scholarly journals Role of conserved residues in structure and stability: Tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily

2009 ◽  
Vol 10 (11) ◽  
pp. 2301-2316 ◽  
Author(s):  
Lesley H. Greene ◽  
Evangelia D. Chrysina ◽  
Laurence I. Irons ◽  
Anastassios C. Papageorgiou ◽  
K. Ravi Acharya ◽  
...  
Keyword(s):  
Human Serum ◽  
Binding Protein ◽  
Protein A ◽  
Retinol Binding Protein ◽  
Serum Retinol ◽  
Conserved Residues ◽  
Structure And Stability

scholarly journals Retinol Binding Protein 4 Levels relate to the presence and severity of coronary artery disease

2021 ◽  
Author(s):  
Gokay Nar ◽  
Sara Cetin Sanlialp ◽  
Rukiye Nar
Keyword(s):  
Coronary Artery Disease ◽  
Coronary Artery ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Serum Retinol ◽  
Retinol Binding Protein 4 ◽  
Coronary Syndrome ◽  
Artery Disease ◽  
The Relationship

Background: The prevous studies has showed that serum retinol binding protein 4 (RBP4) levels increased in metobolic disorders which are closely associated with cardiovascular dieases (CVD).  However the human studies investigating the role of RBP4 in CVD are conflicted. Therefore, we aimed to evaluate the relationship between RBP4 and the presence and the severity of coronary artery disease (CAD) in this study. Methods: 55 patients with presenting acute coronary syndrome (ACS) and 43 control subjects who had various cardiovascular risk factors with normal coronary artery on coronary angiography were included in this study.The serum RBP4 concentrations were measured using ELISA method and clinically and anatomically score models were used to asses the severity of coronary lesion. Results: Serum RBP4 level was significantly higher in patients with ACS compared to the controls (68.40 ± 47.94 mg/L vs. 49.46 ± 13.64 mg/L; p = 0.014).  RBP4 was correlated with GENSINI and SYNTAX I score (r = 0,286 p=0,034; r = 0.403 p = 0.002 respectively). However, there was no relationship between RBP4 and GRACE score. Conclusion: Patients with ACS had increased serum RBP4 levels and its high levels were correlated with CAD severity.

Serum retinol‐binding protein: a novel biomarker for recalcitrant cutaneous warts

2019 ◽  
Vol 58 (12) ◽  
pp. 1435-1438 ◽  
Author(s):  
Fatma El‐Esawy ◽  
Amany I. Mustafa ◽  
Ola El‐Shimi
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Retinol Binding Protein ◽  
Serum Retinol ◽  
Cutaneous Warts

Analysis of normal and truncated holo- and apo-retinol-binding protein (RBP) in human serum: altered ratios in chronic renal failure

1996 ◽  
Vol 134 (5) ◽  
pp. 576-582 ◽  
Author(s):  
Stefano Jaconi ◽  
Jean-Hilaire Saurat ◽  
Georges Siegenthaler
Keyword(s):  
Renal Failure ◽  
Chronic Renal Failure ◽  
Human Serum ◽  
Binding Protein ◽  
Normal Serum ◽  
Retinol Binding Protein ◽  
Hypervitaminosis A ◽  
Analytical Strategy ◽  
Almost All

Jaconi S, Saurat J-H, Siegenthaler G. Analysis of normal and truncated holo- and apo-retinol-binding protein (RBP) in human serum: altered ratios in chronic renal failure. Eur J Endocrinol 1996;134:576–82. ISSN 0804–4643 Retinol, the precursor of the retinoic acid hormone, is transported in the serum by a specific carrier, the retinol-binding protein (RBP). Compared to serum of healthy controls, the serum of patients with chronic renal failure (CRF) contains markedly increased levels of the RBP form truncated at the C-terminal, des(182Leu-183Leu). (RBP2). which suggests that RBP2 is cleared by the kidney in healthy people but accumulates in serum of CRF patients (Jaconi S, et al. J Lipid Res 1995;36:1247–53). To understand better the mechanism of retinol transport, we have developed a new analytical strategy to analyze the various forms of RBP that circulate in the blood: RBP with and without retinol (holo- and apo-RBP, respectively), RBP bound or not to transthyretin (TTR) and to determine in which of these forms RBP2 circulates. We confirm, but now by direct measurement, that holo-RBP and, to a larger extent, apo-RBP are increased in CRF serum compared to normal serum. We also show that almost all apo-RBP and about 50% of total holo-RBP, corresponding to RBP excess in CRF serum, circulate free and are not complexed to TTR, the remaining 50% being complexed to TTR. This observation suggests that the high levels of free holo-RBP, not bound to TTR, which correspond to the increase in total RBPs measured in CRF serum, may alter the tissue uptake of retinol and be responsible for the signs of hypervitaminosis A observed in these patients. Secondly, we found that the truncation resulting in RBP2 does not alter its binding properties for retinol nor those of holo-RBP2 for TTR. We observed that the high amounts of free holo-RBP2 and holo-RBP in sera of CRF patients were low in normal serum, suggesting that these forms are cleared by the kidney in normal conditions. The possible role of free holo-RBPs is discussed in the context of retinol recycling. Georges Siegenthaler, Clinique de Dermatologie, Hôpital Cantonal Universitaire, CH-1211 Geneve 14, Switzerland

Characterization of the Molten Globule of Human Serum Retinol-Binding Protein Using NMR Spectroscopy†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (31) ◽  
pp. 9475-9484 ◽  
Author(s):  
Lesley H. Greene ◽  
Ramani Wijesinha-Bettoni ◽  
Christina Redfield
Keyword(s):  
Nmr Spectroscopy ◽  
Human Serum ◽  
Binding Protein ◽  
Molten Globule ◽  
Retinol Binding Protein ◽  
Serum Retinol

scholarly journals Expression of functional human retinol-binding protein in Escherichia coli using a secretion vector

1993 ◽  
Vol 296 (1) ◽  
pp. 209-215 ◽  
Author(s):  
A Sivaprasadarao ◽  
J B C Findlay
Keyword(s):  
Escherichia Coli ◽  
Signal Sequence ◽  
Binding Protein ◽  
Protein A ◽  
Retinol Binding Protein ◽  
Cell Surface Receptor ◽  
Serum Retinol ◽  
T7 Promoter ◽  
Secretion Vector ◽  
Surface Receptor

In order to express human serum retinol-binding protein (sRBP) in Escherichia coli in a form that is structurally indistinguishable from the native protein, we placed the coding sequence of the RBP cDNA next to that of the outer membrane protein A (OmpA) signal sequence in the secretion vector, pIN-III-OmpA1. However, this construct did not generate detectable expression of RBP in E. coli. When the DNA fragment consisting of the ribosome-binding site and the OmpA-RBP fusion sequence was subcloned downstream to the T7 promoter of pKS-Bluescript, however, the resultant construct (pOmp-RBP2) gave low but detectable secretion of RBP into the periplasm. Deletion of the 3′ untranslated region of the RBP cDNA (pOmp-RBP3) further improved the expression (by approx. 20-fold). After charging with retinol, the secreted RBP was purified from the periplasm on a transthyretin-affinity resin. The purified protein exhibited all the three molecular recognition properties characteristic of sRBP, i.e. it interacted with retinol, transthyretin and its cell-surface receptor. Comparison of the receptor binding properties of the recombinant RBP (rRBP) with those of the serum protein revealed that while the affinity of rRBP is similar to sRBP (50 +/- 20 nM), the Bmax of the rRBP is about 6-8-fold higher. This indicates that a major proportion of RBP, isolated from serum, is incapable of interacting with the receptor.

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