Retinol binding protein 4

Retinol binding protein 4, plasma
	; Human serum retinol binding protein. From PDB 1RBP.
Available structures
PDB	1BRP, 1BRQ, 1JYD, 1JYJ, 1QAB, 1RBP, 1RLB, 2WQ9, 2WQA, 2WR6, 3BSZ, 3FMZ
Identifiers
Symbols	RBP4;
External IDs	OMIM: 180250 MGI: 97879 HomoloGene: 4908 GeneCards: RBP4 Gene
Gene Ontology
Molecular function	• transporter activity; • protein binding; • retinal binding; • retinol binding; • retinol transporter activity;
Cellular component	• extracellular region; • extracellular space; • extracellular space;
Biological process	• eye development; • eye development; • gluconeogenesis; • gluconeogenesis; • spermatogenesis; • heart development; • male gonad development; • embryo development; • maintenance of gastrointestinal epithelium; • lung development; • positive regulation of insulin secretion; • response to retinoic acid; • response to insulin stimulus; • retinol transport; • retinol metabolic process; • retinal metabolic process; • glucose homeostasis; • response to ethanol; • embryonic organ morphogenesis; • embryonic skeletal system development; • cardiac muscle tissue development; • female genitalia morphogenesis; • response to stimulus; • detection of light stimulus involved in visual perception; • positive regulation of immunoglobulin secretion; • retina development in camera-type eye; • negative regulation of cardiac muscle cell proliferation; • embryonic retina morphogenesis in camera-type eye; • uterus development; • vagina development; • urinary bladder development; • heart trabecula formation;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

From Wikipedia, the free encyclopedia

Jump to: navigation, search

Retinol binding protein 4, plasma, also known as RBP4, is protein^[1] that in humans is encoded by the RBP4 gene.^[2]^[3]

[edit] Function

This protein belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, which prevents its loss by filtration through the kidney glomeruli. A deficiency of vitamin A blocks secretion of the binding protein posttranslationally and results in defective delivery and supply to the epidermal cells.^[3]

[edit] Clinical significance

Retinol-binding protein 4 has recently been described as an adipokine that contributes to insulin resistance in the AG4KO mouse model.^[4] It is secreted by adipocytes, and can act as a signal to other cells, when there is a decrease in plasma glucose concentration.^[5]

[edit] See also

Retinol binding protein

[edit] References

^ Rask L, Anundi H, Fohlman J, Peterson PA (1987). "The complete amino acid sequence of human serum retinol-binding protein". Upsala Journal of Medical Sciences 92 (2): 115–46. PMID 2444024.
^ Rocchi M, Covone A, Romeo G, Faraonio R, Colantuoni V (March 1989). "Regional mapping of RBP4 to 10q23----q24 and RBP1 to 3q21----q22 in man". Somatic Cell and Molecular Genetics 15 (2): 185–90. doi:10.1007/BF01535081. PMID 2928844.
^ ^a ^b "Entrez Gene: RBP4 retinol binding protein 4, plasma". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5950.
^ Yang Q, Graham TE, Mody N, Preitner F, Peroni OD, Zabolotny JM, Kotani K, Quadro L, Kahn BB (2005). "Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes". Nature 436 (7049): 356–62. doi:10.1038/nature03711. PMID 16034410.
^ Herman MA, Kahn BB (2006). "Glucose transport and sensing in the maintenance of glucose homeostasis and metabolic harmony". J. Clin. Invest. 116 (7): 1767–75. doi:10.1172/JCI29027. PMID 16823474.

