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1 CRABP(II) expression was shown to be induced in the uter
2 CRABP-II thus facilitates the ligation of RAR and marked
3 CRABPs are members of the superfamily of lipid binding p
6 o measured binding of FA to a retinoic acid (CRABP-I) and a retinol (CRBP-II) binding protein and we
7 production by uterine epithelial cells [and CRABP(II) expression] was also observed if the prepubert
8 etabolism between cells expressing CRABP and CRABP(II) and suggests CRABP(II) may participate in reti
9 ir isoelectric point showed both CRABP I and CRABP II to be present in the cerebellum and P19 cells,
11 retinoic acid-binding proteins (CRABP-I and CRABP-II), a nuclear retinoic acid receptor (RAR alpha),
15 ng functional difference between CRABP-I and CRABP-II, and point at a novel mechanism by which the tr
16 retinoic acid binding proteins, CRABP-I and CRABP-II, and the purified heterocomplexes indicate that
18 lative dissociation constant of CRABP-II and CRABP-I (Kd (CRABP-II)/Kd (CRABP-I)) was determined to b
20 Additional observations demonstrate that apo-CRABP-II is associated with endoplasmic reticulum (ER),
21 nt samples, there was no association between CRABP-H mRNA expression level and APL cellular sensitivi
22 eal a striking functional difference between CRABP-I and CRABP-II, and point at a novel mechanism by
26 rding to their isoelectric point showed both CRABP I and CRABP II to be present in the cerebellum and
31 n Cooperative Oncology Group protocol E2491, CRABP-II mRNA was modestly increased from day 0 values i
32 with PMSG, cells previously shown to express CRABP(II) and confirmed here to continue to express it i
35 larly, injection of an adenovirus expressing CRABP-II into mammary carcinomas that spontaneously deve
36 retinoid metabolism between cells expressing CRABP and CRABP(II) and suggests CRABP(II) may participa
39 l uteri [shown previously to be negative for CRABP(II)] or by smooth muscle and stromal cells taken f
40 earch for a biologically meaningful role for CRABP-II, we examined its effect on RA-induced growth in
41 r movement of RA from CRABP-II, but not from CRABP-I, to RAR strongly depended on the concentration o
42 The data suggest that transfer of RA from CRABP-I to RAR involves dissociation of the ligand from
44 The rate constant for movement of RA from CRABP-II, but not from CRABP-I, to RAR strongly depended
45 model revealed that the change stemmed from CRABP-I/CRABP-II substitution of three spatially aligned
48 d is a proapoptotic agent in cells with high CRABP-II/FABP5 ratio, but it signals through PPARbeta/de
49 acid residues in CRABP-II to the homologous CRABP-I residues resulted in loss of the ability of CRAB
50 of cellular retinoic acid-binding protein I (CRABP I) in the RA signaling was investigated by examini
51 he cellular retinoic acid binding protein I (CRABP I) occurs via a flexible portal region, which func
52 an cellular retinoic acid-binding protein I (CRABP I) was mutated to incorporate in a surface-exposed
53 n, cellular retinoic acid-binding protein I (CRABP I), in the presence of an inert crowding agent (Fi
56 evealed that the change stemmed from CRABP-I/CRABP-II substitution of three spatially aligned residue
57 lar retinoic acid-binding proteins I and II (CRABP-I and -II, respectively) are transport proteins fo
58 Cellular retinoic acid-binding protein II (CRABP-II) is an intracellular lipid-binding protein that
59 Cellular retinoic acid-binding protein II (CRABP-II) undergoes nuclear translocation upon binding o
60 f cellular retinoic acid binding protein-II (CRABP-II) has been invoked as an important mechanism of
62 roteins cellular RA binding protein type II (CRABP-II) and fatty acid binding protein type 5 in adipo
63 cellular retinoic acid-binding protein (II) (CRABP(II)) may have a role in the movement of retinoic a
66 ed arginine residues (Arg-111 and Arg-131 in CRABP-I; Arg-111 and Arg-132 in CRABP-II) that interact
67 d Arg-131 in CRABP-I; Arg-111 and Arg-132 in CRABP-II) that interact with the carboxyl group of retin
69 ingly, these turns are on linked hairpins in CRABP I and represent the best-conserved turns in the iL
70 e peptides, encompassing turns III and IV in CRABP I, have a strong intrinsic bias to form native tur
71 ; range, 0.16-4.13) relative to the level in CRABP-H protein-expressing NB4 cells (arbitrarily set at
72 ely, converting these amino acid residues in CRABP-II to the homologous CRABP-I residues resulted in
73 , our data strongly imply that variations in CRABP-II expression and RA binding activity are not caus
75 ween RARgamma and one of the CRABP isoforms (CRABP II) during the ligand transfer to the receptor.
