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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
4                  We designed and expressed a CRABP I mutant (A35C/T57C), in which a small-scale confo
5 ABP (msCRABP) demonstrates the presence of a CRABP in invertebrates.
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,
10 lar lipid-binding protein termed CRABP-I and CRABP-II and that uses them as RA sensors.
11  retinoic acid-binding proteins (CRABP-I and CRABP-II), a nuclear retinoic acid receptor (RAR alpha),
12  retinoic acid binding proteins (CRABP-I and CRABP-II).
13  retinoic acid-binding proteins (CRABP-I and CRABP-II).
14  retinoic acid-binding proteins (CRABP-I and CRABP-II).
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
17  retinoic acid-binding proteins, CRABP-I and CRABP-II, have been well characterized.
18 lative dissociation constant of CRABP-II and CRABP-I (Kd (CRABP-II)/Kd (CRABP-I)) was determined to b
19 he presence of this NLS in holo- but not apo-CRABP-II.
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
23 sm that involves direct interactions between CRABP-II and RAR.
24                   "Channeling" of RA between CRABP-II and RAR markedly facilitates the formation of t
25              No correlation was seen between CRABP II or CRBP I mRNA levels and the levels of either
26 rding to their isoelectric point showed both CRABP I and CRABP II to be present in the cerebellum and
27 riptional activity of RA can be regulated by CRABP-II.
28               Substituting the corresponding CRABP-II residues onto CRABP-I conferred upon this prote
29               Unfolding of labeled tetra-Cys CRABP I is accompanied by enhancement of FlAsH fluoresce
30 onprone mutant (FlAsH-labeled P39A tetra-Cys CRABP I).
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
33 elium to synthesize RA as well as to express CRABP(II).
34 SG-treated rats (shown previously to express CRABP).
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
37              At no time did cells expressing CRABP exhibit significant retinoic acid synthesis.
38 raced to an aberrantly high intratumor FABP5/CRABP-II ratio.
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
43             In contrast, movement of RA from CRABP-II to the receptor is facilitated by a mechanism t
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
46 r components involved in RA processing (e.g. CRABP).
47 in approximately heart > liver > intestine > CRABP > CRBP.
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
54 of cellular retinoic acid-binding protein I (CRABP I).
55 of cellular retinoic acid binding protein I (CRABP I).
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
61 ding protein cellular RA-binding protein-II (CRABP-II).
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
64  cellular retinoic-acid binding protein(II) [CRABP(II)] in the uterus of the rat.
65 ranslocation in response RA and thus impairs CRABP-II-mediated activation of RAR.
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
68          In contrast, RA caused no change in CRABP(II) message level, even at times as late as 48 h a
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
74             The existence of an invertebrate CRABP has significant evolutionary implications, suggest
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
80                                         L28C CRABP mutants were generated, and the inserted cysteine
81 haracteristic of the promoter region of most CRABPs analyzed.
82          Analysis of the expression of mouse CRABP I from a cDNA expression plasmid in COS-1 cells re
83 lated structural homology with bovine/murine CRABP I shows msCRABP has a ligand binding pocket that c
84                  Compared with bovine/murine CRABP I, the deduced amino acid sequence of msCRABP is 7
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
87                              In the nucleus, CRABP-II directly binds to the nuclear receptor RAR to f
88                       Arg-111 and Arg-132 of CRABP-II were replaced with methionine by site-directed
89 ty of RAR stems directly from the ability of CRABP-II to channel retinoic acid to the receptor.
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,
93                 In contrast, the addition of CRABP I did not significantly affect the interaction of
94      To determine whether this appearance of CRABP(II) was dependent on the production of RA, both E2
95  NLS, mediates ligand-induced association of CRABP-II with importin alpha and is critical for nuclear
96                Moreover, the coexpression of CRABP I in CV-1 cells did not markedly inhibit or enhanc
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
100 ore, we show that RA-induced dissociation of CRABP-II from the ER requires SUMOylation of K102.
101 R), and that RA triggers the dissociation of CRABP-II from this location.
102 re, the mechanisms underlying the effects of CRABP-II on the transcriptional activity of RAR and the
103  in narrowing the conformational ensemble of CRABP I during folding.
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
106 as also been shown to increase expression of CRABP(II).
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
109                         Stable expression of CRABP-II in mammary carcinoma SC115 cells enabled activa
110     The observations show that expression of CRABP-II in preadipocytes is repressed by all three comp
111         Conversely, diminished expression of CRABP-II renders these cells retinoic acid resistant.
112              Here we show that expression of CRABP-II, but not CRABP-I, markedly enhanced RAR-mediate
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
117                    Photoaffinity labeling of CRABP-I with [(3)H]RA was light- and concentration-depen
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
120         The identity and the localization of CRABP I in the cytoplasm as well as the nuclei were also
121 e demonstrate further that overexpression of CRABP-II in MCF-7 mammary carcinoma cells dramatically e
122              Specifically, overexpression of CRABP-II, in the absence of RA, up-regulated the express
123 thesis and is augmented by overexpression of CRABP-II.
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
126              Here, we localize the region of CRABP-II that mediates the interactions of this protein
127 ifferentiation stems from down-regulation of CRABP-II.
