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Characterization of a New Member of the Fatty Acid-binding Protein Family That Binds All-trans-retinol
- Source :
- Journal of Biological Chemistry. 276:1353-1360
- Publication Year :
- 2001
- Publisher :
- Elsevier BV, 2001.
-
Abstract
- Cellular retinol-binding protein, type I (CRBP-I) and type II (CRBP-II) are the only members of the fatty acid-binding protein (FABP) family that process intracellular retinol. Heart and skeletal muscle take up postprandial retinol but express little or no CRBP-I or CRBP-II. We have identified an intracellular retinol-binding protein in these tissues. The 134-amino acid protein is encoded by a cDNA that is expressed primarily in heart, muscle and adipose tissue. It shares 57 and 56% sequence identity with CRBP-I and CRBP-II, respectively, but less than 40% with other members of the FABP family. In situ hybridization demonstrates that the protein is expressed at least as early as day 10 in developing heart and muscle tissue of the embryonic mouse. Fluorescence titrations of purified recombinant protein with retinol isomers indicates binding to all-trans-, 13-cis-, and 9-cis-retinol, with respective K dvalues of 109, 83, and 130 nm. Retinoic acids (all-trans-, 13-cis-, and 9-cis-), retinals (all-trans-, 13-cis-, and 9-cis-), fatty acids (laurate, myristate, palmitate, oleate, linoleate, arachidonate, and docosahexanoate), or fatty alcohols (palmityl, petrosenlinyl, and ricinolenyl) fail to bind. The distinct tissue expression pattern and binding specificity suggest that we have identified a novel FABP family member, cellular retinol-binding protein, type III.
- Subjects :
- DNA, Complementary
Molecular Sequence Data
In situ hybridization
Spodoptera
Muscle Development
Transfection
Biochemistry
Fatty acid-binding protein
Cell Line
Substrate Specificity
Mice
chemistry.chemical_compound
Complementary DNA
Protein A/G
Escherichia coli
Animals
Amino Acid Sequence
All trans retinol
Cloning, Molecular
adipocyte protein 2
Muscle, Skeletal
Vitamin A
Molecular Biology
In Situ Hybridization
Sequence Homology, Amino Acid
biology
Reverse Transcriptase Polymerase Chain Reaction
Myocardium
Retinol
Gene Expression Regulation, Developmental
Heart
Retinol-Binding Proteins, Cellular
Cell Biology
Molecular biology
Recombinant Proteins
Retinol-Binding Proteins
Kinetics
Retinol binding protein
Adipose Tissue
chemistry
biology.protein
Sequence Alignment
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 276
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....68601a52889aa62a22d1187ca2d83b1d