Spatial Distribution of Retinol-Binding Protein and Retinyl Palmitate Hydrolase Activity in Normal and Vitamin A-Deficient Rat Liver

1985 ◽  
Vol 115 (7) ◽  
pp. 856-864 ◽  
Author(s):  
William S. Blaner ◽  
John Edgar Smith ◽  
Ralph B. Dell ◽  
DeWitt S. Goodman
1998 ◽  
Vol 1380 (1) ◽  
pp. 10-20 ◽  
Author(s):  
John Edgar Smith ◽  
Lynne M DeMoor ◽  
Caroline E Handler ◽  
Edna L Green ◽  
Steven J Ritter

2002 ◽  
Vol 82 (3) ◽  
pp. 461-463 ◽  
Author(s):  
M. E. R. Dugan ◽  
D. C. Rolland ◽  
D. R. Best ◽  
W. J. Meadus

Banni et al. (1999) indicated feeding conjugated linoleic acid (CLA) increases rat liver retinol and retinyl-ester levels. We wanted to determine if feeding CLA would affect pig vitamin A status. Feeding 0.5% CLA did not increase pig liver retinyl-palmitate but did increase retinol from 1.56 to 2.56 109g g-1 (P < 0.05) and the level of retinol binding protien mRNA relative to actin mRNA (P < 0.05). Key words: Conjugated linoleic acid, pig, vitamin A, retinol, retinol binding protein


1982 ◽  
Vol 47 (2) ◽  
pp. 273-280 ◽  
Author(s):  
D. Sklan ◽  
Susan Donoghue

1. Serum and intracellular distribution of retinol was determined in equines maintained on four levels of vitamin A intake.2. The form of retinol transported in serum was determined by gel filtration and chromatography to be a complex of retinol bound to a protein of molecular weight (MW) of approximately 20000, which was in turn complexed probably with prealbumin to yield a complex with a MW of 75000 to 80000.3. Increasing dietary vitamin A levels enhanced the concentration of lipoprotein-bound retinyl esters in the plasma.4. Vitamin A in the liver cytosol was found predominantly as retinyl esters in a lipid–protein aggregate of MW approximately 2 × 106 and hydrated density of 1·063–1·111. In the kidney and adrenal gland, two Iipid–protein entitites were found with MW of approximately 1·8 × 106 and 1·7 × 105 respectively. These fractions contained approximately 40 and 20% lipid respectively and had densities of 1·063–1·111 and approximately 1·21.5. All lipid–protein aggregates were associated with retinyl palmitate hydrolase activity and guanidine treatment released a 15000 MW material, presumably intracellular retinol-binding protein.6. Increasing dietary vitamin A enhanced the proportion of retinol in the 1·7 × 105 fraction.7. Findings in equine plasma and liver resemble previous observations in other species. The characterization of two new lipid–protein aggregates in equine kidney and adrenal glands, which have hydrolase activity, may be important in intracellular retinol transport and metabolism, especially in animals subjected to high intakes of vitamin A.


1975 ◽  
Vol 19 (2) ◽  
pp. 379-394
Author(s):  
A.R. Poole ◽  
J.T. Dingle ◽  
A.K. Mallia ◽  
D.S. Goodman

The localization of immunoreactive retinol-binding protein (RBP) in rat liver was studied by immunofluorescence microscopy. The study employed specific antisera to rat RBP prepared in a rabbit and in a sheep. The indirect, two-stage method of localizing tissue antigens was employed, and livers of both normal and vitamin A-deficient rats were examined. Fab' fragments of immunoglobulins were used, to minimize non-specific labelling of the frozen sections of liver. With these techniques, the specific immune staining of RBP was observed within liver parenchymal cells. This staining appeared as both particulate and diffuse within the cytoplasm of the parenchymal cells, and was not concentrated within one region of the liver cell or lobule. Staining for RBP was not observed in nuclei or in cells other than parenchymal cells. Similar particulate and diffuse immune staining for RBP was observed in liver sections from both vitamin A-deficient and normal rats. More intense immune staining appeared to be present in the sections of vitamin A-deficient animals, in good correlation with the expected higher levels of RBP in deficient as compared to normal liver. When liver sections were exposed to an antiserum to rat albumin, instead of one to rat RBP, immune cytoplasmic staining was observed which was entirely of a diffuse nature, and did not appear particulate or granular. The findings suggest that RBP, unlike albumin, is localized in part within cytoplasmic vesicles or granules which are large enough to be detected with immunofluorescence, and which are present in livers of both normal and vitamin A-deficient animals. The nature of these putative RBP-containing particles remains to be explored.


1981 ◽  
Vol 256 (15) ◽  
pp. 8162-8163 ◽  
Author(s):  
M.E. Newcomer ◽  
A. Liljas ◽  
U. Eriksson ◽  
J. Sundelin ◽  
L. Rask ◽  
...  
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