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Human RBP4 Protein expressed in Human Cells - ABIN2002658
Colantuoni, Romano, Bensi, Santoro, Costanzo, Raugei, Cortese: Cloning and sequencing of a full length cDNA coding for human retinol-binding protein. in Nucleic acids research 1984
Show all 8 Pubmed References
Mouse (Murine) RBP4 Protein expressed in Human Cells - ABIN2007447
Quadro, Blaner, Hamberger, Van Gelder, Vogel, Piantedosi, Gouras, Colantuoni, Gottesman: Muscle expression of human retinol-binding protein (RBP). Suppression of the visual defect of RBP knockout mice. in The Journal of biological chemistry 2002
Show all 6 Pubmed References
Human RBP4 Protein expressed in Human - ABIN2131515
Sharif, Hu, Klock, Hampton, Nigoghossian, Knuth, Matzen, Anderson, Trager, Uno, Glynne, Azarian, Caldwell, Brinker: Time-resolved fluorescence resonance energy transfer and surface plasmon resonance-based assays for retinoid and transthyretin binding to retinol-binding protein 4. in Analytical biochemistry 2009
Rat (Rattus) RBP4 Protein expressed in HEK-293 Cells - ABIN1344327
Casillas-Ramírez, Alfany-Fernández, Massip-Salcedo, Juan, Planas, Serafín, Pallàs, Rimola, Rodés, Peralta: Retinol-binding protein 4 and peroxisome proliferator-activated receptor-? in steatotic liver transplantation. in The Journal of pharmacology and experimental therapeutics 2011
Childhood RBP4 serves as a risk factor for subsequent development of metabolic syndrome and its components, independent of pediatric obesity.
In Caucasians 65 years and older, RBP4 serum levels are associated with a number of components of metabolic syndrome.
Baseline RBP4 levels and MELD scores predicted 21-day (=10 mg/L) and 1-year (>/=25) mortality, respectively. In critically ill patients with underlying liver disease, with a link to eGFRs, INRs and TC levels, the baseline RBP4 may serve as a marker for short-term mortality.
our study provides clinical evidence revealing that the serum concentrations of RBP4 were elevated in NAFLD patients in a Chinese population. These findings indicated that RBP4 might be a noninvasive molecular biomarker that detects the presence of NAFLD in middle-aged and elderly population.
Vitreous levels of APOA1 and RBP4 in human rhegmatogenous retinal detachment associated with choroidal detachment reflects the severity of disease.
The overexpression of RBP4 increased cell proliferation, whereas siRNA-mediated RBP4 knockdown significantly decreased HTR8/SVneo cell proliferation via activation of PI3K/AKT signaling.
High RBP4 expression is associated with hypertriglyceridemia.
We observed that knockdown of RBP4 can greatly suppress ovarian cancer cell migration and proliferation.
This study showed that the Levels of circulating RBP4 was significantly higher in Chronic Kidney Disease than in control.
Our results demonstrate that IR is associated with high circulating RBP4 and that suppressed RBP4 adipose tissue expression is accompanied by reduced GLUT4 expression in HD. Renal transplantation or HDF are effective in lowering serum RBP4 levels.
Data suggest that serum levels of RBP4 and LGAL3BP are up-regulated after menopause when complicated by NAFLD (non-alcoholic fatty liver disease); RBP4 and LGAL3BP may serve as biomarkers of NAFLD in postmenopausal women. (RBP4 = retinol binding protein 4; LGAL3BP = galectin-3 binding protein)
Elevated levels of RBP4 were not associated with an increased risk of ischemic stroke among women.
Study showed that dietary weight loss-induced changes in angiotensin-converting enzyme activity, free fatty acids and RBP4 independently contribute to weight regain prediction.
RBP4 is involved in all-trans retinoic acid-induced cleft palate.
the 1.5A resolution structures of human holo-RBP4 and of the protein saturated with palmitic and lauric acid and discuss the interaction of the fatty acids and retinol with the protein, are reported.
Circulating RBP4 levels may not be associated with nonalcoholic fatty liver disease.
Plasma PEDF and RBP4 identified insulin resistance in subjects with no prior diagnosis of diabetes.
Serum RBP4 level was significantly higher and closely associated with blood pressure in prehypertensive Chinese.
Conclusion RBP4 may be used as a predictive factor of diabetic nephropathy patients complicated with silent cerebral infarction (SCI) and is positively correlated with cognitive dysfunction. RBP4/Lp-PLA2/Netrin-1 pathway activation may be one of the occurrence mechanisms in diabetic nephropathy complicated with SCI.
these data demonstrate a key role of STRA6 and RBP4 in the maintenance of colon cancer self-renewal and that this pathway is an important link through which consumption of HFD contributes to colon carcinogenesis.
