to access retinol bound with CRBP provides specificity in retinoid metabolism and allows retinoic acid biosynthesis and retinol esterification to continue, as CRBP protects retinol from the general cellular milieu. Vitamin A 151-158 retinol binding protein 1 Rattus norvegicus 60-64 11165018-12 2001 The ability of some these SDRs to access retinol bound with CRBP provides specificity in retinoid metabolism and allows retinoic acid biosynthesis and retinol esterification to continue, as CRBP protects retinol from the general cellular milieu. Vitamin A 151-158 retinol binding protein 1 Rattus norvegicus 190-194 10801930-2 2000 The objective of this study was to investigate whether age and/or VA status are factors for the hepatic expression of cellular retinol-binding protein (CRBP), the esterification of retinol by lecithin:retinol acyltransferase (LRAT) and the accumulation of VA and lipids in liver. Vitamin A 127-134 retinol binding protein 1 Rattus norvegicus 152-156 10801930-2 2000 The objective of this study was to investigate whether age and/or VA status are factors for the hepatic expression of cellular retinol-binding protein (CRBP), the esterification of retinol by lecithin:retinol acyltransferase (LRAT) and the accumulation of VA and lipids in liver. Vitamin A 66-68 retinol binding protein 1 Rattus norvegicus 118-150 10801930-2 2000 The objective of this study was to investigate whether age and/or VA status are factors for the hepatic expression of cellular retinol-binding protein (CRBP), the esterification of retinol by lecithin:retinol acyltransferase (LRAT) and the accumulation of VA and lipids in liver. Vitamin A 66-68 retinol binding protein 1 Rattus norvegicus 152-156 9013704-7 1997 When CRBP expression was repressed by elevating intracellular cyclic AMP levels, the ability of retinol, but not retinoic acid, to block estrogen-induced changes in keratin expression was severely compromised. Vitamin A 96-103 retinol binding protein 1 Rattus norvegicus 5-9 9013704-8 1997 These results support a critical role for CRBP in cervical cell responsiveness to circulating retinoids (primarily retinol). Vitamin A 115-122 retinol binding protein 1 Rattus norvegicus 42-46 7706939-8 1995 In summary, these studies indicate that CRBP gene expression is regulated by retinoic acid, dexamethasone, and triiodothyronine; thus suggesting that retinol uptake, intracellular transport, and metabolism are dynamically regulated in adipocytes. Vitamin A 150-157 retinol binding protein 1 Rattus norvegicus 40-44 7766612-4 1995 Integral and peripheral RoDH catalyzed retinal synthesis from all-trans-retinol bound to cellular retinol-binding protein, type I (CRBP), with similar Km values of 0.6 and 0.4 microM, respectively. Vitamin A 72-79 retinol binding protein 1 Rattus norvegicus 131-135 8086427-5 1994 In contrast, only a single absorption was observed for bound ligands complexed with rat CRBP over this temperature range, suggesting that the conformational dynamics of retinol binding are different for these two closely homologous proteins. Vitamin A 169-176 retinol binding protein 1 Rattus norvegicus 88-92 7516425-1 1993 The effect of dietary proteins and vitamin A status on the gene expression of cellular retinol-binding protein I (CRBP I) was studied in the rat liver. Vitamin A 35-44 retinol binding protein 1 Rattus norvegicus 78-112 7516425-1 1993 The effect of dietary proteins and vitamin A status on the gene expression of cellular retinol-binding protein I (CRBP I) was studied in the rat liver. Vitamin A 35-44 retinol binding protein 1 Rattus norvegicus 114-120 7516425-3 1993 Though vitamin A status is known to positively regulate the gene expression of CRBP I in the extrahepatic tissues, in the present study we observed that the amount of the CRBP I transcript in liver was neither reduced by vitamin A-deficiency, nor affected by replenishment with an excess dose of all-trans retinoic acid. Vitamin A 7-16 retinol binding protein 1 Rattus norvegicus 79-85 7516425-3 1993 Though vitamin A status is known to positively regulate the gene expression of CRBP I in the extrahepatic tissues, in the present study we observed that the amount of the CRBP I transcript in liver was neither reduced by vitamin A-deficiency, nor affected by replenishment with an excess dose of