[edit] Further reading

Newcomer ME, Ong DE (2000). "Plasma retinol binding protein: structure and function of the prototypic lipocalin.". Biochim. Biophys. Acta 1482 (1-2): 57–64. PMID 11058747.
Fex G, Hansson B (1979). "Retinol-binding protein from human urine and its interaction with retinol and prealbumin.". Eur. J. Biochem. 94 (1): 307–13. doi:10.1111/j.1432-1033.1979.tb12896.x. PMID 571335.
Rask L, Anundi H, Peterson PA (1979). "The primary structure of the human retinol-binding protein.". FEBS Lett. 104 (1): 55–8. doi:10.1016/0014-5793(79)81084-4. PMID 573217.
Fex G, Albertsson PA, Hansson B (1980). "Interaction between prealbumin and retinol-binding protein studied by affinity chromatography, gel filtration and two-phase partition.". Eur. J. Biochem. 99 (2): 353–60. doi:10.1111/j.1432-1033.1979.tb13263.x. PMID 574085.
Monaco HL, Zanotti G (1992). "Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity.". Biopolymers 32 (4): 457–65. doi:10.1002/bip.360320425. PMID 1623143.
Cowan SW, Newcomer ME, Jones TA (1990). "Crystallographic refinement of human serum retinol binding protein at 2A resolution.". Proteins 8 (1): 44–61. doi:10.1002/prot.340080108. PMID 2217163.
Rask L, Anundi H, Fohlman J, Peterson PA (1987). "The complete amino acid sequence of human serum retinol-binding protein.". Ups. J. Med. Sci. 92 (2): 115–46. PMID 2444024.
Rocchi M, Covone A, Romeo G, et al. (1989). "Regional mapping of RBP4 to 10q23----q24 and RBP1 to 3q21----q22 in man.". Somat. Cell Mol. Genet. 15 (2): 185–90. doi:10.1007/BF01535081. PMID 2928844.
D'Onofrio C, Colantuoni V, Cortese R (1986). "Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals.". Embo J. 4 (8): 1981–9. PMC 554451. PMID 2998779. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=554451.
Pfeffer BA, Clark VM, Flannery JG, Bok D (1986). "Membrane receptors for retinol-binding protein in cultured human retinal pigment epithelium.". Invest. Ophthalmol. Vis. Sci. 27 (7): 1031–40. PMID 3013795.
Kameko M, Ichikawa M, Katsuyama T, et al. (1986). "Immunohistochemical localization of plasma retinol-binding protein and prealbumin in human pancreatic islets.". Histochem. J. 18 (4): 164–8. doi:10.1007/BF01676116. PMID 3525470.
Siegenthaler G, Saurat JH (1987). "Loss of retinol-binding properties for plasma retinol-binding protein in normal human epidermis.". J. Invest. Dermatol. 88 (4): 403–8. doi:10.1111/1523-1747.ep12469731. PMID 3559267.
Rask L, Vahlquist A, Peterson PA (1972). "Studies on two physiological forms of the human retinol-binding protein differing in vitamin A and arginine content.". J. Biol. Chem. 246 (21): 6638–46. PMID 5132677.
Colantuoni V, Romano V, Bensi G, et al. (1984). "Cloning and sequencing of a full length cDNA coding for human retinol-binding protein.". Nucleic Acids Res. 11 (22): 7769–76. doi:10.1093/nar/11.22.7769. PMID 6316270.
Newcomer ME, Jones TA, Aqvist J, et al. (1984). "The three-dimensional structure of retinol-binding protein.". Embo J. 3 (7): 1451–4. PMC 557543. PMID 6540172. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=557543.
Rask L, Anundi H, Böhme J, et al. (1981). "Structural and functional studies of vitamin A-binding proteins.". Ann. N. Y. Acad. Sci. 359: 79–90. doi:10.1111/j.1749-6632.1981.tb12739.x. PMID 6942701.
Jaconi S, Rose K, Hughes GJ, et al. (1995). "Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure.". J. Lipid Res. 36 (6): 1247–53. PMID 7666002.
Berni R, Malpeli G, Folli C, et al. (1994). "The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein.". J. Biol. Chem. 269 (38): 23395–8. PMID 8089102.
Seeliger MW, Biesalski HK, Wissinger B, et al. (1999). "Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis.". Invest. Ophthalmol. Vis. Sci. 40 (1): 3–11. PMID 9888420.
Naylor HM, Newcomer ME (1999). "The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP.". Biochemistry 38 (9): 2647–53. doi:10.1021/bi982291i. PMID 10052934.