Retinol binding protein 4, also known as RBP4, is a transporter protein[5] for retinol (vitamin A alcohol). RBP4 has a molecular weight of approximately 21 kDa and is encoded by the RBP4gene in humans.[6][7] It is mainly, though not exclusively, synthesized in the liver and circulates in the bloodstream as a hepatokine bound to retinol in a complex with transthyretin. RBP4 has been a drug target for ophthalmology research due to its role in vision.[8] RBP4 may also be involved in metabolic diseases as suggested by recent studies.
This protein belongs to the lipocalin family and is the specific carrier for retinol (vitamin A) 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.[7]
Structureedit
Two molecules of RBP4 (in yellow and red) bound to retinol (in orange) complexed with four molecules of TTR (in purple and blue)
RBP4 is a single polypeptide chain with a hydrophobic pocket where retinol binds. The RBP4-retinol complex then binds transthyretin in circulation to prevent renal filtration of RBP4.[9]
In serum, TTR and RBP4 bind in a 1 to 1 stoichiometry (two molecules of TTR combine with two molecules of RBP4 to form a complex with a total molecular weight of approximately 80,000 daltons).[10]
Clinical significanceedit
Retinol-binding protein 4 has been a drug target for eye diseases as RBP4 is the sole carrier for retinol, which is an essential nutrient for the visual cycle. Animal studies using RBP4-antagonists showed that lowering RBP4 can lead to reduction in the accumulation of lipofuscin that leads to vision loss in eye diseases like Stargardt's disease and macular degeneration.[8][11] An animal study using ABCA4knockout mouse proved that reduction in serum RBP4 level could inhibit lipofuscin without inhibiting the visual cycle.[ref] One clinical study in age-related macular degeneration (AMD) was conducted using Fenretinide. The study showed trends in reducing lesion growth rate in AMD and rate of conversion from early stage AMD (dry AMD) to late stage AMD (wet AMD) without serious side effects.
RBP4 has recently been described as an adipokine that contributes to insulin resistance and diabetes in the AG4KO mouse model.[12] In addition to the liver, RBP4 is also secreted by adipocytes of the fat tissue in a smaller portion and acts as a signal to surrounding cells, when there is a decrease in plasma glucose concentration.[13] It is suspected that an elevated level of RBP4 attracts macrophages to the fat tissue, causes local inflammation, and leads to insulin resistance.[14][15]
Mutations in the RBP4 gene have recently been linked to a form of autosomal dominant microphthalmia, anophthalmia, and coloboma (MAC) disease.[16] A unique feature of this disease is the maternal inheritance effect, when a fetus inherits a mutated copy of the RBP4 gene from its mother, but not from its father. The physiologic basis lies in pregnancy whereby the mutated gene product, retinol binding protein (RBP), has negative effects in transferring vitamin A from maternal liver storage sites to the placenta, and then again on the fetal circulation side when delivering vitamin A from the placenta to developing fetal tissues, most notably the developing eye. This 'double whammy' effect does not exist when the mutant RBP4 gene is inherited from the father. The above mechanism is separate from previously known types of maternal inheritance effects such as genomic imprinting, mitochondrial inheritance, or maternal oocyte mRNA transfer. The authors of the above study cite the potential of vitamin A supplementation in pregnant females who are known to carry an RBP4 mutation with retinyl ester which utilizes an RBP-independent pathway to deliver retinoids from the maternal intestines directly to the placenta and ultimately is uptaken by the fetus. The key would be to supplement during the first several months of life when the eye begins to develop, as supplementing later in pregnancy would be too late to avoid any potential MAC disease.
^ abcGRCh38: Ensembl release 89: ENSG00000138207 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000024990 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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. doi:10.3109/03009738709178685. 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. S2CID 37896530.
^ ab"Entrez Gene: RBP4 retinol binding protein 4, plasma".
^ abCioffi CL, Dobri N, Freeman EE, Conlon MP, Chen P, Stafford DG, Schwarz DM, Golden KC, Zhu L, Kitchen DB, Barnes KD, Racz B, Qin Q, Michelotti E, Cywin CL, Martin WH, Pearson PG, Johnson G, Petrukhin K (September 2014). "Design, synthesis, and evaluation of nonretinoid retinol binding protein 4 antagonists for the potential treatment of atrophic age-related macular degeneration and Stargardt disease". Journal of Medicinal Chemistry. 57 (18): 7731–57. doi:10.1021/jm5010013. PMC4174998. PMID 25210858.
