The cellular retinoic acid binding proteins

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. Both proteins are expressed during embryogenesis, particularly in the developing nervous system, craniofacial region and limb...

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Bibliographic Details
Published in:Journal of steroid biochemistry and molecular biology 1995-06, Vol.53 (1), p.459-465
Main Authors: Donovan, Mark, Olofsson, Birgitta, Gustafson, Anne-Lee, Dencker, Lennart, Eriksson, Ulf
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Binding and carrier proteins
Biological and medical sciences
Cattle
Cell Compartmentation
Fundamental and applied biological sciences. Psychology
Gene Expression
Humans
Medicin och hälsovetenskap
Mice
Molecular Sequence Data
Proteins
Receptors, Retinoic Acid - chemistry
Receptors, Retinoic Acid - genetics
RNA, Messenger - genetics
Sequence Alignment
Sequence Homology, Amino Acid
Tretinoin - metabolism
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Summary: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. Both proteins are expressed during embryogenesis, particularly in the developing nervous system, craniofacial region and limb bud. CRABP I is also expressed in several adult tissues, however, in contrast, CRABP II expression appears to be limited to the skin. It is likely that these proteins serve as regulators in the transport and metabolism of retinoic acid in the developing embryo and throughout adult life. It has been proposed that CRABP I sequesters retinoic acid in the cytoplasm and prevents nuclear uptake of retinoic acid. A role in catabolism of retinoic acid has also been proposed. Recent gene targeting experiments have shown that neither of the two CRABPs are essential for normal embryonic development or adult life. Examination of CRABP I expression at subcellular resolution reveals a differential cytoplasmic and/or nuclear localization of the protein. A regulated nuclear uptake of CRABP I implies a role for this protein in the intracellular transport of retinoic acid. A protein mediated mechanism which controls the nuclear uptake of retinoic acid may play an important role in the transactivation of the nuclear retinoic acid receptors.
ISSN:0960-0760
1879-1220
DOI:10.1016/0960-0760(95)00092-E