all-trans retinoic acid. Vitamin A 7-16 retinol binding protein 1 Rattus norvegicus 171-177 7516425-5 1993 However, when the rats were fed on the diets that differed in dietary proteins, the gene expression of CRBP I in liver was enhanced by higher quality and quantity of dietary proteins, though no effect of dietary proteins was observed upon the hepatic contents of retinol. Vitamin A 263-270 retinol binding protein 1 Rattus norvegicus 103-109 7516425-6 1993 The concentrations of serum retinol were almost proportional to the mRNA levels of CRBP I. Vitamin A 28-35 retinol binding protein 1 Rattus norvegicus 83-89 7516425-9 1993 Thus, it is likely that in the light of the function of CRBP I on cellular transport and metabolism of retinol, dietary proteins may affect the actions of vitamin A in the extrahepatic tissues through changing the amounts of CRBP I in liver. Vitamin A 103-110 retinol binding protein 1 Rattus norvegicus 56-62 7516425-9 1993 Thus, it is likely that in the light of the function of CRBP I on cellular transport and metabolism of retinol, dietary proteins may affect the actions of vitamin A in the extrahepatic tissues through changing the amounts of CRBP I in liver. Vitamin A 155-164 retinol binding protein 1 Rattus norvegicus 225-231 8286593-2 1993 Cellular retinol-binding protein (CRBP) and lecithin-retinol acyltransferase (LRAT) are two proteins found in Sertoli cells that are known to be involved in vitamin A trafficking. Vitamin A 157-166 retinol binding protein 1 Rattus norvegicus 0-32 8286593-2 1993 Cellular retinol-binding protein (CRBP) and lecithin-retinol acyltransferase (LRAT) are two proteins found in Sertoli cells that are known to be involved in vitamin A trafficking. Vitamin A 157-166 retinol binding protein 1 Rattus norvegicus 34-38 8439537-7 1993 The uptake of [3H]retinol from RBP was also compared to the uptake of retinol from cellular retinol-binding protein (CRBP) and lactoglobulin. Vitamin A 70-77 retinol binding protein 1 Rattus norvegicus 83-115 8371067-5 1993 The activity of LRAT was assayed both by monitoring the esterification of retinol bound to the cellular retinol-binding protein (CRBP) and of solvent-dispersed retinol. Vitamin A 74-81 retinol binding protein 1 Rattus norvegicus 95-127 8371067-5 1993 The activity of LRAT was assayed both by monitoring the esterification of retinol bound to the cellular retinol-binding protein (CRBP) and of solvent-dispersed retinol. Vitamin A 74-81 retinol binding protein 1 Rattus norvegicus 129-133 8463314-1 1993 A comparative study of the interactions of rat cellular retinol-binding protein (CRBP) and cellular retinol-binding protein II (CRBP II) with a number of synthetic phenyl-substituted analogs of all-trans-retinol was performed using fluorescence and nuclear magnetic resonance analysis. Vitamin A 198-211 retinol binding protein 1 Rattus norvegicus 47-79 8395395-6 1993 A specific induction of the cellular retinol-binding protein CRBP I mRNA was observed following retinoid treatment in one of the two FRIC lines examined (FRIC B) and in organ culture. Vitamin A 37-44 retinol binding protein 1 Rattus norvegicus 61-67 8439537-7 1993 The uptake of [3H]retinol from RBP was also compared to the uptake of retinol from cellular retinol-binding protein (CRBP) and lactoglobulin. Vitamin A 70-77 retinol binding protein 1 Rattus norvegicus 117-121 8439537-8 1993 Uptake characteristics of [3H]retinol from CRBP and lactoglobulin were similar to that of [3H]retinol from RBP. Vitamin A 30-37 retinol binding protein 1 Rattus norvegicus 43-47 1527087-2 1992 An NAD-dependent rat liver cytosolic dehydrogenase accepted as substrate retinal generated in situ by microsomes from retinol bound to excess CRBP (cellular retinol binding protein, type I). Vitamin A 118-125 retinol binding protein 1 Rattus norvegicus 142-146 1527087-2 1992 An NAD-dependent rat liver cytosolic dehydrogenase accepted as substrate retinal generated in situ by microsomes from retinol bound to excess CRBP (cellular retinol binding protein, type I). Vitamin A 118-125 retinol binding protein 1 Rattus norvegicus 148-180 2054343-6 1991 The kon"s for retinol associating with CRBP and with RBP were found to be 4.4 x 10(7) and 0.9 x 10(7) M-1 min-1, respectively. Vitamin A 14-21 retinol binding protein 1 Rattus norvegicus 39-43 1898045-2 1991 Retinol bound to cellular retinol-binding protein (CRBP) or dispersed in solvent was esterified in a fatty acyl CoA-independent, PMSF-sensitive reaction, consistent with lecithin:retinol acyltransferase (LRAT) activity. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 17-49 1898045-2 1991 Retinol bound to cellular retinol-binding protein (CRBP) or dispersed in solvent was esterified in a fatty acyl CoA-independent, PMSF-sensitive reaction, consistent with lecithin:retinol acyltransferase (LRAT) activity. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 51-55 1898045-5 1991 Retinol bound to CRBP was not a good substrate for this reaction. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 17-21 1898045-9 1991 These data suggest that retinol esterification is regulated via different mechanisms in liver and mammary gland and support a specific role for CRBP in the liver. Vitamin A 24-31 retinol binding protein 1 Rattus norvegicus 144-148 1855468-1 1991 Cellular retinol-binding protein (CRBP) is a potential mediator of vitamin A action. Vitamin A 67-76 retinol binding protein 1 Rattus norvegicus 0-32 1855468-1 1991 Cellular retinol-binding protein (CRBP) is a potential mediator of vitamin A action. Vitamin A 67-76 retinol binding protein 1 Rattus norvegicus 34-38 1855468-7 1991 We conclude that CRBP gene expression can be modulated by both retinoic acid and dexamethasone in the vitamin A-sufficient animal. Vitamin A 102-111 retinol binding protein 1 Rattus norvegicus 17-21 2054343-0 1991 Interactions of retinol with binding proteins: studies with rat cellular retinol-binding protein and with rat retinol-binding protein. Vitamin A 16-23 retinol binding protein 1 Rattus norvegicus 64-96 2054343-1 1991 The interactions of retinol with rat cellular retinol-binding protein (CRBP) and with rat serum retinol-binding protein (RBP) were studied. Vitamin A 20-27 retinol binding protein 1 Rattus norvegicus 71-75 2054343-4 1991 It was found that although the equilibrium dissociation constants of the two retinol-protein complexes were similar, retinol interacted with CRBP 3-5-fold faster than with RBP; the rate constants for dissociation of retinol from CRBP and from RBP (koff) were 0.57 and 0.18 min-1, respectively. Vitamin A 117-124 retinol binding protein 1 Rattus norvegicus 141-145 2054343-4 1991 It was found that although the equilibrium dissociation constants of the two retinol-protein complexes were similar, retinol interacted with CRBP 3-5-fold faster than with RBP; the rate constants for dissociation of retinol from CRBP and from RBP (koff) were 0.57 and 0.18 min-1, respectively. Vitamin A 117-124 retinol binding protein 1 Rattus norvegicus 141-145 2054343-8 1991 The data indicate further that the distribution of retinol between RBP in blood and CRBP in cytosol is at equilibrium and that intracellular levels of retinol are regulated by the levels of CRBP. Vitamin A 151-158 retinol binding protein 1 Rattus norvegicus 190-194 2611253-11 1989 Furthermore, retinol bound to CRBP, a protein known to be present in Sertoli cells, was not an effective substrate for testicular ARAT. Vitamin A 13-20 retinol binding protein 1 Rattus norvegicus 30-34 2059629-9 1991 Retinal formation from holo-CRBP displayed typical Michaelis-Menten kinetics with a Km about 1.6 microM, less than the physiological retinal concentration of 4-10 microM in the livers of rats fed diets with recommended vitamin A levels. Vitamin A 219-228 retinol binding protein 1 Rattus norvegicus 28-32 1999437-4 1991 In order to determine amino acid residues in CRBP which may be important for the binding of all-trans-retinol, comparative model-building studies were performed in which strong sequence similarities were identified between CRBP and several other binding proteins. Vitamin A 95-109 retinol binding protein 1 Rattus norvegicus 45-49 1999437-4 1991 In order to determine amino acid residues in CRBP which may be important for the binding of all-trans-retinol, comparative model-building studies were performed in which strong sequence similarities were identified between CRBP and several other binding proteins. Vitamin A 95-109 retinol binding protein 1 Rattus norvegicus 223-227 1995621-5 1991 Retinol complexed to CRBPII is readily transferred to CRBP, whereas retinol complexed to CRBP is not readily transferred to CRBPII. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 21-25 1995621-5 1991 Retinol complexed to CRBPII is readily transferred to CRBP, whereas retinol complexed to CRBP is not readily transferred to CRBPII. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 54-58 1995621-8 1991 Results from competitive binding studies with retinol and retinal indicated that there is a much larger difference between the affinities of CRBP for retinol and retinal than between the affinities of CRBPII for these two ligands. Vitamin A 46-53 retinol binding protein 1 Rattus norvegicus 141-145 1995621-8 1991 Results from competitive binding studies with retinol and retinal indicated that there is a much larger difference between the affinities of CRBP for retinol and retinal than between the affinities of CRBPII for these two ligands. Vitamin A 150-157 retinol binding protein 1 Rattus norvegicus 141-145 2380630-1 1990 A study was conducted to determine the levels of cellular retinol-binding protein (CRBP) mRNA and protein in various tissues of the rat, to explore relationship between CRBP mRNA and protein levels in different tissues, and to examine the effects of changes in retinol nutritional status on the tissue distribution and levels of CRBP mRNA. Vitamin A 58-65 retinol binding protein 1 Rattus norvegicus 83-87 2380630-9 1990 After oral repletion with retinol (4-18 h earlier), CRBP mRNA levels for these latter four tissues were found to have risen to control or near-control levels. Vitamin A 26-33 retinol binding protein 1 Rattus norvegicus 52-56 2380630-10 1990 The suggestion is raised that retinol repletion may have directly induced the expression of the CRBP gene in these particular tissues. Vitamin A 30-37 retinol binding protein 1 Rattus norvegicus 96-100 2059629-7 1991 Fourth, the rate of retinal synthesis increased with increases in the concentration of holo-CRBP as a fixed concentration of unbound retinol was maintained. Vitamin A 133-140 retinol binding protein 1 Rattus norvegicus 92-96 2001700-1 1991 Two different metabolic alterations in vitamin A status are known to cause changes in the amount of circulating retinol-binding protein (RBP) and cellular retinol-binding protein (CRBP) in experimental animals; namely vitamin A deficiency, characterized by depleted retinol-liver stores and hypervitaminosis A, characterized by hepatic accumulation of retinyl esters. Vitamin A 39-48 retinol binding protein 1 Rattus norvegicus 180-184 2001700-5 1991 We have found a threefold decrease in the hepatic level of CRBP mRNA in vitamin-A-deficient animals, while the RBP mRNA is not affected by this nutritional deprivation. Vitamin A 72-81 retinol binding protein 1 Rattus norvegicus 59-63 2001700-8 1991 The results are discussed in terms of retinol-dependent stabilization of the mRNA coding for CRBP. Vitamin A 38-45 retinol binding protein 1 Rattus norvegicus 93-97 2555241-9 1989 Considered together, the presence of CRBP and CRABP in a beta-cell line and the increase in KCl-induced insulin release by retinol and retinoic acid are consistent with the idea that retinol has a functional role in insulin secretion and suggest a potential mechanism of action at the beta-cell level similar to that observed in other retinoid-responsive cells. Vitamin A 183-190 retinol binding protein 1 Rattus norvegicus 37-41 3198596-6 1988 The major products were retinyl palmitate/oleate and retinyl stearate in a ratio of approximately 2 to 1 over a range of [3H]retinol-CRBP concentrations from 1 to 8 microM. Vitamin A 125-132 retinol binding protein 1 Rattus norvegicus 133-137 3198596-1 1988 We have investigated the esterification by liver membranes of retinol bound to cellular retinol-binding protein (CRBP). Vitamin A 62-69 retinol binding protein 1 Rattus norvegicus 113-117 3198596-2 1988 When CRBP carrying [3H]retinol as its ligand was purified from rat liver cytosol and incubated with rat liver microsomes, a significant fraction of the [3H]retinol was converted to [3H]retinyl ester. Vitamin A 23-30 retinol binding protein 1 Rattus norvegicus 5-9 3198596-3 1988 Esterification of the CRBP-bound [3H]retinol, which was maximal at pH 6-7, did not require the addition of an exogenous fatty acyl group. Vitamin A 37-44 retinol binding protein 