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

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 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.

scholarly journals Purification and characterization of a uterine retinol-binding protein in the bitch

1995 ◽  
Vol 311 (2) ◽  
pp. 407-415 ◽  
Author(s):  
W C Buhi ◽  
I M Alvarez ◽  
V M Shille ◽  
M J Thatcher ◽  
J P Harney ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Sequences ◽  
Binding Protein ◽  
Amino Acid Content ◽  
Amino Acid Sequences ◽  
Retinol Binding Protein ◽  
Total Amino Acid ◽  
Major Protein ◽  
Serum Retinol ◽  
Two Dimensional Gel Electrophoresis

A major canine endometrial secreted protein (cP6, 23,000-M(r)) was purified by ion-exchange and gel-filtration chromatography and characterized by two-dimensional gel electrophoresis. Anti-[human retinol-binding protein (hRBP)] serum identified cP6 on immunoblot analysis and immunoprecipitated cP6 from culture medium. This major protein was also shown to bind [3H]retinol. N-terminal and internal amino acid sequences were determined and compared with previously identified protein, RNA, or DNA sequences. N-terminal analysis revealed that cP6 had high identity and similarity to serum retinol-binding proteins (RBPs), while internal sequence analysis showed a strong similarity to rat androgen-dependent epididymal protein and beta-lactoglobulins. Amino acid analysis, however, showed significant differences between these proteins and cP6 in both total amino acid content and certain selected amino acids. Immunohistochemical analysis showed staining for RBP only in the uterine luminal epithelium. These studies suggest that bitch endometrium secretes a family of proteins (cP6), some of which bind [3H]retinol, are immunologically related to the RBP family, and have N-terminal and internal sequences with a high similarity to RBP, beta-lactoglobulins and other members of the lipocalin family. This family of proteins may be important in early development for supplying retinol or derivatives to the developing embryo.

scholarly journals Serum Retinol-Binding Protein 4 (RBP4) and retinol in a cohort of borderline obese women with and without gestational diabetes

2010 ◽  
Vol 43 (3) ◽  
pp. 320-323 ◽  
Author(s):  
Beverly J. Tepper ◽  
Youn-Kyung Kim ◽  
Varsha Shete ◽  
Elena Shabrova ◽  
Loredana Quadro
Keyword(s):  
Gestational Diabetes ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Obese Women ◽  
Serum Retinol ◽  
Retinol Binding Protein 4

scholarly journals Serum retinol-binding protein 4 concentrations in response to short-term overfeeding in normal-weight, overweight, and obese men

2007 ◽  
Vol 86 (5) ◽  
pp. 1310-1315 ◽  
Author(s):  
Jennifer Shea ◽  
Edward Randell ◽  
Sudesh Vasdev ◽  
Peizhong Peter Wang ◽  
Barbara Roebothan ◽  
...  
Keyword(s):  
Binding Protein ◽  
Normal Weight ◽  
Retinol Binding Protein ◽  
Serum Retinol ◽  
Short Term ◽  
Retinol Binding Protein 4
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