PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10490651-1 1999 Two sorts of proteins bind to, and mediate the developmental and homeostatic effects of, retinoic acid (RA): the RAR and RXR nuclear receptors, which act as ligand-dependent transcriptional regulators, and the cellular RA binding proteins (CRABPI and CRABPII). Tretinoin 89-102 cellular retinoic acid binding protein 1 Homo sapiens 240-246 10490651-1 1999 Two sorts of proteins bind to, and mediate the developmental and homeostatic effects of, retinoic acid (RA): the RAR and RXR nuclear receptors, which act as ligand-dependent transcriptional regulators, and the cellular RA binding proteins (CRABPI and CRABPII). Tretinoin 104-106 cellular retinoic acid binding protein 1 Homo sapiens 240-246 10446126-1 1999 The pleiotropic effects of retinoic acid (RA) in mammalian cells are mediated by two classes of proteins: the retinoic acid receptors (RAR) and cellular retinoic acid-binding proteins (CRABP-I and CRABP-II). Tretinoin 27-40 cellular retinoic acid binding protein 1 Homo sapiens 185-192 10569185-1 1999 We have mutated the type I cellular retinoic acid binding protein (CRABP-I), individually at the Arg131 (into Ala) and the Tyr133 (into Phe) residues which have been predicted to make direct contact with retinoic acid (RA) based upon previous structural studies. Tretinoin 36-49 cellular retinoic acid binding protein 1 Homo sapiens 67-74 10569185-4 1999 By using an RA-inducible reporter, it is found that the wild type CRABP-I exerts biphasic effects on RA induction of the reporter. Tretinoin 12-14 cellular retinoic acid binding protein 1 Homo sapiens 66-73 10446126-1 1999 The pleiotropic effects of retinoic acid (RA) in mammalian cells are mediated by two classes of proteins: the retinoic acid receptors (RAR) and cellular retinoic acid-binding proteins (CRABP-I and CRABP-II). Tretinoin 42-44 cellular retinoic acid binding protein 1 Homo sapiens 185-192 10446126-6 1999 The rate constant for movement of RA from CRABP-II, but not from CRABP-I, to RAR strongly depended on the concentration of the acceptor. Tretinoin 34-36 cellular retinoic acid binding protein 1 Homo sapiens 42-49 9858140-1 1998 Recognition that cellular retinoic acid binding protein (CRABP)-I and CRABP-II are found in different cell types has provided additional support for the presumably divergent roles of these two proteins in mediating retinoic acid (RA) effects in human skin. Tretinoin 26-39 cellular retinoic acid binding protein 1 Homo sapiens 57-65 9865735-4 1998 Consistent with this finding, the RA binding activity of CRABP in APL cells from three pretreatment cases (range, 27.2-53.2 fmol/mg protein) was similar to that of NB4 cells (22.6 +/- 5.4 fmol/mg protein). Tretinoin 34-36 cellular retinoic acid binding protein 1 Homo sapiens 57-62 9858140-1 1998 Recognition that cellular retinoic acid binding protein (CRABP)-I and CRABP-II are found in different cell types has provided additional support for the presumably divergent roles of these two proteins in mediating retinoic acid (RA) effects in human skin. Tretinoin 215-228 cellular retinoic acid binding protein 1 Homo sapiens 57-65 9858140-5 1998 We report that CRABP-I is expressed in isolated melanocytes at the mRNA level, although under these circumstances the protein has minimal RA-binding activity, and that keratinocytic and dermal influences are required for CRABP-I activity in melanocytes. Tretinoin 16-18 cellular retinoic acid binding protein 1 Homo sapiens 221-228 7556191-7 1995 Exposure of HUVEC to 1 microM retinoic acid or the retinobenzoic acid, Ch55, led to the induction of the two RAR-beta mRNAs, RXR-alpha mRNA and CRBP-I mRNA, whereas the expression of the other receptor and CRABP-I transcripts did not change appreciably. Tretinoin 30-43 cellular retinoic acid binding protein 1 Homo sapiens 206-213 9153406-4 1997 Analyses of the distribution of limiting amounts of [3H]-all-trans-retinoic acid between cytoplasmic retinoic acid binding proteins, CRABP-I and CRABP-II, and the purified heterocomplexes indicate that all-trans-retinoic acid binds with comparable affinity to CRABP-I and the heterocomplexes, but with approximately 10-fold less affinity to CRABP-II. Tretinoin 61-80 cellular retinoic acid binding protein 1 Homo sapiens 145-152 9174119-3 1997 The IC50 plots of DDRA for inhibition of [3H]RA binding to CRABP I and II and to RAR alpha, beta and gamma illustrate that this retinoid binds with the same affinity as RA to these proteins. Tretinoin 20-22 cellular retinoic acid binding protein 1 Homo sapiens 59-73 9174119-3 1997 The IC50 plots of DDRA for inhibition of [3H]RA binding to CRABP I and II and to RAR alpha, beta and gamma illustrate that this retinoid binds with the same affinity as RA to these proteins. Tretinoin 45-47 cellular retinoic acid binding protein 1 Homo sapiens 59-73 8999826-2 1997 It has been suggested that electrostatic interactions are critical for binding of retinoic acid by cellular retinoic acid-binding proteins (CRABP-I and CRABP-II). Tretinoin 82-95 cellular retinoic acid binding protein 1 Homo sapiens 140-147 8999826-3 1997 However, the roles of two conserved arginine residues (Arg-111 and Arg-131 in CRABP-I; Arg-111 and Arg-132 in CRABP-II) that interact with the carboxyl group of retinoic acid have not been evaluated. Tretinoin 161-174 cellular retinoic acid binding protein 1 Homo sapiens 78-85 7492559-1 1995 Cellular retinoic acid binding protein-I (CRABP-I) and cellular retinoic acid binding protein-II (CRABP-II) are highly homologous, 15 kDa proteins which bind all-trans-retinoic acid. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 42-49 7492559-3 1995 To obtain structural information which could aid the design of more selective ligands, isotope-directed NMR methods were employed to observe the CRABP-bound conformation of 13C-labeled retinoic acid and to identify its contact points with neighboring amino acids. Tretinoin 185-198 cellular retinoic acid binding protein 1 Homo sapiens 145-150 7492559-10 1995 The pattern of intermolecular NOESY cross-peaks between 13C-labeled protons in the ring portion of retinoic acid and protein protons were different between CRABP-I and CRABP-II. Tretinoin 99-112 cellular retinoic acid binding protein 1 Homo sapiens 156-163 7726866-2 1995 In chloramphenicol acetyl transferase (CAT) assay with retinoic acid response element-beta, GGA and 4,5-didehydro GGA were both positive, but 2,3-dihydro GGA was negative, even though these GGA derivatives have been reported to be all potent ligands for cellular retinoic-acid-binding protein(CRABP). Tretinoin 55-68 cellular retinoic acid binding protein 1 Homo sapiens 293-298 7626500-6 1995 Considerable data favor a model pathway of RA biosynthesis and metabolism consisting of enzymes that recognize CRBP (apo and holo) and holo-CRABP as substrates and/or affecters of activity. Tretinoin 43-45 cellular retinoic acid binding protein 1 Homo sapiens 140-145 7626500-13 1995 CRABP is also important to modulating the steady-state concentrations of RA, through sequestering RA and facilitating its metabolism, because the complex CRABP/RA acts as a low Km substrate. Tretinoin 1-3 cellular retinoic acid binding protein 1 Homo sapiens 154-159 7626500-13 1995 CRABP is also important to modulating the steady-state concentrations of RA, through sequestering RA and facilitating its metabolism, because the complex CRABP/RA acts as a low Km substrate. Tretinoin 73-75 cellular retinoic acid binding protein 1 Homo sapiens 0-5 7626500-13 1995 CRABP is also important to modulating the steady-state concentrations of RA, through sequestering RA and facilitating its metabolism, because the complex CRABP/RA acts as a low Km substrate. Tretinoin 73-75 cellular retinoic acid binding protein 1 Homo sapiens 154-159 7626495-1 1995 The two cellular retinoic acid binding proteins, CRABP I and CRABP II, belong to a family of small cytosolic lipid binding proteins and are highly conserved during evolution. Tretinoin 17-30 cellular retinoic acid binding protein 1 Homo sapiens 49-56 7626495-5 1995 It has been proposed that CRABP I sequesters retinoic acid in the cytoplasm and prevents nuclear uptake of retinoic acid. Tretinoin 45-58 cellular retinoic acid binding protein 1 Homo sapiens 26-33 7626495-5 1995 It has been proposed that CRABP I sequesters retinoic acid in the cytoplasm and prevents nuclear uptake of retinoic acid. Tretinoin 107-120 cellular retinoic acid binding protein 1 Homo sapiens 26-33 7626495-9 1995 A regulated nuclear uptake of CRABP I implies a role for this protein in the intracellular transport of retinoic acid. Tretinoin 104-117 cellular retinoic acid binding protein 1 Homo sapiens 30-37 8207983-0 1994 In vitro all-trans retinoic acid (ATRA) sensitivity and cellular retinoic acid binding protein (CRABP) levels in relapse leukemic cells after remission induction by ATRA in acute promyelocytic leukemia. Tretinoin 165-169 cellular retinoic acid binding protein 1 Homo sapiens 56-94 7798615-1 1994 The cellular retinoic acid-binding proteins (CRABP