^Kanai M, Raz A, Goodman DS (September 1968). "Retinol-binding protein: the transport protein for vitamin A in human plasma". The Journal of Clinical Investigation. 47 (9): 2025–44. doi:10.1172/jci105889. PMC297364. PMID 5675424.
^Naylor HM, Newcomer ME (March 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.
^Radu RA, Han Y, Bui TV, Nusinowitz S, Bok D, Lichter J, Widder K, Travis GH, Mata NL (December 2005). "Reductions in serum vitamin A arrest accumulation of toxic retinal fluorophores: a potential therapy for treatment of lipofuscin-based retinal diseases". Investigative Ophthalmology & Visual Science. 46 (12): 4393–401. doi:10.1167/iovs.05-0820. PMID 16303925.
^Yang Q, Graham TE, Mody N, Preitner F, Peroni OD, Zabolotny JM, Kotani K, Quadro L, Kahn BB (July 2005). "Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes". Nature. 436 (7049): 356–62. Bibcode:2005Natur.436..356Y. doi:10.1038/nature03711. PMID 16034410. S2CID 4343960.
^Herman MA, Kahn BB (July 2006). "Glucose transport and sensing in the maintenance of glucose homeostasis and metabolic harmony". The Journal of Clinical Investigation. 116 (7): 1767–75. doi:10.1172/JCI29027. PMC1483149. PMID 16823474.
^Moraes-Vieira PM, Yore MM, Dwyer PM, Syed I, Aryal P, Kahn BB (March 2014). "RBP4 activates antigen-presenting cells, leading to adipose tissue inflammation and systemic insulin resistance". Cell Metabolism. 19 (3): 512–26. doi:10.1016/j.cmet.2014.01.018. PMC4078000. PMID 24606904.
^Galic S, Oakhill JS, Steinberg GR (March 2010). "Adipose tissue as an endocrine organ". Molecular and Cellular Endocrinology. 316 (2): 129–39. doi:10.1016/j.mce.2009.08.018. PMID 19723556. S2CID 7385199.
^Chou CM, Nelson C, Tarlé SA, Pribila JT, Bardakjian T, Woods S, Schneider A, Glaser T (April 2015). "Biochemical Basis for Dominant Inheritance, Variable Penetrance, and Maternal Effects in RBP4 Congenital Eye Disease". Cell. 161 (3): 634–646. doi:10.1016/j.cell.2015.03.006. PMC4409664. PMID 25910211.
Further readingedit
Quadro L, Hamberger L, Colantuoni V, Gottesman ME, Blaner WS (December 2003). "Understanding the physiological role of retinol-binding protein in vitamin A metabolism using transgenic and knockout mouse models". Molecular Aspects of Medicine. 24 (6): 421–30. doi:10.1016/S0098-2997(03)00038-4. PMID 14585313.
Newcomer ME, Ong DE (October 2000). "Plasma retinol binding protein: structure and function of the prototypic lipocalin". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1482 (1–2): 57–64. doi:10.1016/s0167-4838(00)00150-3. PMID 11058747.
Fex G, Hansson B (February 1979). "Retinol-binding protein from human urine and its interaction with retinol and prealbumin". European Journal of Biochemistry. 94 (1): 307–13. doi:10.1111/j.1432-1033.1979.tb12896.x. PMID 571335.
Rask L, Anundi H, Peterson PA (August 1979). "The primary structure of the human retinol-binding protein". FEBS Letters. 104 (1): 55–8. doi:10.1016/0014-5793(79)81084-4. PMID 573217. S2CID 8540537.
Fex G, Albertsson PA, Hansson B (September 1979). "Interaction between prealbumin and retinol-binding protein studied by affinity chromatography, gel filtration and two-phase partition". European Journal of Biochemistry. 99 (2): 353–60. doi:10.1111/j.1432-1033.1979.tb13263.x. PMID 574085.
Monaco HL, Zanotti G (April 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. S2CID 34994569.
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. S2CID 21613341.
D'Onofrio C, Colantuoni V, Cortese R (August 1985). "Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals". The EMBO Journal. 4 (8): 1981–9. doi:10.1002/j.1460-2075.1985.tb03881.x. PMC554451. PMID 2998779.
