Retinol binding protein 4

edit
Retinol binding protein 4, plasma

Human serum retinol binding protein. From PDB 1RBP.
Available structures
1aqb, 1brp, 1brq, 1erb, 1fel, 1fem, 1fen, 1hbp, 1hbq, 1jyd, 1jyj, 1kt3, 1kt4, 1kt5, 1kt6, 1kt7, 1qab, 1rbp, 1rlb
Identifiers
SymbolsRBP4;
External IDsOMIM: 180250 MGI: 97879 HomoloGene: 4908 GeneCards: RBP4 Gene
RNA expression pattern
PBB GE RBP4 219140 s at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez595019662
EnsemblENSG00000138207ENSMUSG00000024990
UniProtP02753Q3TF08
RefSeq (mRNA)NM_006744XM_993476
RefSeq (protein)NP_006735XP_998570
Location (UCSC)Chr 10:
95.34 - 95.35 Mb		Chr 19:
38.18 - 38.19 Mb
PubMed search[1][2]

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

Contents

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]

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]

See also

References

  1. ^ 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. 
  2. ^ 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. PMID 2928844. 
  3. ^ a b "Entrez Gene: RBP4 retinol binding protein 4, plasma". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5950. 
  4. ^ 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. 
  5. ^ 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. 

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. PMID 2998779. 
  • 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. PMID 6540172. 
  • 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. 

External links

v • d • e
Proteins: carrier proteins
Fatty acid
FABP1 · FABP2 · FABP3 · FABP4 · FABP5 · FABP6 · FABP7
Hormone
Metal/element
Vitamin
Other
© This material from Wikipedia is licensed under the GFDL