I and II) are thought to mediate the effects of retinoic acid on target cells. Tretinoin 13-26 cellular retinoic acid binding protein 1 Homo sapiens 45-59 7798615-1 1994 The cellular retinoic acid-binding proteins (CRABP I and II) are thought to mediate the effects of retinoic acid on target cells. Tretinoin 99-112 cellular retinoic acid binding protein 1 Homo sapiens 45-59 8207983-0 1994 In vitro all-trans retinoic acid (ATRA) sensitivity and cellular retinoic acid binding protein (CRABP) levels in relapse leukemic cells after remission induction by ATRA in acute promyelocytic leukemia. Tretinoin 165-169 cellular retinoic acid binding protein 1 Homo sapiens 96-101 8207983-6 1994 We have demonstrated that AML3 patients" cells (from four patients) at relapse show high levels of CRABP, a cytosolic retinoic acid binding protein and this protein was not detected prior to ATRA therapy. Tretinoin 191-195 cellular retinoic acid binding protein 1 Homo sapiens 99-104 8207983-9 1994 This induced ATRA hypercatabolytic state should be monitored during consolidation therapy and at relapse by evaluating CRABP and RA metabolite levels, in order to detect ATRA resistance in patients with AML3. Tretinoin 13-17 cellular retinoic acid binding protein 1 Homo sapiens 119-124 8144640-11 1994 Reduced metabolism of CRABP-bound C4-derivatized retinoids suggests pathways of retinoic acid metabolism besides the one initiated by C4-hydroxylation. Tretinoin 80-93 cellular retinoic acid binding protein 1 Homo sapiens 22-27 8185324-9 1994 Binding studies demonstrated that CRABP-I and CRABP-II possess two classes of RA-binding sites: one class of high-affinity binding sites with a constant of dissociation (Kd) of 1.5 nM for CRABP-I and 4.7 nM for CRABP-II and one class of low-affinity binding sites with a Kd of 69 nM for CRABP-I and 101 nM for CRABP-II. Tretinoin 35-37 cellular retinoic acid binding protein 1 Homo sapiens 188-201 8144640-13 1994 Ketoconazole inhibited the metabolism by testis microsomes of free and CRABP-bound retinoic acid with IC50 values of 2 and 0.7 microM, respectively, denoting catalysis by cytochrome P-450. Tretinoin 83-96 cellular retinoic acid binding protein 1 Homo sapiens 71-76 8144640-2 1994 This report extends our observation that cellular retinoic acid-binding protein type I (CRABP) serves as substrate for retinoic acid metabolism by testis microsomes. Tretinoin 50-63 cellular retinoic acid binding protein 1 Homo sapiens 88-93 8144640-14 1994 These results indicate that cloistering retinoic acid in CRABP, while permitting metabolism, may operate throughout CRABP-expressing tissues as a mechanism of controlling the concentrations of free retinoic acid. Tretinoin 40-53 cellular retinoic acid binding protein 1 Homo sapiens 57-62 8144640-3 1994 Retinoic acid bound to excess CRABP was metabolized at 70% of the unbound retinoic acid rate with testis microsomes and at the same rates as unbound retinoic acid with kidney and lung microsomes. Tretinoin 0-13 cellular retinoic acid binding protein 1 Homo sapiens 30-35 8144640-3 1994 Retinoic acid bound to excess CRABP was metabolized at 70% of the unbound retinoic acid rate with testis microsomes and at the same rates as unbound retinoic acid with kidney and lung microsomes. Tretinoin 74-87 cellular retinoic acid binding protein 1 Homo sapiens 30-35 8144640-14 1994 These results indicate that cloistering retinoic acid in CRABP, while permitting metabolism, may operate throughout CRABP-expressing tissues as a mechanism of controlling the concentrations of free retinoic acid. Tretinoin 40-53 cellular retinoic acid binding protein 1 Homo sapiens 116-121 8144640-3 1994 Retinoic acid bound to excess CRABP was metabolized at 70% of the unbound retinoic acid rate with testis microsomes and at the same rates as unbound retinoic acid with kidney and lung microsomes. Tretinoin 149-162 cellular retinoic acid binding protein 1 Homo sapiens 30-35 8144640-14 1994 These results indicate that cloistering retinoic acid in CRABP, while permitting metabolism, may operate throughout CRABP-expressing tissues as a mechanism of controlling the concentrations of free retinoic acid. Tretinoin 198-211 cellular retinoic acid binding protein 1 Homo sapiens 57-62 8144640-7 1994 Retinoids bound to CRABP, isolated from a testis microsomal incubation, consisted of 50% retinoic acid, 32% P1 and 17% P2, suggesting that CRABP may bind retinoic acid metabolites in vivo. Tretinoin 89-102 cellular retinoic acid binding protein 1 Homo sapiens 19-24 8144640-14 1994 These results indicate that cloistering retinoic acid in CRABP, while permitting metabolism, may operate throughout CRABP-expressing tissues as a mechanism of controlling the concentrations of free retinoic acid. Tretinoin 198-211 cellular retinoic acid binding protein 1 Homo sapiens 116-121 8144640-7 1994 Retinoids bound to CRABP, isolated from a testis microsomal incubation, consisted of 50% retinoic acid, 32% P1 and 17% P2, suggesting that CRABP may bind retinoic acid metabolites in vivo. Tretinoin 89-102 cellular retinoic acid binding protein 1 Homo sapiens 139-144 8144640-7 1994 Retinoids bound to CRABP, isolated from a testis microsomal incubation, consisted of 50% retinoic acid, 32% P1 and 17% P2, suggesting that CRABP may bind retinoic acid metabolites in vivo. Tretinoin 154-167 cellular retinoic acid binding protein 1 Homo sapiens 19-24 8061932-4 1994 We have analyzed the effects of topical application of triamcinolone acetonide (TA) on the retinoic acid-induced altered expression of CRABP I and II in normal human skin, at the protein and mRNA levels. Tretinoin 91-104 cellular retinoic acid binding protein 1 Homo sapiens 135-142 8144640-7 1994 Retinoids bound to CRABP, isolated from a testis microsomal incubation, consisted of 50% retinoic acid, 32% P1 and 17% P2, suggesting that CRABP may bind retinoic acid metabolites in vivo. Tretinoin 154-167 cellular retinoic acid binding protein 1 Homo sapiens 139-144 8061932-6 1994 In contrast, CRABP I protein was decreased by topical retinoic acid, and the down modulating effect of retinoic acid was counteracted by triamcinolone acetonide. Tretinoin 54-67 cellular retinoic acid binding protein 1 Homo sapiens 13-20 8387121-6 1993 CRABP (I), previously recognized as a transport protein of retinoic acid to the nucleus, is now assumed to sequester retinoic acid from retinoic acid receptor(s) in the tissue where retinoic acid levels are required to be low. Tretinoin 59-72 cellular retinoic acid binding protein 1 Homo sapiens 0-5 7815831-0 1994 In vitro all-trans retinoic acid (ATRA) sensitivity and cellular retinoic acid binding protein (CRABP) levels in relapse leukemic cells after remission induction by ATRA in acute promyelocytic leukemia. Tretinoin 165-169 cellular retinoic acid binding protein 1 Homo sapiens 56-94 7815831-0 1994 In vitro all-trans retinoic acid (ATRA) sensitivity and cellular retinoic acid binding protein (CRABP) levels in relapse leukemic cells after remission induction by ATRA in acute promyelocytic leukemia. Tretinoin 165-169 cellular retinoic acid binding protein 1 Homo sapiens 96-101 7815831-6 1994 We have demonstrated that AML3 patients" cells (from four patients) at relapse show high levels of CRABP, a cytosolic retinoic acid binding protein and this protein was not detected prior to ATRA therapy. Tretinoin 191-195 cellular retinoic acid binding protein 1 Homo sapiens 99-104 7815831-9 1994 This induced ATRA hypercatabolytic state should be monitored during consolidation therapy and at relapse by evaluating CRABP and RA metabolite levels, in order to detect ATRA resistance in patients with AML3. Tretinoin 13-17 cellular retinoic acid binding protein 1 Homo sapiens 119-124 8162338-1 1993 Mammalian cell cytoplasm contains at least two proteins which bind retinoic acid (RA): CRABP I and CRABP II. Tretinoin 67-80 cellular retinoic acid binding protein 1 Homo sapiens 87-94 8162338-1 1993 Mammalian cell cytoplasm contains at least two proteins which bind retinoic acid (RA): CRABP I and CRABP II. Tretinoin 82-84 cellular retinoic acid binding protein 1 Homo sapiens 87-94 8387121-6 1993 CRABP (I), previously recognized as a transport protein of retinoic acid to the nucleus, is now assumed to sequester retinoic acid from retinoic acid receptor(s) in the tissue where retinoic acid levels are required to be low. Tretinoin 117-130 cellular retinoic acid binding protein 1 Homo sapiens 0-5 8387121-6 1993 CRABP (I), previously recognized as a transport protein of retinoic acid to the nucleus, is now assumed to sequester retinoic acid from retinoic acid receptor(s) in the tissue where retinoic acid levels are required to be low. Tretinoin 117-130 cellular retinoic acid binding protein 1 Homo sapiens 0-5 8387121-7 1993 CRABP (I) also functions in the catabolism of retinoic acid to modulate its concentration in the cell. Tretinoin 46-59 cellular retinoic acid binding protein 1 Homo sapiens 0-5 1314862-3 1992 In an attempt to identify other potential regulators of RA responsiveness, we have used RNA blot hybridization