Pfeffer BA, Clark VM, Flannery JG, Bok D (July 1986). "Membrane receptors for retinol-binding protein in cultured human retinal pigment epithelium". Investigative Ophthalmology & Visual Science. 27 (7): 1031–40. PMID 3013795.
Kameko M, Ichikawa M, Katsuyama T, Kanai M, Kato M, Akamatsu T (April 1986). "Immunohistochemical localization of plasma retinol-binding protein and prealbumin in human pancreatic islets". The Histochemical Journal. 18 (4): 164–8. doi:10.1007/BF01676116. PMID 3525470. S2CID 2959823.
Siegenthaler G, Saurat JH (April 1987). "Loss of retinol-binding properties for plasma retinol-binding protein in normal human epidermis". The Journal of Investigative Dermatology. 88 (4): 403–8. doi:10.1111/1523-1747.ep12469731. PMID 3559267.
Rask L, Vahlquist A, Peterson PA (November 1971). "Studies on two physiological forms of the human retinol-binding protein differing in vitamin A and arginine content". The Journal of Biological Chemistry. 246 (21): 6638–46. doi:10.1016/S0021-9258(19)34162-6. PMID 5132677.
Colantuoni V, Romano V, Bensi G, Santoro C, Costanzo F, Raugei G, Cortese R (November 1983). "Cloning and sequencing of a full length cDNA coding for human retinol-binding protein". Nucleic Acids Research. 11 (22): 7769–76. doi:10.1093/nar/11.22.7769. PMC326530. PMID 6316270.
Newcomer ME, Jones TA, Aqvist J, Sundelin J, Eriksson U, Rask L, Peterson PA (July 1984). "The three-dimensional structure of retinol-binding protein". The EMBO Journal. 3 (7): 1451–4. doi:10.1002/j.1460-2075.1984.tb01995.x. PMC557543. PMID 6540172.
Rask L, Anundi H, Böhme J, Eriksson U, Ronne H, Sege K, Peterson PA (February 1981). "Structural and functional studies of vitamin A-binding proteins". Annals of the New York Academy of Sciences. 359 (1): 79–90. Bibcode:1981NYASA.359...79R. doi:10.1111/j.1749-6632.1981.tb12739.x. PMID 6942701. S2CID 5781208.
Jaconi S, Rose K, Hughes GJ, Saurat JH, Siegenthaler G (June 1995). "Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure". Journal of Lipid Research. 36 (6): 1247–53. doi:10.1016/S0022-2275(20)41132-0. PMID 7666002.
Berni R, Malpeli G, Folli C, Murrell JR, Liepnieks JJ, Benson MD (September 1994). "The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein". The Journal of Biological Chemistry. 269 (38): 23395–8. doi:10.1016/S0021-9258(17)31527-2. PMID 8089102.
Seeliger MW, Biesalski HK, Wissinger B, Gollnick H, Gielen S, Frank J, Beck S, Zrenner E (January 1999). "Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis". Investigative Ophthalmology & Visual Science. 40 (1): 3–11. PMID 9888420.
Overview of all the structural information available in the PDB for UniProt: P02753 (Retinol-binding protein 4) at the PDBe-KB.