76 iation constant of CRABP-II and CRABP-I (Kd (CRABP-II)/Kd (CRABP-I)) was determined to be 2-3, in clo
77 t of CRABP-II and CRABP-I (Kd (CRABP-II)/Kd (CRABP-I)) was determined to be 2-3, in close agreement w
78 constants of R111M and R132M (Kd (R111M)/Kd (CRABP-II) and Kd (R132M)/Kd(CRABP-II)) were determined t
79 (Kd (R111M)/Kd (CRABP-II) and Kd (R132M)/Kd(CRABP-II)) were determined to be 40-45 and 6-8, respecti
83 lated structural homology with bovine/murine CRABP I shows msCRABP has a ligand binding pocket that c
85 We previously showed that CRABP-II, but not CRABP-I, delivers RA to RAR through direct protein-prote
86 we show that expression of CRABP-II, but not CRABP-I, markedly enhanced RAR-mediated transcriptional
90 residues resulted in loss of the ability of CRABP-II to interact with RAR and to augment the recepto
91 ion of this residue abolishes the ability of CRABP-II to undergo nuclear translocation in response RA
92 ith this finding, the RA binding activity of CRABP in APL cells from three pretreatment cases (range,
95 NLS, mediates ligand-induced association of CRABP-II with importin alpha and is critical for nuclear
97 brium dissociation constants of complexes of CRABP-I or CRABP-II with RA were found to differ by 2-fo
98 ition, the relative dissociation constant of CRABP-II and CRABP-I (Kd (CRABP-II)/Kd (CRABP-I)) was de
99 o RA binding is critical for dissociation of CRABP-II from ER and, consequently, for mobilization of
102 re, the mechanisms underlying the effects of CRABP-II on the transcriptional activity of RAR and the
104 extract containing a 10-fold molar excess of CRABP I was incubated with RAR alpha extract in the pres
105 The ability of E2 to induce expression of CRABP(II) suggests that it can enhance the activity of R
107 In turn, KLF2 induces the expression of CRABP-II and RARgamma, further potentiating inhibition o
108 they suggest that constitutive expression of CRABP-II could have a facilitative role in the response
110 The observations show that expression of CRABP-II in preadipocytes is repressed by all three comp
113 05 does not alter the kinetics of folding of CRABP I, which indicates that the flexible loop containi
114 data unequivocally establish the function of CRABP-II in modulating the RAR-mediated biological activ
115 We show here that RA induces interactions of CRABP-II with the E2 SUMO ligase Ubc9 and triggers SUMOy
116 ificantly retarded the unfolding kinetics of CRABP I without influencing the urea dependence of the u
118 re was no change from pretreatment levels of CRABP-II mRNA (median, 0.98) or, in three relapse cases
119 tography procedures to examine the levels of CRABP-II mRNA and RA binding activity in APL patient sam
121 e demonstrate further that overexpression of CRABP-II in MCF-7 mammary carcinoma cells dramatically e
124 tween the electrostatic surface potential of CRABP-I and II revealed the presence of a sole region di
125 data demonstrate that the surface region of CRABP-II containing residues Gln75, Pro81, and Lys102 is
128 ons demonstrate that permanent repression of CRABP-II in mature adipocytes is exerted by the master r
130 observations emphasize the important role of CRABP-II in regulating the transcriptional activity of R
133 of crowding on the equilibrium stability of CRABP I was less than our experimental error (i.e., < or
134 effect of crowding on the denatured state of CRABP I by measuring side-chain accessibility using iodi
141 ing the corresponding CRABP-II residues onto CRABP-I conferred upon this protein the ability to chann
143 quamous), the levels of nuclear receptors or CRABPs, and the response of the cells to the growth-inhi
144 anization of msCRABP is conserved with other CRABP family members and the larger LBP superfamily.