to study the expression of the cellular retinoic acid binding proteins (CRABP) CRABP-I and CRABP-II, the RAR-gamma isoforms RAR-gamma 1 and RAR-gamma 2, and the low-affinity RAR homologue RXR in normal, RA-treated, and psoriatic human epidermis. Tretinoin 56-58 cellular retinoic acid binding protein 1 Homo sapiens 190-197 8382035-4 1993 In binding studies the equilibrium dissociation constant, Kd, of retinoic acid (RA) for E. coli-derived CRABP-I and CRABP-II was 6.8 and 39 nM, respectively. Tretinoin 65-78 cellular retinoic acid binding protein 1 Homo sapiens 104-111 8382035-4 1993 In binding studies the equilibrium dissociation constant, Kd, of retinoic acid (RA) for E. coli-derived CRABP-I and CRABP-II was 6.8 and 39 nM, respectively. Tretinoin 80-82 cellular retinoic acid binding protein 1 Homo sapiens 104-111 8382035-6 1993 RA competed with the binding of CD 367 to CRABP-I and CRABP-II with IC50 values of 20.0 and 90.0 nM, respectively. Tretinoin 0-2 cellular retinoic acid binding protein 1 Homo sapiens 42-49 8382035-10 1993 The observed difference in affinity for RA supports the idea that CRABP-I, which is constitutively expressed, and CRABP-II, which is induced by RA, have different functions in the cell. Tretinoin 40-42 cellular retinoic acid binding protein 1 Homo sapiens 66-73 1332671-6 1992 We show that CRABP-I and -II have similar M(r) values (15,000), but differ in their dissociation constant towards retinoic acid (Kd of 16.6 nM and 50 nM respectively), in pI (4.86 and 5.13) and in their relative mobilities (RF) on PAGE under nondenaturating conditions (RF values 0.65 and 0.44). Tretinoin 114-127 cellular retinoic acid binding protein 1 Homo sapiens 13-28 1332671-17 1992 The sharp increases in CRABP-II levels are associated with an alteration in the differentiation programme, as well as with cell response to retinoic acid overload, whereas CRABP-I might be a marker for terminal differentiation. Tretinoin 140-153 cellular retinoic acid binding protein 1 Homo sapiens 23-30 8381481-0 1993 Biosynthesis and metabolism of retinoic acid: roles of CRBP and CRABP in retinoic acid: roles of CRBP and CRABP in retinoic acid homeostasis. Tretinoin 31-44 cellular retinoic acid binding protein 1 Homo sapiens 64-69 8381481-0 1993 Biosynthesis and metabolism of retinoic acid: roles of CRBP and CRABP in retinoic acid: roles of CRBP and CRABP in retinoic acid homeostasis. Tretinoin 31-44 cellular retinoic acid binding protein 1 Homo sapiens 106-111 1328234-0 1992 The level of CRABP-I expression influences the amounts and types of all-trans-retinoic acid metabolites in F9 teratocarcinoma stem cells. Tretinoin 78-91 cellular retinoic acid binding protein 1 Homo sapiens 13-20 1328234-3 1992 We have previously shown that overexpression of the CRABP-I protein in stably transfected F9 stem cell lines results in a lower sensitivity to a given external concentration of retinoic acid relative to that of untransfected F9 cells; in contrast, reduced CRABP-I expression in CRABP-I cDNA anti-sense transfected lines is associated with increased sensitivity of these lines to retinoic acid. Tretinoin 177-190 cellular retinoic acid binding protein 1 Homo sapiens 52-59 1328234-3 1992 We have previously shown that overexpression of the CRABP-I protein in stably transfected F9 stem cell lines results in a lower sensitivity to a given external concentration of retinoic acid relative to that of untransfected F9 cells; in contrast, reduced CRABP-I expression in CRABP-I cDNA anti-sense transfected lines is associated with increased sensitivity of these lines to retinoic acid. Tretinoin 379-392 cellular retinoic acid binding protein 1 Homo sapiens 52-59 1328234-4 1992 These three types of cell lines were cultured in the presence of 50 nM [3H]retinoic acid, and the metabolism of retinoic acid was followed over the next 24 h. The results demonstrate that CRABP-I has the ability to alter both the levels and types of RA metabolites produced in the cytoplasm of differentiating embryonic stem cells. Tretinoin 75-88 cellular retinoic acid binding protein 1 Homo sapiens 188-195 1328234-4 1992 These three types of cell lines were cultured in the presence of 50 nM [3H]retinoic acid, and the metabolism of retinoic acid was followed over the next 24 h. The results demonstrate that CRABP-I has the ability to alter both the levels and types of RA metabolites produced in the cytoplasm of differentiating embryonic stem cells. Tretinoin 112-125 cellular retinoic acid binding protein 1 Homo sapiens 188-195 1328234-5 1992 Moreover, the level of CRABP-I determines the rate of RA metabolism to 4-oxo-RA such that the higher the CRABP-I level, the faster the metabolism of [3H]retinoic acid. Tretinoin 149-166 cellular retinoic acid binding protein 1 Homo sapiens 23-30 1328234-5 1992 Moreover, the level of CRABP-I determines the rate of RA metabolism to 4-oxo-RA such that the higher the CRABP-I level, the faster the metabolism of [3H]retinoic acid. Tretinoin 149-166 cellular retinoic acid binding protein 1 Homo sapiens 105-112 1378478-1 1992 We have previously shown that cellular retinoic acid-binding protein II (CRABP-II), but not cellular retinoic acid-binding protein I (CRABP-I), mRNA expression is markedly induced in human skin by topical retinoic acid. Tretinoin 39-52 cellular retinoic acid binding protein 1 Homo sapiens 73-80 1321791-1 1992 Two highly conserved forms of cellular retinoic acid binding protein (CRABP-I and CRABP-II) have been described, and one, CRABP-II, is highly expressed in human skin. Tretinoin 39-52 cellular retinoic acid binding protein 1 Homo sapiens 70-77 1334741-7 1992 The cellular transport and biological activity of retinoids may be mediated by their specific cytoplasmic binding proteins cellular retinol binding protein (CRBP) and the cellular retinoic acid binding protein (CRABP) which may function as shuttles targetting RA to nucleosol fraction and/or as regulator of cellular concentration of RA. Tretinoin 212-214 cellular retinoic acid binding protein 1 Homo sapiens 171-209 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1654334-1 1991 Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro. Tretinoin 0-13 cellular retinoic acid binding protein 1 Homo sapiens 36-43 1654334-6 1991 External application of 0.1% retinoic acid cream in vivo for 16 h resulted in a 16-fold induction of CRABP-II transcripts, while CRABP-I mRNA remained undetectable. Tretinoin 29-42 cellular retinoic acid binding protein 1 Homo sapiens 101-108 1654334-7 1991 Expression of CRABP-II, but not CRABP-I mRNA, was also markedly increased (greater than 15-fold) by retinoic acid treatment of fibroblasts cultured from human skin, whereas no significant induction of CRABP-II mRNA was observed in human lung fibroblasts. Tretinoin 100-113 cellular retinoic acid binding protein 1 Homo sapiens 14-21 1653241-1 1991 Characterization and evidence that holo-CRABP is a substrate in retinoic acid metabolism. Tretinoin 64-77 cellular retinoic acid binding protein 1 Homo sapiens 40-45 1653241-2 1991 Cellular retinoic acid binding protein (CRABP) has been expressed efficiently in Escherichia coli from the cDNA of bovine adrenal CRABP and characterized, especially with respect to affinity for endogenous retinoids and a role for it in retinoic acid metabolism. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 40-45 1653241-2 1991 Cellular retinoic acid binding protein (CRABP) has been expressed efficiently in Escherichia coli from the cDNA of bovine adrenal CRABP and characterized, especially with respect to affinity for endogenous retinoids and a role for it in retinoic acid metabolism. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 130-135 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 31-44 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-7 1991 These data indicate a direct role for CRABP in retinoic acid metabolism and suggest a mechanism for discriminating metabolically between all-trans- and 13-cis-retinoids. Tretinoin 47-60 cellular retinoic acid binding protein 1 Homo sapiens 38-43 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653151-11 1991 The data presented here indicate that fetal CRABP appears to play a role in differential accumulation of retinoic acid in certain structures of the developing hamster. Tretinoin 105-118 cellular retinoic acid binding protein 1 Homo sapiens 44-49 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 5-10 1653241-6 1991 Holo-CRABP was a substrate for retinoic acid catabolism in rat testes microsomes by three criteria: 1) the rate of retinoic acid metabolism with CRABP in excess of retinoic acid exceeded the rate supported by the free retinoic acid; 2) increasing the apo-CRABP did not decrease the rate as predicted if free retinoic acid were the only substrate; and 3) holo-CRABP had a lower Michaelis constant (1.8 nM) for retinoic acid elimination than did free retinoic acid (49 nM). Tretinoin 115-128 cellular retinoic acid binding protein 1 Homo sapiens 145-150 1768424-2 1991 Tritiated analogues of retinol (ROL) and retinoic