January 01, 1970
retinol, binding, protein, also, known, rbp4, transporter, protein, retinol, vitamin, alcohol, rbp4, molecular, weight, approximately, encoded, rbp4, gene, humans, mainly, though, exclusively, synthesized, liver, circulates, bloodstream, hepatokine, bound, ret. Retinol binding protein 4 also known as RBP4 is a transporter protein 5 for retinol vitamin A alcohol RBP4 has a molecular weight of approximately 21 kDa and is encoded by the RBP4 gene in humans 6 7 It is mainly though not exclusively synthesized in the liver and circulates in the bloodstream as a hepatokine bound to retinol in a complex with transthyretin RBP4 has been a drug target for ophthalmology research due to its role in vision 8 RBP4 may also be involved in metabolic diseases as suggested by recent studies RBP4Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1BRP 1BRQ 1JYD 1JYJ 1QAB 1RBP 1RLB 2WQ9 2WQA 2WR6 3BSZ 3FMZ 4O9S 4PSQIdentifiersAliasesRBP4 MCOPCB10 RDCCAS retinol binding protein 4External IDsOMIM 180250 MGI 97879 HomoloGene 4908 GeneCards RBP4Gene location Human Chr Chromosome 10 human 1 Band10q23 33Start93 591 687 bp 1 End93 601 744 bp 1 Gene location Mouse Chr Chromosome 19 mouse 2 Band19 C2 19 32 75 cMStart38 105 077 bp 2 End38 113 729 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright lobe of liversubcutaneous adipose tissuepituitary glandanterior pituitaryabdominal fattibiasynovial jointnucleus accumbenskidneypericardiumTop expressed inleft lobe of liveryolk sacgallbladderwhite adipose tissuebrown adipose tissueascending aortaprimitive streaksubcutaneous adipose tissueislet of Langerhansaortic valveMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionretinol transmembrane transporter activity transporter activity protein binding retinoid binding protein heterodimerization activity retinol binding retinal binding small molecule bindingCellular componentcytosol extracellular region extracellular exosome extracellular space protein containing complexBiological processeye development gluconeogenesis heart trabecula formation response to retinoic acid glucose homeostasis response to stimulus cardiac muscle tissue development lung development vagina development urinary bladder development retinol metabolic process embryonic organ morphogenesis embryonic skeletal system development retinoid metabolic process female genitalia morphogenesis uterus development heart development maintenance of gastrointestinal epithelium retinol transport embryonic retina morphogenesis in camera type eye response to ethanol negative regulation of cardiac muscle cell proliferation visual perception positive regulation of insulin secretion transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez595019662EnsemblENSG00000138207ENSMUSG00000024990UniProtP02753Q00724RefSeq mRNA NM 006744NM 001323517NM 001323518NM 001159487NM 011255RefSeq protein NP 001310446NP 001310447NP 006735NP 001152959NP 035385Location UCSC Chr 10 93 59 93 6 MbChr 19 38 11 38 11 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Structure 3 Clinical significance 4 See also 5 References 6 Further reading 7 External linksFunction editThis protein belongs to the lipocalin family and is the specific carrier for retinol vitamin A 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 7 Structure edit nbsp Two molecules of RBP4 in yellow and red bound to retinol in orange complexed with four molecules of TTR in purple and blue RBP4 is a single polypeptide chain with a hydrophobic pocket where retinol binds The RBP4 retinol complex then binds transthyretin in circulation to prevent renal filtration of RBP4 9 In serum TTR and RBP4 bind in a 1 to 1 stoichiometry two molecules of TTR combine with two molecules of RBP4 to form a complex with a total molecular weight of approximately 80 000 daltons 10 Clinical significance editRetinol binding protein 4 has been a drug target for eye diseases as RBP4 is the sole carrier for retinol which is an essential nutrient for the visual cycle Animal studies using RBP4 antagonists showed that lowering RBP4 can lead to reduction in the accumulation of lipofuscin that leads to vision loss in eye diseases like Stargardt s disease and macular degeneration 8 11 An animal study using ABCA4 knockout mouse proved that reduction in serum RBP4 level could inhibit lipofuscin without inhibiting the visual cycle ref One clinical study in age related macular degeneration AMD was conducted using Fenretinide The study showed trends in reducing lesion growth rate in AMD and rate of conversion from early stage AMD dry AMD to late stage AMD wet AMD without