1 Rattus norvegicus 22-26 3198596-7 1988 The addition of progesterone, a known inhibitor of the acyl-CoA:retinol acyltransferase reaction, consistently increased the rate of retinyl ester formation when [3H]retinol was delivered bound to CRBP. Vitamin A 64-71 retinol binding protein 1 Rattus norvegicus 197-201 3198596-8 1988 These experiments indicate that retinol presented to liver microsomal membranes by CRBP can be converted to retinyl ester and that this process, in contrast to the esterification of dispersed retinol, is independent of the addition of an activated fatty acid and produces a pattern of retinyl ester species similar to that observed in intact liver. Vitamin A 32-39 retinol binding protein 1 Rattus norvegicus 83-87 3198596-9 1988 A possible role of phospholipids as endogenous acyl donors in the esterification of retinol bound to CRBP is supported by our observations that depletion of microsomal phospholipid with phospholipase A2 prior to addition of retinol-CRBP decreased the retinol-esterifying activity almost 50%. Vitamin A 84-91 retinol binding protein 1 Rattus norvegicus 101-105 3198596-9 1988 A possible role of phospholipids as endogenous acyl donors in the esterification of retinol bound to CRBP is supported by our observations that depletion of microsomal phospholipid with phospholipase A2 prior to addition of retinol-CRBP decreased the retinol-esterifying activity almost 50%. Vitamin A 84-91 retinol binding protein 1 Rattus norvegicus 232-236 3198596-9 1988 A possible role of phospholipids as endogenous acyl donors in the esterification of retinol bound to CRBP is supported by our observations that depletion of microsomal phospholipid with phospholipase A2 prior to addition of retinol-CRBP decreased the retinol-esterifying activity almost 50%. Vitamin A 224-231 retinol binding protein 1 Rattus norvegicus 101-105 3198596-9 1988 A possible role of phospholipids as endogenous acyl donors in the esterification of retinol bound to CRBP is supported by our observations that depletion of microsomal phospholipid with phospholipase A2 prior to addition of retinol-CRBP decreased the retinol-esterifying activity almost 50%. Vitamin A 224-231 retinol binding protein 1 Rattus norvegicus 101-105 3198596-10 1988 Conversely, incubating microsomes with a lipid-generating system containing choline, CDP-choline, glycerol 3-phosphate, and an acyl-CoA-generating system prior to addition of retinol-CRBP increased retinol esterification significantly as compared to buffer-treated controls. Vitamin A 175-182 retinol binding protein 1 Rattus norvegicus 183-187 2837191-1 1988 The levels of mRNA for cellular retinol binding protein (CRBP) were studied in primary rat Sertoli cell cultures treated with cAMP analogues and retinol. Vitamin A 32-39 retinol binding protein 1 Rattus norvegicus 57-61 3053716-1 1988 Cellular retinol-binding protein (CRBP) and cellular retinol-binding protein II (CRBP II) are 132-residue cytosolic proteins which have 56% amino acid sequence identity and bind all-trans-retinol as their endogenous ligand. Vitamin A 9-16 retinol binding protein 1 Rattus norvegicus 34-38 3053716-10 1988 However, all-trans-retinal could displace all-trans-retinol bound to CRBP II but not to CRBP. Vitamin A 46-59 retinol binding protein 1 Rattus norvegicus 69-73 3190677-1 1988 Retinol deficiency resulted in decreased mRNA levels for cellular retinol-binding protein (CRBP) in the lungs and the testes. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 57-89 3190677-1 1988 Retinol deficiency resulted in decreased mRNA levels for cellular retinol-binding protein (CRBP) in the lungs and the testes. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 91-95 3190677-2 1988 The level of lung CRBP mRNA increased 2.3-fold one hour after oral administration of retinoic acid to retinol deficient rats. Vitamin A 102-109 retinol binding protein 1 Rattus norvegicus 18-22 3190677-4 1988 Our data indicate that retinoic acid regulates CRBP mRNA level in the whole animal and this rapid effect suggests a role for CRBP in the mechanism of vitamin A action at genomic level. Vitamin A 150-159 retinol binding protein 1 Rattus norvegicus 47-51 3190677-4 1988 Our data indicate that retinoic acid regulates CRBP mRNA level in the whole animal and this rapid effect suggests