acid corresponding to substituted benzo[b]thiophene (CD-270) alcohol and carboxylic acid, respectively, were used for the binding studies of the cellular retinoic acid-(CRABP-) and retinol-(CRBP-) binding proteins in human epidermal cells and serum retinol-binding protein (RBP). Tretinoin 41-54 cellular retinoic acid binding protein 1 Homo sapiens 219-224 1768424-2 1991 Tritiated analogues of retinol (ROL) and retinoic acid corresponding to substituted benzo[b]thiophene (CD-270) alcohol and carboxylic acid, respectively, were used for the binding studies of the cellular retinoic acid-(CRABP-) and retinol-(CRBP-) binding proteins in human epidermal cells and serum retinol-binding protein (RBP). Tretinoin 204-217 cellular retinoic acid binding protein 1 Homo sapiens 219-224 34480899-9 2021 The kcat/Km value for holo-CRABP-1, however, decreased ~65-fold in comparison with reactions with free all-trans retinoic acid. Tretinoin 113-126 cellular retinoic acid binding protein 1 Homo sapiens 27-34 16788631-5 1990 The cytosolic retinoic acid-binding protein (CRABP), which is differentially expressed during squamous differentiation of human epidermal keratinocytes, may control the effective concentration of retinoic acid in the cell and therefore regulate indirectly gene expression. Tretinoin 14-27 cellular retinoic acid binding protein 1 Homo sapiens 45-50 1966833-5 1990 A candidate gene involved in the regulation of endogenous RA concentrations is the gene encoding cellular RA binding protein (CRABP). Tretinoin 58-60 cellular retinoic acid binding protein 1 Homo sapiens 126-131 2163611-8 1990 Using PAGE/radiobinding assay, we demonstrated that retinoic acid formed from retinol was bound in differentiating keratinocytes to endogenous cellular retinoic acid-binding protein (CRABP). Tretinoin 52-65 cellular retinoic acid binding protein 1 Homo sapiens 143-181 2163611-8 1990 Using PAGE/radiobinding assay, we demonstrated that retinoic acid formed from retinol was bound in differentiating keratinocytes to endogenous cellular retinoic acid-binding protein (CRABP). Tretinoin 52-65 cellular retinoic acid binding protein 1 Homo sapiens 183-188 2164349-2 1990 RA inhibition of cell invasive potential was accompanied by a significant increase in specific high affinity cellular retinoic acid binding protein (CRABP) level. Tretinoin 0-2 cellular retinoic acid binding protein 1 Homo sapiens 109-147 2164349-2 1990 RA inhibition of cell invasive potential was accompanied by a significant increase in specific high affinity cellular retinoic acid binding protein (CRABP) level. Tretinoin 0-2 cellular retinoic acid binding protein 1 Homo sapiens 149-154 35565751-1 2022 Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 41-47 35565751-1 2022 Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. Tretinoin 65-88 cellular retinoic acid binding protein 1 Homo sapiens 41-47 35565751-1 2022 Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. Tretinoin 90-94 cellular retinoic acid binding protein 1 Homo sapiens 41-47 35565751-2 2022 CRABP1 and CRABP2 have been shown to interact with the atRA-clearing cytochrome P450 enzymes CYP26B1 and CYP26C1 and with nuclear retinoic acid receptors (RARs). Tretinoin 130-143 cellular retinoic acid binding protein 1 Homo sapiens 0-6 35565751-3 2022 We hypothesized that CRABP1 and CRABP2 also alter atRA metabolism and clearance by CYP26A1, the third key atRA-metabolizing enzyme in the CYP26 family. Tretinoin 50-54 cellular retinoic acid binding protein 1 Homo sapiens 21-27 35565751-6 2022 In comparison, the apparent kcat value was about 30% lower (0.71 +- 0.07 min-1 for holo-CRABP1 and 0.75 +- 0.09 min-1 for holo-CRABP2) in the presence of CRABPs than with free atRA (1.07 +- 0.08 min-1). Tretinoin 176-180 cellular retinoic acid binding protein 1 Homo sapiens 88-94 2457503-2 1988 In the present study the levels of cellular retinoic acid (CRABP)- and retinol (CRBP)-binding proteins were measured in cultured normal human epidermal keratinocytes. Tretinoin 44-57 cellular retinoic acid binding protein 1 Homo sapiens 59-64 2543582-1 1989 Retinoic acid (RA) is bound intracellularly by a specific, low molecular weight protein (CRABP), that is unrelated to its nuclear receptor and whose function and regulation are still unknown. Tretinoin 0-13 cellular retinoic acid binding protein 1 Homo sapiens 89-94 2543582-1 1989 Retinoic acid (RA) is bound intracellularly by a specific, low molecular weight protein (CRABP), that is unrelated to its nuclear receptor and whose function and regulation are still unknown. Tretinoin 15-17 cellular retinoic acid binding protein 1 Homo sapiens 89-94 2543582-3 1989 We found increased CRABP after daily application during 4 days of natural or synthetic retinoids (RA, acitretin, isotretinoin, Ro137410, retinol), that have either a high affinity to CRABP or can be transformed into RA. Tretinoin 20-22 cellular retinoic acid binding protein 1 Homo sapiens 183-188 35406141-0 2022 CRABP1 in Non-Canonical Activities of Retinoic Acid in Health and Diseases. Tretinoin 38-51 cellular retinoic acid binding protein 1 Homo sapiens 0-6 35406141-1 2022 In this review, we discuss the emerging role of Cellular Retinoic Acid Binding Protein 1 (CRABP1) as a mediator of non-canonical activities of retinoic acid (RA) and relevance to human diseases. Tretinoin 143-156 cellular retinoic acid binding protein 1 Homo sapiens 48-88 35406141-1 2022 In this review, we discuss the emerging role of Cellular Retinoic Acid Binding Protein 1 (CRABP1) as a mediator of non-canonical activities of retinoic acid (RA) and relevance to human diseases. Tretinoin 143-156 cellular retinoic acid binding protein 1 Homo sapiens 90-96 2645590-4 1989 Human skin extracts incubated with either [3H]retinol or [3H]retinoic acid and analyzed by PAGE is a novel technique for the study of cellular retinol-(CRBP) and retinoic acid-(CRABP) binding proteins; it allows one to more specifically analyse these binding proteins and differentiate them from RBP. Tretinoin 61-74 cellular retinoic acid binding protein 1 Homo sapiens 177-182 2645590-4 1989 Human skin extracts incubated with either [3H]retinol or [3H]retinoic acid and analyzed by PAGE is a novel technique for the study of cellular retinol-(CRBP) and retinoic acid-(CRABP) binding proteins; it allows one to more specifically analyse these binding proteins and differentiate them from RBP. Tretinoin 162-175 cellular retinoic acid binding protein 1 Homo sapiens 177-182 2645590-6 1989 When the ability of some synthetic analogs of retinoic acid to compete with [3H]retinoic acid binding on human skin CRABP was studied, two important observations were made: (1) the analogs that, when given to human subjects were pharmacologically active, were found to be good competitors and vice-versa, (2) no strict correlation was found between the IC50 and the pharmacological potency of the retinoid. Tretinoin 46-59 cellular retinoic acid binding protein 1 Homo sapiens 116-121 2645590-6 1989 When the ability of some synthetic analogs of retinoic acid to compete with [3H]retinoic acid binding on human skin CRABP was studied, two important observations were made: (1) the analogs that, when given to human subjects were pharmacologically active, were found to be good competitors and vice-versa, (2) no strict correlation was found between the IC50 and the pharmacological potency of the retinoid. Tretinoin 80-93 cellular retinoic acid binding protein 1 Homo sapiens 116-121 2842235-8 1988 The presence of cRABP suggest that retinoic acid may have a role to play in the function of the pancreas. Tretinoin 35-48 cellular retinoic acid binding protein 1 Homo sapiens 16-21 2825608-4 1987 A third intracellular protein, cellular retinoic acid-binding protein (CRABP) also is structurally similar but binds only retinoic acid. Tretinoin 40-53 cellular retinoic acid binding protein 1 Homo sapiens 71-76 2839288-1 1988 Binding proteins for retinoic acid (cellular retinoid acid binding protein, CRABP), and for vitamin A (cellular retinol binding protein, CRBP) have been demonstrated in various cell types; these binding proteins display the characteristics of receptors. Tretinoin 21-34 cellular retinoic acid binding protein 1 Homo sapiens 76-81 3133373-6 1988 Am 80 and Am 580 inhibited the specific binding of 3H-retinoic acid to CRABP, but also showed less affinity than authentic unlabeled retinoic acid and compound 19. Tretinoin 54-67 cellular retinoic acid binding protein 1 Homo sapiens 71-76 3365571-9 1988 One explanation of these results is that only well differentiated cells have functional cellular retinoic acid-binding protein (cRABP), and that certain actions of retinoic acid (inhibition of anchorage-dependent growth) are independent of the presence of cRABP. Tretinoin 97-110 cellular retinoic acid binding protein 1 Homo sapiens 128-133 2856163-1 1988 In order to better understand the respective roles of the nuclear retinoic acid receptors (RARs) and the cytosolic retinoic acid binding protein (CRABP) in the mode of action of retinoic acid (RA), several types of RA analogs have been synthesized. Tretinoin 147-149 cellular retinoic acid binding protein 1 Homo sapiens 105-144 2825608-9 1987 Like CRBP, CRABP can deliver its ligand retinoic acid to specific binding sites within the nucleus, sites different from those for retinol. Tretinoin 40-53 cellular retinoic acid binding protein 1 Homo sapiens 11-16 2820396-2 1987 Omega-6 fatty acids such as linoleic acid and arachidonic acid, precursors of prostaglandin synthesis, caused inhibition of retinoic acid binding to CRABP. Tretinoin 124-137 cellular retinoic acid binding protein 1 Homo sapiens 149-154 2820396-6 1987 Competition by omega-6 fatty acids with retinoic acid for CRABP may neutralize the binding protein-mediated biological functions of retinoic acid, and could thereby enhance tumor production. Tretinoin 40-53 cellular retinoic acid binding protein 1 Homo sapiens 58-63 2820396-1 1987 Cellular retinoic acid-binding protein (CRABP) is the putative mediator of the biological effects of retinoic acid in the control of epithelial differentiation and tumorigenesis. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 40-45 2820396-6 1987 Competition by omega-6 fatty acids with retinoic acid for CRABP may neutralize the binding protein-mediated biological functions of retinoic acid, and could thereby enhance tumor production. Tretinoin 132-145 cellular retinoic acid binding protein 1 Homo sapiens 58-63 3007157-3 1986 The presence of cellular retinoic acid binding protein (cRABP) was indicated by the cellular uptake of [3H]all-trans-retinoic acid. Tretinoin 110-130 cellular retinoic acid binding protein 1 Homo sapiens 16-54 3035450-1 1987 Binding proteins for retinoic acid (cellular retinoic acid binding protein, CRABP) have been demonstrated in various cell types, and display the characteristics of receptors. Tretinoin 21-34 cellular retinoic acid binding protein 1 Homo sapiens 76-81 2425004-2 1986 A 200% increase in CRABP levels, measured by the ability of the protein to bind retinoic acid, was observed in the normal skin during treatment. Tretinoin 80-93 cellular retinoic acid binding protein 1 Homo sapiens 19-24 3031026-1 1987 F9 teratocarcinoma cells contain a cellular retinoic acid-binding protein (CRABP) that may mediate the retinoic acid-induced differentiation of this cell line. Tretinoin 44-57 cellular retinoic acid binding protein 1 Homo sapiens 75-80 3031026-2 1987 Specific [3H]retinoic acid binding to CRABP in F9 stem cell cytosol is protein-dependent, reaches equilibrium within 4 h at 4 degrees C, and yields 643 +/- 105 fmol of [3H]retinoic acid per mg of protein with an apparent dissociation constant of 9.2 +/- 1.1 nM. Tretinoin 13-26 cellular retinoic acid binding protein 1 Homo sapiens 38-43 3031026-2 1987 Specific [3H]retinoic acid binding to CRABP in F9 stem cell cytosol is protein-dependent, reaches equilibrium within 4 h at 4 degrees C, and yields 643 +/- 105 fmol of [3H]retinoic acid per mg of protein with an apparent dissociation constant of 9.2 +/- 1.1 nM. Tretinoin 172-185 cellular retinoic acid binding protein 1 Homo sapiens 38-43 3031026-4 1987 The effect of these drugs on CRABP activity is both time and concentration-dependent, resulting in an increase in the number of binding sites for [3H]retinoic acid with no change in their affinity. Tretinoin 150-163 cellular retinoic acid binding protein 1 Homo sapiens 29-34 2833143-2 1987 Studies on CRBP and CRABP suggest that both retinol and retinoic acid are involved in maintaining testicular function. Tretinoin 56-69 cellular retinoic acid binding protein 1 Homo sapiens 20-25 3015289-2 1986 Intracellular metabolism is complex and involves the binding to specific receptors for retinol (CRBP) and retinoic acid (CRABP) followed by a nuclear translocation. Tretinoin 106-119 cellular retinoic acid binding protein 1 Homo sapiens 121-126 3007157-3 1986 The presence of cellular retinoic acid binding protein (cRABP) was indicated by the cellular uptake of [3H]all-trans-retinoic acid. Tretinoin 110-130 cellular retinoic acid binding protein 1 Homo sapiens 56-61 2427593-4 1986 Since psoriatic plaques are particularly responsive to systemic retinoids, specifically to retinoic acid analogues, our results suggest for the first time a link between the levels of CRABP and the responsiveness of a nonneoplastic hyperproliferative tissue to systemic administration of retinoids in the human. Tretinoin 91-104 cellular retinoic acid binding protein 1 Homo sapiens 184-189 2992894-6 1985 Retinol and RA might be translocated to nuclei by their respective binding proteins [cellular retinol-binding protein (CRBP) and cellular retinoic acid-binding protein (CRABP)]: isolated EC nuclei have specific, independent binding sites for both holoproteins but not their ligands. Tretinoin 12-14 cellular retinoic acid binding protein 1 Homo sapiens 129-167 2995045-1 1985 The cellular content of receptors for retinol (CRBP) and retinoic acid (CRABP) was measured in 148 human mammary carcinomas. Tretinoin 57-70 cellular retinoic acid binding protein 1 Homo sapiens 72-77 2992894-6 1985 Retinol and RA might be translocated to nuclei by their respective binding proteins [cellular retinol-binding protein (CRBP) and cellular retinoic acid-binding protein (CRABP)]: isolated EC nuclei have specific, independent binding sites for both holoproteins but not their ligands. Tretinoin 12-14 cellular retinoic acid binding protein 1 Homo sapiens 169-174 6090748-7 1984 These results indicate that RA resistance in these sublines is not secondary to a defect of RA uptake or of binding of RA to cRABP; the resistance may result from a defect distal to binding to cRABP, or alternatively, cRABP may not mediate this effect of RA. Tretinoin 28-30 cellular retinoic acid binding protein 1 Homo sapiens 193-198 6090748-7 1984 These results indicate that RA resistance in these sublines is not secondary to a defect of RA uptake or of binding of RA to cRABP; the resistance may result from a defect distal to binding to cRABP, or alternatively, cRABP may not mediate this effect of RA. Tretinoin 28-30 cellular retinoic acid binding protein 1 Homo sapiens 193-198 6306117-7 1983 Retinoic acid, which binds to CRABP but not CRBP, induces differentiation of teratocarcinoma cells. Tretinoin 0-13 cellular retinoic acid binding protein 1 Homo sapiens 30-35 6310582-8 1983 Thus, although CRABP is not necessarily correlated with growth inhibition in monolayer culture, it is associated with retinoic acid"s ability to inhibit neuroblastoma colony formation in soft agar. Tretinoin 118-131 cellular retinoic acid binding protein 1 Homo sapiens 15-20 6310582-4 1983 All five lines contain significant levels of cytosolic CRABP (2.5-7.5 pmol/mg of protein), which display typical properties of specific high affinity retinoic acid binding, a sedimentation coefficient of 2 S, and inhibition by PCMBS. Tretinoin 150-163 cellular retinoic acid binding protein 1 Homo sapiens 55-60 6942700-9 1981 A number of tissues of rats, humans, and other species contain soluble proteins with binding specificity for retinol (CRBP) or for retinoic acid (CRABP). Tretinoin 131-144 cellular retinoic acid binding protein 1 Homo sapiens 146-151 6684744-6 1983 CRBP and CRABP are assumed to be mediating factors for the retinol and retinoic acid action. Tretinoin 71-84 cellular retinoic acid binding protein 1 Homo sapiens 9-14 6684744-7 1983 Since the presence of CRABP is a constant finding, we propose that retinoic acid and its synthetic derivatives with high affinity for CRABP could be appropriate antineoplastic drugs in these tissues. Tretinoin 67-80 cellular retinoic acid binding protein 1 Homo sapiens 22-27 6684744-7 1983 Since the presence of CRABP is a constant finding, we propose that retinoic acid and its synthetic derivatives with high affinity for CRABP could be appropriate antineoplastic drugs in these tissues. Tretinoin 67-80 cellular retinoic acid binding protein 1 Homo sapiens 134-139 6299278-1 1982 Cellular retinoic acid-binding protein (CRABP) was detected in the nuclear fraction of N-methyl-N-nitrosourea-induced mammary cancers after the incubation of cytosol containing [3H]retinoic acid (RA)-bound CRABP with isolated nuclei. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 40-45 6299278-1 1982 Cellular retinoic acid-binding protein (CRABP) was detected in the nuclear fraction of N-methyl-N-nitrosourea-induced mammary cancers after the incubation of cytosol containing [3H]retinoic acid (RA)-bound CRABP with isolated nuclei. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 206-211 6279709-4 1982 A number of tissues of rats, humans, and other species contain soluble binding proteins with specificity for either retinol (cellular retinol-binding protein, CRBP) or retinoic acid (cellular retinoic acid-binding protein, CRABP). Tretinoin 168-181 cellular retinoic acid binding protein 1 Homo sapiens 223-228 89058-4 1979 In addition to cellular retinol-binding protein (CRBP) and retinoic acid-binding protein (CRABP), a new molecular species having affinity for both retinol and retinoic acid was detected in the cytosols obtained from hepatocellular carcinoma as well as glioma by means of gel filtration on Sephadex G-75. Tretinoin 59-72 cellular retinoic acid binding protein 1 Homo sapiens 90-95 6258773-1 1980 Blinded analyses of the concentrations of binding proteins for retinol and retinoic acid (CRABP) in homogenates of cancer and normal tissue aliquots obtained from human cervix, endometrium, ovary, breast, and lung were carried out by the sucrose gradient ultracentrifugation technique. Tretinoin 75-88 cellular retinoic acid binding protein 1 Homo sapiens 90-95 6258776-3 1980 This technique allows, after incubation with tritiated retinoic acid (RA) overnight, the separation of the specific CRABP activity from the nonspecific serum-originated binding activity and from the free RA. Tretinoin 55-68 cellular retinoic acid binding protein 1 Homo sapiens 116-121 6258776-3 1980 This technique allows, after incubation with tritiated retinoic acid (RA) overnight, the separation of the specific CRABP activity from the nonspecific serum-originated binding activity and from the free RA. Tretinoin 70-72 cellular retinoic acid binding protein 1 Homo sapiens 116-121 7193082-1 1980 Human colon adenocarcinomas and adjacent non-cancerous, normal colon from the same patient were assayed for the presence and amounts of cellular binding proteins for retinol (CRBP) and retinoic acid (CRABP) by sucrose gradient analysis. Tretinoin 185-198 cellular retinoic acid binding protein 1 Homo sapiens 200-205 31728066-0 2019 Publisher Correction: A new regulatory mechanism for Raf kinase activation, retinoic acid-bound Crabp1. Tretinoin 76-89 cellular retinoic acid binding protein 1 Homo sapiens 96-102 32527063-3 2020 Retinoic acid (RA)/sonic hedgehog (Shh)-induced embryonic stem cells differentiation into motor neurons are employed to study up-regulation of Crabp1 by Shh. Tretinoin 0-13 cellular retinoic acid binding protein 1 Homo sapiens 143-149 32527063-3 2020 Retinoic acid (RA)/sonic hedgehog (Shh)-induced embryonic stem cells differentiation into motor neurons are employed to study up-regulation of Crabp1 by Shh. Tretinoin 15-17 cellular retinoic acid binding protein 1 Homo sapiens 143-149 33832420-1 2021 Retinoic acid (RA) binding proteins, CRABP1 and CRABP2, are molecular chaperones that mediate intracellular activity of RA, the key promoter of cell differentiation with tumor suppressor activity. Tretinoin 0-13 cellular retinoic acid binding protein 1 Homo sapiens 37-43 33832420-1 2021 Retinoic acid (RA) binding proteins, CRABP1 and CRABP2, are molecular chaperones that mediate intracellular activity of RA, the key promoter of cell differentiation with tumor suppressor activity. Tretinoin 15-17 cellular retinoic acid binding protein 1 Homo sapiens 37-43 33832420-3 2021 The functions of CRABP1 are less studied but are apparently associated with sequestration of RA in cytoplasm and limitation of its transcriptional activity, suggesting involvement of this protein in the development of RA resistance. Tretinoin 93-95 cellular retinoic acid binding protein 1 Homo sapiens 17-23 33832420-8 2021 Moreover, suppression of the CRABP1 level in both RA-sensitive and RA-resistant cells was shown in the cells with cells with knockdown of CRABP2 gene. Tretinoin 50-52 cellular retinoic acid binding protein 1 Homo sapiens 29-35 31358819-0 2019 A new regulatory mechanism for Raf kinase activation, retinoic acid-bound Crabp1. Tretinoin 54-67 cellular retinoic acid binding protein 1 Homo sapiens 74-80 31358819-3 2019 We recently reported that all-trans retinoic acid (atRA) rapidly (within minutes) activates Erk1/2 to modulate cell cycle progression in stem cells, which is mediated by cellular retinoic acid binding protein 1 (Crabp1). Tretinoin 26-49 cellular retinoic acid binding protein 1 Homo sapiens 170-210 31358819-3 2019 We recently reported that all-trans retinoic acid (atRA) rapidly (within minutes) activates Erk1/2 to modulate cell cycle progression in stem cells, which is mediated by cellular retinoic acid binding protein 1 (Crabp1). Tretinoin 26-49 cellular retinoic acid binding protein 1 Homo sapiens 212-218 31358819-3 2019 We recently reported that all-trans retinoic acid (atRA) rapidly (within minutes) activates Erk1/2 to modulate cell cycle progression in stem cells, which is mediated by cellular retinoic acid binding protein 1 (Crabp1). Tretinoin 51-55 cellular retinoic acid binding protein 1 Homo sapiens 170-210 31358819-3 2019 We recently reported that all-trans retinoic acid (atRA) rapidly (within minutes) activates Erk1/2 to modulate cell cycle progression in stem cells, which is mediated by cellular retinoic acid binding protein 1 (Crabp1). Tretinoin 51-55 cellular retinoic acid binding protein 1 Homo sapiens 212-218 31358819-7 2019 However, Crabp1 can also compete with Ras for direct interaction with the RBD of Raf, thereby negatively modulating growth factor-stimulated Raf activation, which can be enhanced by atRA binding to Crabp1. Tretinoin 182-186 cellular retinoic acid binding protein 1 Homo sapiens 9-15 31358819-7 2019 However, Crabp1 can also compete with Ras for direct interaction with the RBD of Raf, thereby negatively modulating growth factor-stimulated Raf activation, which can be enhanced by atRA binding to Crabp1. Tretinoin 182-186 cellular retinoic acid binding protein 1 Homo sapiens 198-204 30728260-8 2019 In summary, our study demonstrates that CRABPs serve as an on-off switch that modulates the efficiency of the HCV life cycle and elucidates how HCV evades the antiviral properties of ATRA via the exploitation of CRABP1 functionality.IMPORTANCE ATRA, a biologically active metabolite of vitamin A, exerts pleiotropic biological effects, including the activation of both innate and adaptive immunity, thereby serving as a potent antimicrobial compound against numerous viral pathogens. Tretinoin 183-187 cellular retinoic acid binding protein 1 Homo sapiens 212-218 30728260-8 2019 In summary, our study demonstrates that CRABPs serve as an on-off switch that modulates the efficiency of the HCV life cycle and elucidates how HCV evades the antiviral properties of ATRA via the exploitation of CRABP1 functionality.IMPORTANCE ATRA, a biologically active metabolite of vitamin A, exerts pleiotropic biological effects, including the activation of both innate and adaptive immunity, thereby serving as a potent antimicrobial compound against numerous viral pathogens. Tretinoin 244-248 cellular retinoic acid binding protein 1 Homo sapiens 212-218 30728260-10 2019 Here, we discovered that the hepatocellular response to ATRA creates either a proviral or an antiviral environment depending on its engagement with CRABP1 or -2, respectively. Tretinoin 56-60 cellular retinoic acid binding protein 1 Homo sapiens 148-154 27242163-3 2016 Immunocytochemistry was used to localize different components of RA signaling within sections of the retina and optic tectum, namely, the synthetic enzyme retinaldehyde dehydrogenase (RALDH), the RA binding proteins CRABPI and II, the retinoic acid receptors RARalpha, beta and gamma, and finally the catabolic enzyme CYP26A1. Tretinoin 65-67 cellular retinoic acid binding protein 1 Homo sapiens 216-222 30322383-2 2018 In addition to nuclear receptors, there are other intracellular RA binding proteins such as cellular retinoic acid binding proteins (CRABP1 and CRABP2) and cytochrome P450 (CYP) enzymes, whose contributions to the RA signaling pathway have not been fully understood. Tretinoin 64-66 cellular retinoic acid binding protein 1 Homo sapiens 133-139 27435798-0 2016 Corrigendum: All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation. Tretinoin 17-36 cellular retinoic acid binding protein 1 Homo sapiens 95-101 27416800-3 2016 atRA bound to CRABPs (holo-CRABP) was efficiently metabolized by CYP26B1. Tretinoin 0-4 cellular retinoic acid binding protein 1 Homo sapiens 14-19 26935534-0 2016 All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation. Tretinoin 4-23 cellular retinoic acid binding protein 1 Homo sapiens 82-88 26935534-6 2016 Re-expressing Crabp1 in Crabp1-negative cancer cells also sensitizes their apoptotic induction by atRA. Tretinoin 98-102 cellular retinoic acid binding protein 1 Homo sapiens 14-20 26935534-6 2016 Re-expressing Crabp1 in Crabp1-negative cancer cells also sensitizes their apoptotic induction by atRA. Tretinoin 98-102 cellular retinoic acid binding protein 1 Homo sapiens 24-30 26935534-7 2016 This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction, and provides a new cancer therapeutic strategy whereby compounds specifically targeting Crabp1 can modulate cell cycle and cancer cell apoptosis in a RAR-independent fashion, thereby avoiding atRA"s toxicity caused by its genomic effects. Tretinoin 74-78 cellular retinoic acid binding protein 1 Homo sapiens 92-98 26935534-7 2016 This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction, and provides a new cancer therapeutic strategy whereby compounds specifically targeting Crabp1 can modulate cell