Retinol-binding protein 4 (RBP4) is a specific transporter of retinol and was recently identified as an adipokine potentially involved in type 2 diabetes in humans and rodents. However, the function and structure of feline RBP4 have not been reported. In this study, we describe the molecular cloning and expression analysis of feline RBP4. The complete feline RBP4 cDNA encodes a precursor protei...

Retinol-binding protein 4 (RBP4) is a plasma protein involved in retinol transportation, and recent evidence in rodents suggests that RBP4 is also a metabolic regulator that modifies insulin sensitivity. To assess how RBP4 levels are regulated in ruminants, we determined the RBP4 concentrations in bovine plasma and milk using Western blot analysis. Plasma RBP4 levels in non-pregnant non-lactati...

The fat-soluble vitamin A has, of necessity, to be transported in the body by carrier proteins since it functions in an aqueous environment. At the same time, control of the distribution of the alcohol form, via specific retinol-binding proteins (RBP), provides additional physiological advantages. The concentration of the amphiphilic molecule is more easily limited in tissue fluids where, if fr...

Background & Objective: Diabetic retinopathy (DR) is a common microvascular complication of type 2 diabetes mellitus (T2DM) and the leading cause of vision loss in working-age adults. Vitamin A (retinol) has a role in the mechanism of vision process and retinol binding protein-4 (RBP4), is a carrier of vitamin A, and as an adipokine may be associated with increased risk for insulin resistance a...

The binding and metabolism of [3H]vitamin A-containing chylomicron (CM) remnants by the human hepatoma cell line HepG2 were studied. Mesenteric lymph chylomicrons were collected from [3H]retinol-fed rats and incubated with lipoprotein lipase to obtain CM remnants. At 4 degrees C, specific CM remnant binding was inhibited by an excess of unlabeled CM remnants. Specific binding predominated at lo...

Prealbumin was isolated from human plasma by chromatography on columns of diethylaminoethyl Sephadex and Sephadex G-200, followed by preparative polyacrylamide gel electrophoresis. The prealbumin was homogeneous in the analytical ultracentrifuge with an s=z~,~ of 3.7 S and with a molecular weight of about 50,000. Prealbumin formed a protein-protein complex with plasma retinol-binding protein in...