a role for CRBP in the mechanism of vitamin A action at genomic level. Vitamin A 150-159 retinol binding protein 1 Rattus norvegicus 125-129 2837191-3 1988 Retinol concentrations above 10 nM induced a dose- and time-dependent increase (2-3 fold) in mRNA levels for CRBP. Vitamin A 0-7 retinol binding protein 1 Rattus norvegicus 109-113 2837191-4 1988 Assuming that CRBP is important for vitamin A action, our data indicate that both cAMP and retinol itself modulate the sensitivity of the Sertoli cells for retinol. Vitamin A 36-45 retinol binding protein 1 Rattus norvegicus 14-18 2837191-4 1988 Assuming that CRBP is important for vitamin A action, our data indicate that both cAMP and retinol itself modulate the sensitivity of the Sertoli cells for retinol. Vitamin A 91-98 retinol binding protein 1 Rattus norvegicus 14-18 2837191-4 1988 Assuming that CRBP is important for vitamin A action, our data indicate that both cAMP and retinol itself modulate the sensitivity of the Sertoli cells for retinol. Vitamin A 156-163 retinol binding protein 1 Rattus norvegicus 14-18 4038610-11 1985 Vitamin A-deficient rats showed markedly reduced specific immune staining for CRBP in both testes and epididymides, and greatly reduced levels of CRBP in these tissues on radioimmunoassay. Vitamin A 0-9 retinol binding protein 1 Rattus norvegicus 78-82 3025324-1 1986 A study was conducted to explore the effects of retinoic acid, fed to retinol-deficient rats, on the tissue distribution and levels of cellular retinol-binding protein (CRBP) and cellular retinoic acid-binding protein (CRABP). Vitamin A 70-77 retinol binding protein 1 Rattus norvegicus 135-167 3025324-5 1986 Analysis of the data indicated that only the CRBP level of the proximal epididymis in the retinol-deficient/retinoic acid group differed significantly from (was lower than) the corresponding control level, at the 1% confidence level. Vitamin A 90-97 retinol binding protein 1 Rattus norvegicus 45-49 3461459-5 1986 Both polypeptides contain reactive thiol groups, but the rate of disruption of CRBP II-retinol complexes by p-chloromercuribenzoate is greater than that of CRBP-retinol. Vitamin A 87-94 retinol binding protein 1 Rattus norvegicus 79-83 2998635-7 1985 The tissue distribution of CRBP and CRABP, together with their relation to lipid transporting proteins suggests that CRBP and CRABP are cellular transporting proteins for retinol and retinoic acid, respectively. Vitamin A 171-178 retinol binding protein 1 Rattus norvegicus 27-31 2998635-7 1985 The tissue distribution of CRBP and CRABP, together with their relation to lipid transporting proteins suggests that CRBP and CRABP are cellular transporting proteins for retinol and retinoic acid, respectively. Vitamin A 171-178 retinol binding protein 1 Rattus norvegicus 117-121 3860818-14 1985 The cell-specific localization pattern determined for these two proteins suggests that CRBP(II), rather than CRBP, is the protein that plays a role in the absorption of retinol. Vitamin A 169-176 retinol binding protein 1 Rattus norvegicus 87-91 2983610-2 1985 Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP). Vitamin A 31-38 retinol binding protein 1 Rattus norvegicus 127-159 2983610-2 1985 Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP). Vitamin A 31-38 retinol binding protein 1 Rattus norvegicus 161-165 2983610-2 1985 Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP). Vitamin A 88-95 retinol binding protein 1 Rattus norvegicus 127-159 2983610-2 1985 Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP). Vitamin A 88-95 retinol binding protein 1 Rattus norvegicus 161-165 2983610-4 1985 A preparation of solubilized chromatin isolated from liver nuclei was able to accept retinol from its complex with CRBP as described previously for nuclei and chromatin. Vitamin A 85-92 retinol binding protein 1 Rattus norvegicus 115-119 3584109-1 1987 Cellular retinol-binding protein (CRBP) and cellular retinol-binding protein II (CRBP II) are two highly homologous cytoplasmic proteins that bind all-trans-retinol. Vitamin A 9-16 retinol binding protein 1 Rattus norvegicus 34-38 3472205-1 1987 Cellular retinol-binding protein (CRBP) may be an important mediator of vitamin A action. Vitamin A 72-81 retinol binding protein 1 Rattus norvegicus 0-32 3472205-1 1987 Cellular