cycle and cancer cell apoptosis in a RAR-independent fashion, thereby avoiding atRA"s toxicity caused by its genomic effects. Tretinoin 74-78 cellular retinoic acid binding protein 1 Homo sapiens 250-256 26142905-0 2015 CRABP1 is associated with a poor prognosis in breast cancer: adding to the complexity of breast cancer cell response to retinoic acid. Tretinoin 120-133 cellular retinoic acid binding protein 1 Homo sapiens 0-6 27830500-5 2016 Intracellular retinoic acid binding-proteins (CRABP1 and 2, and FABP5) seem to have more diverse functions distinctive to each, such as directing retinoic acid to catabolism, delivering retinoic acid to specific nuclear receptors, and generating non-canonical actions. Tretinoin 14-27 cellular retinoic acid binding protein 1 Homo sapiens 46-58 27830500-5 2016 Intracellular retinoic acid binding-proteins (CRABP1 and 2, and FABP5) seem to have more diverse functions distinctive to each, such as directing retinoic acid to catabolism, delivering retinoic acid to specific nuclear receptors, and generating non-canonical actions. Tretinoin 146-159 cellular retinoic acid binding protein 1 Homo sapiens 46-58 27830500-5 2016 Intracellular retinoic acid binding-proteins (CRABP1 and 2, and FABP5) seem to have more diverse functions distinctive to each, such as directing retinoic acid to catabolism, delivering retinoic acid to specific nuclear receptors, and generating non-canonical actions. Tretinoin 146-159 cellular retinoic acid binding protein 1 Homo sapiens 46-58 26142905-13 2015 We demonstrate that CRABP1 expression attenuates RA-induced cell growth arrest and inhibits RA signalling in breast cancer cells by sequestering RA in the cytoplasm. Tretinoin 49-51 cellular retinoic acid binding protein 1 Homo sapiens 20-26 26142905-13 2015 We demonstrate that CRABP1 expression attenuates RA-induced cell growth arrest and inhibits RA signalling in breast cancer cells by sequestering RA in the cytoplasm. Tretinoin 49-51 cellular retinoic acid binding protein 1 Homo sapiens 20-26 26142905-17 2015 We propose that these three RA-binding proteins can serve as biomarkers for predicting triple-negative breast cancer response to RA, with elevated levels of either cytoplasmic CRABP1 or FABP5 associated with RA resistance, and elevated levels of nuclear CRABP2 associated with sensitivity to RA. Tretinoin 28-30 cellular retinoic acid binding protein 1 Homo sapiens 176-182 21435396-2 2012 In cytoplasm, RA binds specifically to cellular retinoic acid binding proteins I (CRABPI), and II. Tretinoin 14-16 cellular retinoic acid binding protein 1 Homo sapiens 39-80 22982089-3 2013 In this study, we have found that cellular retinoic acid binding protein I (CRABPI) mediates the non-canonical, RAR- and membrane signal-independent activation of ERK1/2 by atRA in various cellular backgrounds. Tretinoin 173-177 cellular retinoic acid binding protein 1 Homo sapiens 34-74 22982089-3 2013 In this study, we have found that cellular retinoic acid binding protein I (CRABPI) mediates the non-canonical, RAR- and membrane signal-independent activation of ERK1/2 by atRA in various cellular backgrounds. Tretinoin 173-177 cellular retinoic acid binding protein 1 Homo sapiens 76-82 22658364-3 2012 As a CRABP-II-recognizing moiety, all-trans retinoic acid (ATRA, 3), a physiological ligand of CRABP, was chosen. Tretinoin 44-57 cellular retinoic acid binding protein 1 Homo sapiens 5-10 22658364-3 2012 As a CRABP-II-recognizing moiety, all-trans retinoic acid (ATRA, 3), a physiological ligand of CRABP, was chosen. Tretinoin 59-63 cellular retinoic acid binding protein 1 Homo sapiens 5-10 24294399-8 2013 Expression of cellular retinoic acid Binding Protein, CRABP-1 in whole ovarian cancer tissue sections was higher than in the TMA tissue cores. Tretinoin 23-36 cellular retinoic acid binding protein 1 Homo sapiens 54-61 21435396-2 2012 In cytoplasm, RA binds specifically to cellular retinoic acid binding proteins I (CRABPI), and II. Tretinoin 14-16 cellular retinoic acid binding protein 1 Homo sapiens 82-88 19636436-9 2009 However, expression of E-cadherin, RAR, and CRABP increased upon ATRA treatment. Tretinoin 65-69 cellular retinoic acid binding protein 1 Homo sapiens 44-49 21270509-9 2011 CONCLUSIONS: The findings of differential expression of CRABP1 in prolactinomas and of RERG in NFPA compared to normal pituitary suggests that retinoic acid and estrogen receptor, respectively, could be involved in the tumorigenesis of these adenomas subtypes. Tretinoin 143-156 cellular retinoic acid binding protein 1 Homo sapiens 56-62 20501978-9 2010 We propose other candidates such as STRA6, LRAT, CRBP1, CRBP2 and CRABP1 are directly implicated in retinoic acid metabolism. Tretinoin 100-113 cellular retinoic acid binding protein 1 Homo sapiens 66-72 20552429-4 2010 This method uses cellular retinoic acid-binding protein I (CRABP-I), a protein that binds RA with high affinity and specificity, as a "read-out" for its ligand. Tretinoin 60-62 cellular retinoic acid binding protein 1 Homo sapiens 17-57 19087254-12 2008 This consequently reduced all-trans retinoic acid (RA)-induced differentiation, validated by CRABP1 knock down, which led to recovery of the cellular response to RA treatment and cellular sprouting under physiological RA concentrations. Tretinoin 26-49 cellular retinoic acid binding protein 1 Homo sapiens 93-99 19087254-12 2008 This consequently reduced all-trans retinoic acid (RA)-induced differentiation, validated by CRABP1 knock down, which led to recovery of the cellular response to RA treatment and cellular sprouting under physiological RA concentrations. Tretinoin 51-53 cellular retinoic acid binding protein 1 Homo sapiens 93-99 18805411-3 2008 We show that cellular RA-binding proteins CRABP1 and CRABP2 and the fatty acid-binding protein FABP5 are dynamically expressed during skin development and in adult tissue. Tretinoin 22-24 cellular retinoic acid binding protein 1 Homo sapiens 42-48 16919229-3 2006 We describe a fluorescence-based method for quantitating RA that takes advantage of the high affinity and selectivity of the intracellular lipid-binding protein termed CRABP-I and CRABP-II and that uses them as RA sensors. Tretinoin 57-59 cellular retinoic acid binding protein 1 Homo sapiens 168-175 16316409-8 2005 As CRABPI was elevated far more than any other genes, we observed that the retinoids, all-trans retinoic acid and 9-cis retinoic acid, that bind CRABPI, promoted nitroblue tetrazolium-associated functional cell differentiation in p75NTR PC-3 cells, but not in neo control PC-3 cells. Tretinoin 96-109 cellular retinoic acid binding protein 1 Homo sapiens 145-151 16316409-8 2005 As CRABPI was elevated far more than any other genes, we observed that the retinoids, all-trans retinoic acid and 9-cis retinoic acid, that bind CRABPI, promoted nitroblue tetrazolium-associated functional cell differentiation in p75NTR PC-3 cells, but not in neo control PC-3 cells. Tretinoin 96-109 cellular retinoic acid binding protein 1 Homo sapiens 3-9 14713576-0 2003 CRABP I expression and the mediation of the sensitivity of human tumour cells to retinoic acid and irradiation. Tretinoin 81-94 cellular retinoic acid binding protein 1 Homo sapiens 0-7 15907702-1 2005 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin 21-34 cellular retinoic acid binding protein 1 Homo sapiens 43-83 15907702-1 2005 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin 21-34 cellular retinoic acid binding protein 1 Homo sapiens 85-92 15907702-1 2005 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin 36-38 cellular retinoic acid binding protein 1 Homo sapiens 43-83 15907702-1 2005 Binding of all-trans Retinoic Acid (RA) to Cellular Retinoic Acid Binding Protein I (CRABP I) does not result in significant changes of the protein tertiary structure, even though the binding site is inaccessible in a static apo-protein conformation. Tretinoin 36-38 cellular retinoic acid binding protein 1 Homo sapiens 85-92 15907702-3 2005 In this work, RA binding to CRABP I is studied in dilute solutions (low micro-molar range), where no dimer and/or oligomer formation occurs. Tretinoin 14-16 cellular retinoic acid binding protein 1 Homo sapiens 28-35 12941622-4 2003 At all sites, expression of additional RA signaling molecules (RARalpha, RARbeta, RXR, CRABP1) depends on M/E interactions. Tretinoin 39-41 cellular retinoic acid binding protein 1 Homo sapiens 87-93 15281009-1 2004 The aim of this study was to confirm if catabolism of all-trans retinoic acid (RA) is enhanced by type I cellular retinoic acid binding protein (CRABP-I) expression and to investigate the effect of this enhanced catabolism on cell proliferation of the head and neck squamous cell carcinoma (HNSCC) cell line, AMC-HN-7. Tretinoin 64-77 cellular retinoic acid binding protein 1 Homo sapiens 145-152 15281009-1 2004 The aim of this study was to confirm if catabolism of all-trans retinoic acid (RA) is enhanced by type I cellular retinoic acid binding protein (CRABP-I) expression and to investigate the effect of this