scholarly journals The expression of cellular retinoic acid binding protein (CRABP) in the neural tube and notochord of mouse embryo.

1989 ◽  
Vol 65 (2) ◽  
pp. 9-12 ◽  
Author(s):  
Mariko Y. MOMOI ◽  
Michiko HAYASAKA ◽  
Kazunori HANAOKA ◽  
Takashi MOMOI
1990 ◽  
Vol 54 (2) ◽  
pp. 161-167 ◽  
Author(s):  
Mariko Momoi ◽  
Takanori Yamagata ◽  
Kou Ichihashi ◽  
Masayoshi Yanagisawa ◽  
Makoto Yamakado ◽  
...  

1992 ◽  
Vol 37 (1-2) ◽  
pp. 13-23 ◽  
Author(s):  
Malcolm Maden ◽  
Claire Horton ◽  
Anthony Graham ◽  
Lisa Leonard ◽  
John Pizzey ◽  
...  

1989 ◽  
Vol 40 (2) ◽  
pp. 99-105 ◽  
Author(s):  
Marie-Josée Vaessen ◽  
Erika Kootwijk ◽  
Dirk Bootsma ◽  
Ad Geurts van Kessel ◽  
Christine Mummery ◽  
...  

Development ◽  
1991 ◽  
Vol 111 (1) ◽  
pp. 35-43 ◽  
Author(s):  
M. Maden ◽  
P. Hunt ◽  
U. Eriksson ◽  
A. Kuroiwa ◽  
R. Krumlauf ◽  
...  

We have investigated by immunocytochemistry the spatial and temporal distribution of cellular retinoic acid-binding protein (CRABP) in the developing nervous system of the chick embryo in order to answer two specific questions: do neural crest cells contain CRABP and where and when do CRABP-positive neuroblasts first arise in the neural tube? With regard to the neural crest, we have compared CRABP staining with HNK-1 staining (a marker of migrating neural crest) and found that they do indeed co-localise, but cephalic and trunk crest behave slightly differently. In the cephalic region in tissues such as the frontonasal mass and branchial arches, HNK-1 immunoreactivity is intense at early stages, but it disappears as CRABP immunoreactivity appears. Thus the two staining patterns do not overlap, but are complementary. In the trunk, HNK-1 and CRABP stain the same cell populations at the same time, such as those migrating through the anterior halves of the somites. In the neural tube, CRABP-positive neuroblasts first appear in the rhombencephalon just after the neural folds close and then a particular pattern of immunoreactivity appears within the rhombomeres of the hindbrain. Labelled cells are present in the future spinal cord, the posterior rhombencephalon up to rhombomere 6 and in rhombomere 4 thus producing a single stripe pattern. This pattern is dynamic and gradually changes as anterior rhombomeres begin to label. The similarity of this initial pattern to the arrangement of certain homeobox genes in the mouse stimulated us to examine the expression of the chicken Hox-2.9 gene. We show that at stage 15 the pattern of expression of this gene is closely related to that of CRABP. The relationship between retinoic acid, CRABP and homeobox genes is discussed.


2002 ◽  
Vol 362 (2) ◽  
pp. 265-271 ◽  
Author(s):  
Manickavasagam SUNDARAM ◽  
Daan M. F. van AALTEN ◽  
John B. C. FINDLAY ◽  
Asipu SIVAPRASADARAO

Members of the lipocalin superfamily share a common structural fold, but differ from each other with respect to the molecules with which they interact. They all contain eight β-strands (A—H) that fold to form a well-defined β-barrel, which harbours a binding pocket for hydrophobic ligands. These strands are connected by loops that vary in size and structure and make up the closed and open ends of the pocket. In addition to binding ligands, some members of the family interact with other macromolecules, the specificity of which is thought to be associated with the variable loop regions. Here, we have investigated whether the macromolecular-recognition properties can be transferred from one member of the family to another. For this, we chose the prototypical lipocalin, the plasma retinol-binding protein (RBP) and its close structural homologue the epididymal retinoic acid-binding protein (ERABP). RBP exhibits three molecular-recognition properties: it binds to retinol, to transthyretin (TTR) and to a cell-surface receptor. ERABP binds retinoic acid, but whether it interacts with other macromolecules is not known. Here, we show that ERABP does not bind to TTR and the RBP receptor, but when the loops of RBP near the open end of the pocket (L-1, L-2 and L-3, connecting β-strands A—B, C—D and E—F, respectively) were substituted into the corresponding regions of ERABP, the resulting chimaera acquired the ability to bind TTR and the receptor. L-2 and L-3 were found to be the major determinants of the receptor- and TTR-binding specificities respectively. Thus we demonstrate that lipocalins serve as excellent scaffolds for engineering novel biological functions.


The Prostate ◽  
1987 ◽  
Vol 11 (2) ◽  
pp. 127-132 ◽  
Author(s):  
Jaswant K. Jutley ◽  
Jerry Kelleher ◽  
Peter Whelan ◽  
John Mikel

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