serious side effects RBP4 has recently been described as an adipokine that contributes to insulin resistance and diabetes in the AG4KO mouse model 12 In addition to the liver RBP4 is also secreted by adipocytes of the fat tissue in a smaller portion and acts as a signal to surrounding cells when there is a decrease in plasma glucose concentration 13 It is suspected that an elevated level of RBP4 attracts macrophages to the fat tissue causes local inflammation and leads to insulin resistance 14 15 Mutations in the RBP4 gene have recently been linked to a form of autosomal dominant microphthalmia anophthalmia and coloboma MAC disease 16 A unique feature of this disease is the maternal inheritance effect when a fetus inherits a mutated copy of the RBP4 gene from its mother but not from its father The physiologic basis lies in pregnancy whereby the mutated gene product retinol binding protein RBP has negative effects in transferring vitamin A from maternal liver storage sites to the placenta and then again on the fetal circulation side when delivering vitamin A from the placenta to developing fetal tissues most notably the developing eye This double whammy effect does not exist when the mutant RBP4 gene is inherited from the father The above mechanism is separate from previously known types of maternal inheritance effects such as genomic imprinting mitochondrial inheritance or maternal oocyte mRNA transfer The authors of the above study cite the potential of vitamin A supplementation in pregnant females who are known to carry an RBP4 mutation with retinyl ester which utilizes an RBP independent pathway to deliver retinoids from the maternal intestines directly to the placenta and ultimately is uptaken by the fetus The key would be to supplement during the first several months of life when the eye begins to develop as supplementing later in pregnancy would be too late to avoid any potential MAC disease See also editRetinol Adipokine Transthyretin TTR References edit a b c GRCh38 Ensembl release 89 ENSG00000138207 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000024990 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 doi 10 3109 03009738709178685 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 S2CID 37896530 a b Entrez Gene RBP4 retinol binding protein 4 plasma a b Cioffi CL Dobri N Freeman EE Conlon MP Chen P Stafford DG Schwarz DM Golden KC Zhu L Kitchen DB Barnes KD Racz B Qin Q Michelotti E Cywin CL Martin WH Pearson PG Johnson G Petrukhin K September 2014 Design synthesis and evaluation of nonretinoid retinol binding protein 4 antagonists for the potential treatment of atrophic age related macular degeneration and Stargardt disease Journal of Medicinal Chemistry 57 18 7731 57 doi 10 1021 jm5010013 PMC 4174998 PMID 25210858 Kanai M Raz A Goodman DS September 1968 Retinol binding protein the transport protein for vitamin A in human plasma The Journal of Clinical Investigation 47 9 2025 44 doi 10 1172 jci105889 PMC 297364 PMID 5675424 Naylor HM Newcomer ME March 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 Radu RA Han Y Bui TV Nusinowitz S Bok D Lichter J Widder K Travis GH Mata NL December 2005 Reductions in serum vitamin A arrest accumulation of toxic retinal fluorophores a potential therapy for treatment of lipofuscin based retinal diseases Investigative Ophthalmology amp Visual Science 46 12 4393 401 doi 10 1167 iovs 05 0820 PMID 16303925 Yang Q Graham TE Mody N Preitner F Peroni OD Zabolotny JM Kotani K Quadro L Kahn BB July 2005 Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes Nature 436 7049 356 62 Bibcode 2005Natur 436 356Y doi 10 1038 nature03711 PMID 16034410 S2CID 4343960 Herman MA Kahn BB July 2006 Glucose transport and sensing in the maintenance of glucose homeostasis and metabolic harmony The Journal of Clinical Investigation 116 7 1767 75 doi 10 1172 JCI29027 PMC 1483149 PMID 16823474 Moraes Vieira PM Yore MM Dwyer PM Syed I Aryal P Kahn BB March 2014 RBP4 activates antigen presenting cells leading to adipose tissue inflammation and systemic insulin resistance Cell Metabolism 19 3 512 26 doi 10 1016 j cmet 2014 01 018 PMC 4078000 PMID 24606904 Galic S Oakhill JS Steinberg GR March 2010 Adipose tissue as an endocrine organ Molecular and Cellular Endocrinology 316 2 129 39 doi 10 1016 j mce 2009 08 018 PMID 19723556 S2CID 7385199 Chou CM Nelson C Tarle SA Pribila JT Bardakjian T Woods S Schneider A Glaser T April 2015 Biochemical Basis for Dominant Inheritance Variable Penetrance and Maternal Effects in RBP4 Congenital Eye Disease Cell 161 3 634 646 doi 10 1016 j cell 2015 03 006 