enhanced catabolism on cell proliferation of the head and neck squamous cell carcinoma (HNSCC) cell line, AMC-HN-7. Tretinoin 114-127 cellular retinoic acid binding protein 1 Homo sapiens 145-152 14713576-6 2003 RESULTS: The basal CRABP I level clearly correlated with the clonogenic survival of tumour cells and normal fibroblasts after treatment with retinoic acid and ionizing irradiation (IR). Tretinoin 141-154 cellular retinoic acid binding protein 1 Homo sapiens 19-26 14713576-7 2003 Cells expressing high basal CRABP I were more resistant to combined retinoic acid radiation treatment than cells with low basal expression. Tretinoin 68-81 cellular retinoic acid binding protein 1 Homo sapiens 28-35 14713576-8 2003 Overexpression of CRABP I in retinoic acid-sensitive HTB35 cells induced a retinoic acid-insensitive phenotype resistant to combined treatment with retinoic acid and radiation. Tretinoin 29-42 cellular retinoic acid binding protein 1 Homo sapiens 18-25 14713576-10 2003 CRABP I overexpression resulted in stimulated cyclin D1 expression indicating the dependency of this cell cycle control protein on retinoic acid metabolism. Tretinoin 131-144 cellular retinoic acid binding protein 1 Homo sapiens 0-7 14713576-11 2003 CONCLUSION: CRABP I plays an important role not only in mediating the retinoid effects, but also in modulating the radiation sensitivity of tumour cells after combined retinoic acid radiation treatment. Tretinoin 168-181 cellular retinoic acid binding protein 1 Homo sapiens 12-19 14585314-10 2003 Recent studies proved that the control occurs by different expressions of retinoid receptors as well as by time-dependent changes of the vitamin-A-metabolism respectively via cellular vitamin-A-binding proteins (CRBP: cytoplasmatic retinol binding protein; CRABP: cytoplasmatic retinoic acid binding protein). Tretinoin 278-291 cellular retinoic acid binding protein 1 Homo sapiens 257-262 14713576-1 2003 PURPOSE: To examine the role cytoplasmic retinoic acid binding protein type 1 (CRABP I) and retinoic acid receptor beta 2 (RAR-beta 2) in mediating radiosensitization of human tumour cells in vitro by retinoic acid. Tretinoin 41-54 cellular retinoic acid binding protein 1 Homo sapiens 79-86 14713576-5 2003 The retinoic acid-sensitive cell line HTB35 was transfected for inducible CRABP I overexpression to test the role of this protein in modulating the sensitivity to retinoic acid and radiation as well as in regulating RAR-beta 2 and cyclin D1 expression. Tretinoin 4-17 cellular retinoic acid binding protein 1 Homo sapiens 74-81 12844477-6 2003 Indinavir leads to altered retinoic acid signaling most likely by an activation of the RAR/RXR heterodimer, perhaps by displacing all-trans-retinoic acid from CRABP. Tretinoin 27-40 cellular retinoic acid binding protein 1 Homo sapiens 159-164 11027136-1 2000 Cellular retinoic acid-binding proteins I and II (CRABP-I and -II, respectively) are transport proteins for all-trans-retinoic acid (RA), an active metabolite of vitamin A (retinol), and have been reported to be directly involved in the metabolism of RA. Tretinoin 133-135 cellular retinoic acid binding protein 1 Homo sapiens 50-65 11437413-3 2001 BHY cells expressed all of retinoid nuclear receptors (RARalpha, beta, gamma, and RXRalpha) and cytoplasmic retinoic acid binding proteins (CRABP1 and CRABP2). Tretinoin 108-121 cellular retinoic acid binding protein 1 Homo sapiens 140-146 11162104-1 2001 The pleiotropic effects of retinoic acid (RA) in mammalian cells are mediated by two classes of proteins: the retinoic acid receptors (RAR), and cellular retinoic acid binding proteins (CRABP-I and CRABP-II). Tretinoin 27-40 cellular retinoic acid binding protein 1 Homo sapiens 186-193 11162104-1 2001 The pleiotropic effects of retinoic acid (RA) in mammalian cells are mediated by two classes of proteins: the retinoic acid receptors (RAR), and cellular retinoic acid binding proteins (CRABP-I and CRABP-II). Tretinoin 42-44 cellular retinoic acid binding protein 1 Homo sapiens 186-193 11133659-3 2001 Three proteins involved in 1) serum transport of retinol (retinol binding protein [RBP]), 2) cellular transport and metabolism of retinol (cellular RBP [CRBP] I), and 3) retinoic acid (cellular retinoic acid binding protein [CRABP] I), respectively, have been located by immunohistochemistry during gestation in the porcine placenta. Tretinoin 170-183 cellular retinoic acid binding protein 1 Homo sapiens 185-223 11914476-6 2001 Since retinoic acid inhibits the secretion of parathyroid hormone and CRABP I is thought to play a key role in regulating the amount of retinoic acid available to interact with specific nuclear receptors, these data may suggest impaired transport of retinoic acid to cell nuclei, thus contributing to the development of hyperparathyroidism. Tretinoin 6-19 cellular retinoic acid binding protein 1 Homo sapiens 70-77 11914476-6 2001 Since retinoic acid inhibits the secretion of parathyroid hormone and CRABP I is thought to play a key role in regulating the amount of retinoic acid available to interact with specific nuclear receptors, these data may suggest impaired transport of retinoic acid to cell nuclei, thus contributing to the development of hyperparathyroidism. Tretinoin 136-149 cellular retinoic acid binding protein 1 Homo sapiens 70-77 11914476-6 2001 Since retinoic acid inhibits the secretion of parathyroid hormone and CRABP I is thought to play a key role in regulating the amount of retinoic acid available to interact with specific nuclear receptors, these data may suggest impaired transport of retinoic acid to cell nuclei, thus contributing to the development of hyperparathyroidism. Tretinoin 136-149 cellular retinoic acid binding protein 1 Homo sapiens 70-77 11266607-3 2001 Photoaffinity labeling of purified CRABPs with [(3)H]atRA was light- and concentration-dependent, saturable, and protected by several retinoids in a concentration-dependent manner, indicating that binding occurred in the CRABP atRA-binding site. Tretinoin 53-57 cellular retinoic acid binding protein 1 Homo sapiens 35-40 11266607-10 2001 Therefore, photoaffinity labeling with [(3)H]atRA can be used to identify new ligands for CRABP and retinoid nuclear receptors and also provide information concerning the identity of amino acid(s) localized in the atRA-binding site of these proteins. Tretinoin 45-49 cellular retinoic acid binding protein 1 Homo sapiens 90-95 12034496-1 2002 Members of the cellular retinoic acid (CRABP) and retinol binding (CRBP) proteins family are involved in the metabolic pathways of retinoic acid (RA) and retinal respectively. Tretinoin 24-37 cellular retinoic acid binding protein 1 Homo sapiens 39-44 12034496-1 2002 Members of the cellular retinoic acid (CRABP) and retinol binding (CRBP) proteins family are involved in the metabolic pathways of retinoic acid (RA) and retinal respectively. Tretinoin 131-144 cellular retinoic acid binding protein 1 Homo sapiens 39-44 11994141-0 2002 Topical retinoic acid alters the expression of cellular retinoic acid-binding protein-I and cellular retinoic acid-binding protein-II in non-lesional but not lesional psoriatic skin. Tretinoin 8-21 cellular retinoic acid binding protein 1 Homo sapiens 47-133 11027136-0 2000 Direct photoaffinity labeling of cellular retinoic acid-binding protein I (CRABP-I) with all-trans-retinoic acid: identification of amino acids in the ligand binding site. Tretinoin 92-112 cellular retinoic acid binding protein 1 Homo sapiens 33-73 11027136-0 2000 Direct photoaffinity labeling of cellular retinoic acid-binding protein I (CRABP-I) with all-trans-retinoic acid: identification of amino acids in the ligand binding site. Tretinoin 92-112 cellular retinoic acid binding protein 1 Homo sapiens 75-82 11027136-1 2000 Cellular retinoic acid-binding proteins I and II (CRABP-I and -II, respectively) are transport proteins for all-trans-retinoic acid (RA), an active metabolite of vitamin A (retinol), and have been reported to be directly involved in the metabolism of RA. Tretinoin 9-22 cellular retinoic acid binding protein 1 Homo sapiens 50-65 11027136-1 2000 Cellular retinoic acid-binding proteins I and II (CRABP-I and -II, respectively) are transport proteins for all-trans-retinoic acid (RA), an active metabolite of vitamin A (retinol), and have been reported to be directly involved in the metabolism of RA. Tretinoin 112-131 cellular retinoic acid binding protein 1 Homo sapiens 50-65 11027136-3 2000 Photoaffinity labeling of CRABP-I with [(3)H]RA was light- and concentration-dependent and was protected by unlabeled RA and various retinoids, indicating that the labeling was directed to the RA-binding site. Tretinoin 45-47 cellular retinoic acid binding protein 1 Homo sapiens 26-33 11027136-3 2000 Photoaffinity labeling of CRABP-I with [(3)H]RA was light- and concentration-dependent and was protected by unlabeled RA and various retinoids, indicating that the labeling was directed to the RA-binding site. Tretinoin 45-47 cellular retinoic acid binding protein 1 Homo sapiens 26-33