retinol-binding protein (CRBP) may be an important mediator of vitamin A action. Vitamin A 72-81 retinol binding protein 1 Rattus norvegicus 34-38 3472205-8 1987 Finally, when retinol-deficient rats are fed retinyl acetate for 4 hr, about 4-fold accumulation of CRBP-specific mRNA is observed in the lungs. Vitamin A 14-21 retinol binding protein 1 Rattus norvegicus 100-104 3013093-4 1986 If CRABP charged with nonlabeled retinoic acid was included in the incubation, binding of radioactivity was diminished, whereas inclusion of free retinoic acid, or the complex of retinol with cellular retinol binding protein (CRBP) or serum retinol binding protein had no effect. Vitamin A 179-186 retinol binding protein 1 Rattus norvegicus 192-224 3013093-9 1986 Further, CRBP, the putative mediator of retinol action, was found to enable retinol to be bound to testicular nuclei, in an interaction similar to the binding of retinol to liver nuclei described previously. Vitamin A 40-47 retinol binding protein 1 Rattus norvegicus 9-13 3013093-9 1986 Further, CRBP, the putative mediator of retinol action, was found to enable retinol to be bound to testicular nuclei, in an interaction similar to the binding of retinol to liver nuclei described previously. Vitamin A 76-83 retinol binding protein 1 Rattus norvegicus 9-13 3013093-9 1986 Further, CRBP, the putative mediator of retinol action, was found to enable retinol to be bound to testicular nuclei, in an interaction similar to the binding of retinol to liver nuclei described previously. Vitamin A 76-83 retinol binding protein 1 Rattus norvegicus 9-13 4038610-11 1985 Vitamin A-deficient rats showed markedly reduced specific immune staining for CRBP in both testes and epididymides, and greatly reduced levels of CRBP in these tissues on radioimmunoassay. Vitamin A 0-9 retinol binding protein 1 Rattus norvegicus 146-150 4038610-12 1985 These studies on the localization of CRBP provide information concerning the specific cells and anatomic loci within the testis and epididymis where retinol may be playing an important role in sperm formation and maturation. Vitamin A 149-156 retinol binding protein 1 Rattus norvegicus 37-41 6889638-5 1982 To confirm the autoradiographic localization of vitamin A, the cellular retinol-binding protein (CRBP) assay demonstrates the presence of CRBP in the interstitial tissue and seminiferous tubules. Vitamin A 48-57 retinol binding protein 1 Rattus norvegicus 63-95 6746230-9 1984 Interpretation of the results includes a dual role for CRBP in the RPE, namely its involvement in gene expression and transcytoplasmic transport of retinol. Vitamin A 148-155 retinol binding protein 1 Rattus norvegicus 55-59 4077397-8 1985 A relationship between these phenomena and the subcellular distribution of the retinyl palmitate hydrolase (RPH) and the cellular vitamin A binding proteins (CRBP) is likely to exist. Vitamin A 130-139 retinol binding protein 1 Rattus norvegicus 158-162 6373783-9 1984 The prominence of the CRBP-positive fat-storing cells changed markedly with vitamin A status. Vitamin A 76-85 retinol binding protein 1 Rattus norvegicus 22-26 6889638-5 1982 To confirm the autoradiographic localization of vitamin A, the cellular retinol-binding protein (CRBP) assay demonstrates the presence of CRBP in the interstitial tissue and seminiferous tubules. Vitamin A 48-57 retinol binding protein 1 Rattus norvegicus 138-142 7197683-3 1981 We have previously reported that purified cellular retinol-binding (CRBP) will mediate specific binding of retinol to nuclei isolated from rat liver. Vitamin A 51-58 retinol binding protein 1 Rattus norvegicus 68-72 7197683-3 1981 We have previously reported that purified cellular retinol-binding (CRBP) will mediate specific binding of retinol to nuclei isolated from rat liver. Vitamin A 107-114 retinol binding protein 1 Rattus norvegicus 68-72 7197683-4 1981 We now report that pure CRBP delivers retinol to the specific nuclear binding sites without itself remaining bound. Vitamin A 38-45 retinol binding protein 1 Rattus norvegicus 24-28 7197683-6 1981 CRBP is also capable of delivering retinol specifically to isolated chromatin with no apparent loss of binding sites, as compared to whole nuclei. Vitamin A 35-42 retinol binding protein 1 Rattus norvegicus 0-4 7197683-7 1981 