PMC 4409664 PMID 25910211 Further reading editQuadro L Hamberger L Colantuoni V Gottesman ME Blaner WS December 2003 Understanding the physiological role of retinol binding protein in vitamin A metabolism using transgenic and knockout mouse models Molecular Aspects of Medicine 24 6 421 30 doi 10 1016 S0098 2997 03 00038 4 PMID 14585313 Newcomer ME Ong DE October 2000 Plasma retinol binding protein structure and function of the prototypic lipocalin Biochimica et Biophysica Acta BBA Protein Structure and Molecular Enzymology 1482 1 2 57 64 doi 10 1016 s0167 4838 00 00150 3 PMID 11058747 Fex G Hansson B February 1979 Retinol binding protein from human urine and its interaction with retinol and prealbumin European Journal of Biochemistry 94 1 307 13 doi 10 1111 j 1432 1033 1979 tb12896 x PMID 571335 Rask L Anundi H Peterson PA August 1979 The primary structure of the human retinol binding protein FEBS Letters 104 1 55 8 doi 10 1016 0014 5793 79 81084 4 PMID 573217 S2CID 8540537 Fex G Albertsson PA Hansson B September 1979 Interaction between prealbumin and retinol binding protein studied by affinity chromatography gel filtration and two phase partition European Journal of Biochemistry 99 2 353 60 doi 10 1111 j 1432 1033 1979 tb13263 x PMID 574085 Monaco HL Zanotti G April 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 S2CID 34994569 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 S2CID 21613341 D Onofrio C Colantuoni V Cortese R August 1985 Structure and cell specific expression of a cloned human retinol binding protein gene the 5 flanking region contains hepatoma specific transcriptional signals The EMBO Journal 4 8 1981 9 doi 10 1002 j 1460 2075 1985 tb03881 x PMC 554451 PMID 2998779 Pfeffer BA Clark VM Flannery JG Bok D July 1986 Membrane receptors for retinol binding protein in cultured human retinal pigment epithelium Investigative Ophthalmology amp Visual Science 27 7 1031 40 PMID 3013795 Kameko M Ichikawa M Katsuyama T Kanai M Kato M Akamatsu T April 1986 Immunohistochemical localization of plasma retinol binding protein and prealbumin in human pancreatic islets The Histochemical Journal 18 4 164 8 doi 10 1007 BF01676116 PMID 3525470 S2CID 2959823 Siegenthaler G Saurat JH April 1987 Loss of retinol binding properties for plasma retinol binding protein in normal human epidermis The Journal of Investigative Dermatology 88 4 403 8 doi 10 1111 1523 1747 ep12469731 PMID 3559267 Rask L Vahlquist A Peterson PA November 1971 Studies on two physiological forms of the human retinol binding protein differing in vitamin A and arginine content The Journal of Biological Chemistry 246 21 6638 46 doi 10 1016 S0021 9258 19 34162 6 PMID 5132677 Colantuoni V Romano V Bensi G Santoro C Costanzo F Raugei G Cortese R November 1983 Cloning and sequencing of a full length cDNA coding for human retinol binding protein Nucleic Acids Research 11 22 7769 76 doi 10 1093 nar 11 22 7769 PMC 326530 PMID 6316270 Newcomer ME Jones TA Aqvist J Sundelin J Eriksson U Rask L Peterson PA July 1984 The three dimensional structure of retinol binding protein The EMBO Journal 3 7 1451 4 doi 10 1002 j 1460 2075 1984 tb01995 x PMC 557543 PMID 6540172 Rask L Anundi H Bohme J Eriksson U Ronne H Sege K Peterson PA February 1981 Structural and functional studies of vitamin A binding proteins Annals of the New York Academy of Sciences 359 1 79 90 Bibcode 1981NYASA 359 79R doi 10 1111 j 1749 6632 1981 tb12739 x PMID 6942701 S2CID 5781208 Jaconi S Rose K Hughes GJ Saurat JH Siegenthaler G June 1995 Characterization of two post translationally processed forms of human serum retinol binding protein altered ratios in chronic renal failure Journal of Lipid Research 36 6 1247 53 doi 10 1016 S0022 2275 20 41132 0 PMID 7666002 Berni R Malpeli G Folli C Murrell JR Liepnieks JJ Benson MD September 1994 The Ile 84 gt Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol binding protein The Journal of Biological Chemistry 269 38 23395 8 doi 10 1016 S0021 9258 17 31527 2 PMID 8089102 Seeliger MW Biesalski HK Wissinger B Gollnick H Gielen S Frank J Beck S Zrenner E January 1999 Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis Investigative Ophthalmology amp Visual Science 40 1 3 11 PMID 9888420 External links editRBP4 protein human at the U S National Library of Medicine Medical Subject Headings MeSH Overview of all the structural information available in the PDB for UniProt P02753 Retinol binding protein 4 at the PDBe KB Retrieved from https en wikipedia org w index php title Retinol binding protein 4 amp oldid 1222977796, wikipedia, wiki, book, books, library,