128 ons demonstrate that permanent repression of CRABP-II in mature adipocytes is exerted by the master r
129          In agreement with the known role of CRABP-II in enhancing the transcriptional activity of RA
130 observations emphasize the important role of CRABP-II in regulating the transcriptional activity of R
131                      The primary sequence of CRABP-II contains three putative SUMOylation sites, cent
132  acids comprising the ligand binding site of CRABP-I.
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
135        The ligand-controlled NLS "switch" of CRABP-II may represent a general mechanism for posttrans
136 on constants of the site-directed mutants of CRABPs.
137 ecific amino acids in the RA-binding site of CRABPs by photoaffinity labeling.
138                         This work focuses on CRABP-II, a cytosolic protein that moves to the nucleus
139  sufficient for maximal tumor suppression on CRABP-II overexpression.
140 nt in the cerebellum and P19 cells, and only CRABP II to be present in the choroid plexus.
141 ing the corresponding CRABP-II residues onto CRABP-I conferred upon this protein the ability to chann
142 ciation constants of complexes of CRABP-I or CRABP-II with RA were found to differ by 2-fold.
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
149                                 Photolabeled CRABP-I was hydrolyzed with endoproteinase Lys-C to yiel
150  cognate intracellular lipid-binding protein CRABP-II.
151                 Cellular RA binding protein (CRABP II) colocalized with RALDH 1.
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
154  the cellular retinoic acid-binding protein (CRABP) II, in this process.
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
157  by the intracellular lipid binding proteins CRABP-II and FABP5.
158 ir respective cognate lipid-binding proteins CRABP-II and FABP5.
159 for cellular retinoic acid-binding proteins (CRABP-I and CRABP-II), a nuclear retinoic acid receptor
160 and cellular retinoic acid-binding proteins (CRABP-I and CRABP-II).
161  by cellular retinoic acid-binding proteins (CRABP-I and CRABP-II).
162 and cellular retinoic acid binding proteins (CRABP-I and CRABP-II).
163 des cellular retinoic acid-binding proteins (CRABPs) and fatty acid binding proteins (FABPs).
164 us isoforms of cellular RA binding proteins (CRABPs) and RA receptor gamma (RARgamma).
165     Cellular retinoic acid-binding proteins (CRABPs) I and II were detected in one and three of the e
166 ding proteins [cellular RA binding proteins (CRABPs)-I and -II].
167 ate cellular retinoic acid binding proteins (CRABPs).
168  cytoplasmic retinoic acid binding proteins, CRABP-I and CRABP-II, and the purified heterocomplexes i
169  cytoplasmic retinoic acid-binding proteins, CRABP-I and CRABP-II, have been well characterized.
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
172 ment in the CRABP-II promoter and to repress CRABP-II expression.
173 residue) peptides corresponding to the seven CRABP I turns were analyzed by circular dichroism and NM
174            This discovery of a Manduca sexta CRABP (msCRABP) demonstrates the presence of a CRABP in
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
178                         With this technique, CRABP I could also be detected in the HL60 cell line.
179 e intracellular lipid-binding protein termed CRABP-I and CRABP-II and that uses them as RA sensors.
180               These results demonstrate that CRABP I, while it might be important for RA homeostasis,
181                                We found that CRABP-II mRNA in APL cells from pretreatment patients (n
182         Surprisingly, the data indicate that CRABP-II also displays proapoptotic activities on its ow
183 rlies RA resistance in tumors, indicate that CRABP-II functions as a tumor suppressor, and suggest th
184                  We previously reported that CRABP-II enhances the transcriptional activity of RAR by
185                 The observations reveal that CRABP-II plays a critical role in sensitizing tumors to
186                 Recent studies revealed that CRABP-II functions by "channeling" RA to RAR, thereby en
187                   The data further show that CRABP-II is a direct target gene for the glucocorticoid
188                                 We show that CRABP-II, a predominantly cytosolic protein, massively u
189                    We previously showed that CRABP-II enhances the transcriptional activity of the nu
190                    We previously showed that CRABP-II, but not CRABP-I, delivers RA to RAR through di
191  that, in the presence of retinoic acid, the CRABP-II-RAR complex is a short-lived intermediate.
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
194 ccompanied by a proportional increase in the CRABP I fraction.
195 ciate with a cognate response element in the CRABP-II promoter and to repress CRABP-II expression.
196 nding protein alpha-response elements in the CRABP-II promoter.
197 ncomitantly with a transient increase in the CRABP-II/FABP5 ratio at early stages of differentiation.
198                 The unique properties of the CRABP I mutant described in this work can be used to ins
199 ty acid composition without induction of the CRABP II message.
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.
203 rmation about the ligand binding site of the CRABP-I molecule in solution.
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
206 he mechanisms by which RA transfers from the CRABPs to RAR were thus investigated directly.
207  although it binds with high affinity to the CRABPs.
208 inoic acid binds with comparable affinity to CRABP-I and the heterocomplexes, but with approximately
209  with approximately 10-fold less affinity to CRABP-II.
210    Some of the 7-oxa-7,8-dihydro-RAs bind to CRABP and RARalpha.
211 ance of FA binding to FABP, binding of FA to CRABP-I was entropically driven.
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
215  are highly similar to that of the wild-type CRABP-II.
216                                        While CRABP-II does not contain an NLS in its primary sequence
217 staining of the transfected COS-1 cells with CRABP I-specific antibody.

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