CRBP again does not remain bound after transferring retinol to the chromatin binding sites. Vitamin A 52-59 retinol binding protein 1 Rattus norvegicus 0-4 7197683-8 1981 When isolated nuclei are incubated with [3H]retinol-CRBP, sectioned, and autoradiographed, specifically bound retinol is found distributed throughout the nuclei. Vitamin A 44-51 retinol binding protein 1 Rattus norvegicus 52-56 7197683-9 1981 Thus, CRBP delivers retinol to the interior of the nucleus, to specific binding sites which are primarily, if not solely, on the chromatin. Vitamin A 20-27 retinol binding protein 1 Rattus norvegicus 6-10 6159246-1 1980 Cellular retinol-binding protein (CRBP) in cancers and in vitro-transformed epithelial cells of the ACI/N rat urinary bladder was assayed with radiolabeled retinol by sucrose density gradient centrifugation. Vitamin A 9-16 retinol binding protein 1 Rattus norvegicus 34-38 6159246-5 1980 The addition of retinol to the culture medium prevented the in vitro keratinization of CRBP-positive cells but it had no effect on the keratinization of CRBP-negative cells. Vitamin A 16-23 retinol binding protein 1 Rattus norvegicus 87-91 573703-2 1979 One, called cellular retinol-binding protein (CRBP), binds retinol with high specificity and affinity, but not retinal or retinoic acid. Vitamin A 21-28 retinol binding protein 1 Rattus norvegicus 46-50 573703-9 1979 It appears that the cell nucleus is a target for retinol action, as CRBP allows specific interaction of retinol with the nucleus, showing the presence of specific binding sites for retinol. Vitamin A 49-56 retinol binding protein 1 Rattus norvegicus 68-72 573703-9 1979 It appears that the cell nucleus is a target for retinol action, as CRBP allows specific interaction of retinol with the nucleus, showing the presence of specific binding sites for retinol. Vitamin A 104-111 retinol binding protein 1 Rattus norvegicus 68-72 573703-9 1979 It appears that the cell nucleus is a target for retinol action, as CRBP allows specific interaction of retinol with the nucleus, showing the presence of specific binding sites for retinol. Vitamin A 104-111 retinol binding protein 1 Rattus norvegicus 68-72 573704-5 1979 The ultraviolet absorption spectrums of the cytosol binding protein for retinol (CRBP) and of the cytosol binding protein for retinoic acid (CRABP) were almost identical despite differences in the nature of the ligands bound by these two proteins. Vitamin A 72-79 retinol binding protein 1 Rattus norvegicus 81-85 569012-6 1978 The CRBP of the tumor was associated with endogenous retinol (77 to 100% saturation) and was similar to, if not identical with, CRBP of normal tissue, as judged by fluorescence spectra, sedimentation behavior, and elution position on Sephadex G-75. Vitamin A 53-60 retinol binding protein 1 Rattus norvegicus 4-8 287060-1 1979 Purified cellular retinol-binding protein (CRBP), a potential mediator of vitamin A action, was found to enable retinol to bind in a specific manner to isolated nuclei from livers of vitamin A deficient rats. Vitamin A 74-83 retinol binding protein 1 Rattus norvegicus 43-47 287060-1 1979 Purified cellular retinol-binding protein (CRBP), a potential mediator of vitamin A action, was found to enable retinol to bind in a specific manner to isolated nuclei from livers of vitamin A deficient rats. Vitamin A 18-25 retinol binding protein 1 Rattus norvegicus 43-47 287060-1 1979 Purified cellular retinol-binding protein (CRBP), a potential mediator of vitamin A action, was found to enable retinol to bind in a specific manner to isolated nuclei from livers of vitamin A deficient rats. Vitamin A 183-192 retinol binding protein 1 Rattus norvegicus 43-47 287060-4 1979 CRBP charged with unlabeled retinol or CRBP without retinol diminished binding of radioactivity whereas free retinol did not. Vitamin A 28-35 retinol binding protein 1 Rattus norvegicus 0-4 287060-4 1979 CRBP charged with unlabeled retinol or CRBP without retinol diminished binding of radioactivity whereas free retinol did not. Vitamin A 52-59 retinol binding protein 1 Rattus norvegicus 0-4 287060-4 1979 CRBP charged with unlabeled retinol or CRBP without retinol diminished binding of radioactivity whereas free retinol did not. Vitamin A 52-59 retinol binding protein 1 Rattus norvegicus 0-4