The effect of progesterone on the synthesis of retinol-binding protein by Japanese quail liver in vitro

1980 ◽  
Vol 8 (3) ◽  
pp. 302-303
Author(s):  
R. RANJINI RAO ◽  
DAVID J. HEAF ◽  
JOHN GLOVER
Keyword(s):  
Japanese Quail ◽  
Binding Protein ◽  
Retinol Binding Protein

Retinoids: in vitro interaction with retinol‐binding protein and influence on plasma retinol

1993 ◽  
Vol 7 (12) ◽  
pp. 1179-1184 ◽  
Author(s):  
Rodolfo Berni ◽  
Monica Clerici ◽  
Giorgio Malpeli ◽  
Loredana Cleris ◽  
Franca Formelli
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Plasma Retinol ◽  
In Vitro Interaction

scholarly journals Preparative Scale Production of Recombinant Human Transthyretin for Biophysical Studies of Protein-Ligand and Protein-Protein Interactions

2020 ◽  
Vol 21 (24) ◽  
pp. 9640
Author(s):  
Ellen Y. Cotrina ◽  
Marta Vilà ◽  
Joan Nieto ◽  
Gemma Arsequell ◽  
Antoni Planas
Keyword(s):  
Binding Protein ◽  
Amyloid Β ◽  
Retinol Binding Protein ◽  
Familial Amyloidotic Polyneuropathy ◽  
Main Role ◽  
Scale Production ◽  
In Vitro Screening ◽  
Preparative Scale ◽  
Screening Assays

Human transthyretin (hTTR), a serum protein with a main role in transporting thyroid hormones and retinol through binding to the retinol-binding protein, is an amyloidogenic protein involved in familial amyloidotic polyneuropathy (FAP), familial amyloidotic cardiomyopathy, and central nervous system selective amyloidosis. hTTR also has a neuroprotective role in Alzheimer disease, being the major Aβ binding protein in human cerebrospinal fluid (CSF) that prevents amyloid-β (Aβ) aggregation with consequent abrogation of toxicity. Here we report an optimized preparative expression and purification protocol of hTTR (wt and amyloidogenic mutants) for in vitro screening assays of TTR ligands acting as amyloidogenesis inhibitors or acting as molecular chaperones to enhance the TTR:Aβ interaction. Preparative yields were up to 660 mg of homogenous protein per L of culture in fed-batch bioreactor. The recombinant wt protein is mainly unmodified at Cys10, the single cysteine in the protein sequence, whereas the highly amyloidogenic Y78F variant renders mainly the S-glutathionated form, which has essentially the same amyloidogenic behavior than the reduced protein with free Cys10. The TTR production protocol has shown inter-batch reproducibility of expression and protein quality for in vitro screening assays.

scholarly journals Endocytosis and degradation of interstitial retinol-binding protein: differential capabilities of cells that border the interphotoreceptor matrix.

1985 ◽  
Vol 100 (5) ◽  
pp. 1676-1681 ◽  
Author(s):  
J G Hollyfield ◽  
H H Varner ◽  
M E Rayborn ◽  
G I Liou ◽  
C D Bridges
Keyword(s):  
Acid Phosphatase ◽  
Binding Protein ◽  
Pigment Epithelium ◽  
Retinol Binding Protein ◽  
Apical Plasma Membrane ◽  
Multivesicular Bodies ◽  
Cone Photoreceptors ◽  
Interphotoreceptor Matrix ◽  
Rod And Cone Photoreceptors

Between the pigment epithelium and the outer limiting membrane of the retina is an extracellular compartment filled with the interphotoreceptor matrix (IPM). A prominent component of the IPM is a glycoprotein known as interstitial retinol-binding protein (IRBP). Using in vitro techniques, we compared the ability of the cells that border this compartment to internalize colloidal gold (CG) coated with either IRBP or ovalbumin, a glycoprotein not found in the IPM. Neither IRBP-CG nor ovalbumin-CG was internalized by the Muller's cells. Both rod and cone photoreceptors take up IRBP-CG, which is observed in small vesicles and multivesicular bodies. Neither photoreceptor type takes up ovalbumin-CG. Acid phosphatase cytochemistry indicates that acid phosphatase reaction product in the multivesicular bodies co-localizes with IRBP-CG, which suggests that this molecule is degraded by rod and cone photoreceptors and is not recycled. The pigment epithelium internalizes IRBP-CG and ovalbumin-CG, both of which remain in small cytoplasmic vesicles near the apical plasma membrane. There is no indication that vesicles that contain either IRBP-CG or ovalbumin-CG fuse with the lysosomal system in the pigment epithelial cells during the incubation.

RETINOL-BINDING PROTEIN METABOLISM IN LIVER CELLS IN VIVO AND IN VITRO

1981 ◽  
Vol 359 (1 Modulation of) ◽  
pp. 171-180 ◽  
Author(s):  
John Edgar Smith ◽  
Carmia Borek ◽  
DeWitt S. Goodman
Keyword(s):  
Protein Metabolism ◽  
Binding Protein ◽  
Liver Cells ◽  
Retinol Binding Protein

Retinol uptake from retinol-binding protein (RBP) by liver parenchymal cells in vitro does not specifically depend on its binding to RBP

Biochemistry ◽  
1993 ◽  
Vol 32 (7) ◽  
pp. 1727-1733 ◽  
Author(s):  
Ariette M. Van Bennekum ◽  
William S. Blaner ◽  
Ingrid Seifert-Bock ◽  
Maria Moukides ◽  
Adriaan Brouwer ◽  
...  
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Liver Parenchymal ◽  
Parenchymal Cells

scholarly journals Changes in plasma concentrations of thyroxine binding prealbumin and retinol binding protein in Japanese quail after hatching

1980 ◽  
Vol 44 (3) ◽  
pp. 287-293 ◽  
Author(s):  
D. J. Heaf ◽  
M. El-Sayed ◽  
J. Glover
Keyword(s):  
Japanese Quail ◽  
Total Protein ◽  
Protein Concentration ◽  
Binding Protein ◽  
Plasma Concentrations ◽  
Coturnix Japonica ◽  
Retinol Binding Protein ◽  
Free Access ◽  
Coturnix Coturnix ◽  
Access To Food

1. Male and female Japanese quail (Coturnix coturnix japonica) were reared under short daily photoperiods (8 h light–16 h dark) to inhibit sexual development with free access to food and water. Blood was sampled at frequent intervals for 13 weeks from hatching in order to monitor the developmental changes in plasma concentrations of the two proteins which are important in the transport of retinol, retinol-binding protein (RBP) and thyroxine-binding prealbumin (TBPA).2. Measurements of body-weight, blood packed cell volume and plasma total protein concentration showed that the birds had a normal pattern of growth and haematological development. Plasma concentrations of TBPA, total immunoreactive RBP (IRBP) and holoRBP were 220, 60 and 45 μg/ml respectively in 1-d-old quail and rose to 430, 165 and 140 μg/ml at 14 d of age, which was 10 d after the corresponding change in total protein. Neither RBP nor TBPA concentrations were significantly different between the sexes during the 13 weeks, but there were minor fluctuations in concentration within relatively narrow limits.

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