145 al of FlAsH on the tetra-Cys-containing P39A CRABP I is sensitive to whether this protein is native o
146 llular retinoic acid-binding protein I (P39A CRABP I), which forms inclusion bodies when expressed in
147 may slow closure of the beta-barrel in P39A CRABP I relative to the wild type, leaving it vulnerable
148 the aggregation-prone intermediates of P39A CRABP I contain predominantly beta-strands structured in
152 n of cellular retinoic acid-binding protein (CRABP) and cellular retinoic-acid binding protein(II) [C
153 n of cellular retinoic-acid-binding protein (CRABP) and cellular retinol-binding protein (CRBP), as w
155 n), ILBP (ileal fatty acid-binding protein), CRABP I (cellular retinoic acid-binding protein), and CR
156 to the two known acidic RA-binding proteins CRABP I and II, the cerebellum expressed a third RA-bind
159 for cellular retinoic acid-binding proteins (CRABP-I and CRABP-II), a nuclear retinoic acid receptor
165 Cellular retinoic acid-binding proteins (CRABPs) I and II were detected in one and three of the e
168 cytoplasmic retinoic acid binding proteins, CRABP-I and CRABP-II, and the purified heterocomplexes i
170 by two intracellular lipid-binding proteins-CRABP-II, which targets RA to RAR, and FABP5, which deli
171 known role in direct delivery of RA to RAR, CRABP-II may have an additional, RA-independent, functio
173 residue) peptides corresponding to the seven CRABP I turns were analyzed by circular dichroism and NM
175 s analyses demonstrate that K102 is the sole CRABP-II residue to be SUMOylated in response to RA.
176 ficant evolutionary implications, suggesting CRABPs appeared during the evolution of the LBP superfam
177 expressing CRABP and CRABP(II) and suggests CRABP(II) may participate in retinoic acid production an
179 e intracellular lipid-binding protein termed CRABP-I and CRABP-II and that uses them as RA sensors.
183 rlies RA resistance in tumors, indicate that CRABP-II functions as a tumor suppressor, and suggest th
192 adipocyte differentiation by activating the CRABP-II/RARgamma path in preadipose cells, thereby upre
193 s to neuronal progenitors is mediated by the CRABP-II/RAR path and that the FABP5/PPARbeta/delta path
195 ciate with a cognate response element in the CRABP-II promoter and to repress CRABP-II expression.
197 ncomitantly with a transient increase in the CRABP-II/FABP5 ratio at early stages of differentiation.
200 interaction between RARgamma and one of the CRABP isoforms (CRABP II) during the ligand transfer to
201 E2 administration induced expression of the CRABP(II) gene in the uterus within 4 h, and this induct
202 inding site in the 5'-flanking region of the CRABP(II) gene was also required for this induction.
204 tion of endogenous retinoic acid between the CRABPs and the nuclear receptors and thus affect retinoi
205 places [3H]-all-trans-retinoic acid from the CRABPs and increases retinoic acid occupancy of the hete
208 inoic acid binds with comparable affinity to CRABP-I and the heterocomplexes, but with approximately
212 -E-isomers of UAB retinoids bound tightly to CRABPs and RAR alpha, the binding affinity of the all-E-
213 differential expression patterns of the two CRABPs suggest that they serve distinct biological funct
214 ns of the aromatic residues of the wild-type CRABP-II and the two mutants were sequentially assigned
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