There were no statistical differences between the BB genotype and the AB genotype of ESR2 locus in regard to the examined traits. However, a noticeable superiority (P < 0.01) of the BB genotype compared to the homozygous AA genotype, adding almost 2 piglets/litter in TNB and NBA trait, was found.
RBP4 has a role in adipogenesis of porcine preadipocytes through the insulin signaling pathways
Data show that there were two genotypes for RBP4 gene in Tibet pig, which did not have significant effect on the reproductive traits.
The aim of this work was to study the effects on litter size of variants of the porcine genes RBP4, ESR1 and IGF2, currently used in genetic tests for different purposes.
Response to selection for increased litter size could not be attributed to effects at the estrogen receptor, retinol-binding protein or follistatin loci.
study found significant association of two diallelic polymorphisms in the porcine genes for leukaemia inhibitory factor (LIF) and retinol-binding protein 4 (RBP4) with number of piglets born alive (NBA) in two German pig lines
The results showed that the polymorphic sites of both PRLR and RBP4 genes are closely related to litter size traits.
progesterone modulates uterine RBP4 mRNA and protein abundance in a time- and concentration-dependent manner.
Two novel single nucleotide polymorphisms (SNPs) and 4-bp deletion mutation of RBP4 gene in Chinese cattle
results suggest that retinol-binding protein 4 is transferred from maternal stores to calves through colostrum
Serum albumin and serum retinol-binding protein(sRBP) are not components of bovine interphotoreceptor matrix(IPM). Serum albumin and sRBP can not participate in binding and transport of visual cycle retinoids in IPM of bovine retina.
RBP4-induced inflammation is largely mediated by TLR4.
New insights into ghrelin cell physiology, and given the known functions of RBP4 and TTR, support an emerging role for the ghrelin cell in blood glucose handling and metabolism.
Retinal degeneration in RBP4-Tg mice is RBP4-dependent and light-independent.
Rbp4-deficient mice accumulated retinol in the liver but it was undetectable in the serum, indicating an inverse relation between serum and liver retinol levels. RBP4 is critical for the mobilization of retinol from hepatic storage pools, and such mobilization is necessary for ocular development and visual function.
Hepatocytes Are the Principal Source of Circulating RBP4 in Mice
RBP4 may be a critical modulator promoting the vicious cycle of insulin resistance and heart failure by activating TLR4/MyD88-mediated inflammatory pathways. Potentially, lowering RBP4 might break the vicious cycle and improve both insulin resistance and cardiac hypertrophy.
Data (including data from studies in knockout mice) suggest that Rbp4 (plasma retinol-binding protein 4) is critical for antigen presentation and activation of CD4-positive T-lymphocyte in development of insulin resistance in mice obese due to high-fat diet.
A novel mechanism for circadian regulation of RBP4, but also a critical role of RBP4, acting as a hepatokine in the regulation of glucose metabolism by the circadian clock.
Elevated serum RBP4 raises BP.
These data show that decreasing circulating TTR levels or altering TTR-RBP4 binding could be a potential therapeutic approach for the treatment of type 2 diabetes.
findings suggest that RBP4 impaired in vivo adipogenesis, partly through the repression of the insulin pathway
The data implicate the involvement of chondrocytic Rbp4 in bone growth, particularly in the formation of the secondary ossification center of the limb.
Rbp4 and its membrane receptor STRA6 control adipogenesis by regulating cellular retinoid homeostasis and RARalpha activity.
STRA6 in tissues other than the eye appears to be the coupling of circulating holo-RBP levels to cell signaling, in turn regulating key processes such as insulin response.
expression of RBPR2 in liver and fat suggests a possible role in mediating established metabolic actions of RBP4 in those tissues
TTR blocks the ability of holo-retinol-binding protein to associate with STRA6 and thereby effectively suppresses both STRA6-mediated retinol uptake and STRA6-initiated cell signaling.
Suggest that RBP4 may be involved in the dyslipidemia associated with polycystic ovary syndrome in nonobese adolescents and that there may be an independent relationship between RBP4 and triglycerides but not between RBP4 and insulin resistance.
PPARgamma- and PPARalpha-mediated signaling controls RBP4 gene expression and releases in brown adipose tissue
RBP4 is not only an adipocytokine, but also a hepatic cytokine leading to metabolic syndrome, non-alcoholic fatty liver disease and type 2 diabetes.
these data support the model thatretinol binding protein 4 and retinoic acid precursors are present within the CSF and used for synthesis of retinoic acid, which promotes embryonic neuroepithelial survival
YSL-expressed Rbp4 plays a role in formation of both yolk extension and liver bud, the latter may also require migration of liver progenitor cells
STRA6 deficiency lead to accumulation of RBP-4 bound vitamin A and developmental abnormalities.
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.
, plasma retinol-binding protein
, retinol-binding protein 4
, retinol-binding protein 4, interstitial
, retinol-binding protein 4, plasma
, Plasma retinol-binding protein
, retinol binding protein 4, cellular
, serum retinol binding protein