HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Smith, J. E. Articles by Goodman, D. S. Search for Related Content PubMed PubMed Citation Articles by Smith, J. E. Articles by Goodman, D. S. Social Bookmarking                      What's this?

Journal of Lipid Research, Vol 16, 318-323, Copyright © 1975 by Lipid Research, Inc.

ARTICLES

Tissue distribution and subcellular localization of retinol-binding protein in normal and vitamin A-deficient rats

JE Smith, Y Muto and DS Goodman

Levels of retinol-binding (RBP), the plasma transport protein for vitamin A, were measured by radioimmunoassay in sera and in a large number of tissues from both normal and vitamin A-deficient rats. The tissues included liver, kidney, fat, muscle, brain, eye, salivary gland, thymus, lung, heart, intestine, spleen, adrenal, testes, thyroid, and red blood cells. The RBP levels in tissues other than serum, liver, and kidneys varied from 12 mug/g of tissue for normal spleen to an undetectable level in red blood cells. Much of the RBP in the tissues with low levels may have been due to residual serum in the samples. In general, except for liver, RBP levels were lower in tissues from vitamin A-deficient rats than in those from normal rats. In normal rats, the liver, kidney, and serum levels were 30 plus or minus 4 (mean plus orminus SEM), 151 plus or minus 22, and 44 plus or minus 3 mug/g, respectively. In vitamin A-deficient rats, the liver RBP level was about three times the normal level whereas the kidney and serum levels were about one-fifth the normal values. When normal liver homogenates were fractionated by centrifugation, 67% of the RBP was recovered in the microsomal fraction and only 9% was found in the soluble 105,000 g supernate. In contrast, 76% of the RBP in homogenates of normal kidneys was in the soluble fraction. Similar results were obtained with deficient livers and kidneys. Incubation with deoxycholate released the liver RBP into the soluble fraction. RBP is produced in the liver and removed from the blood by the kidneys. The levels of RBP in normal and deficient liver, serum, and kidney appear to reflect the relative rates of RBP secretion and turnover.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H. D. Dawson, Y. Yamamoto, R. Zolfaghari, F. J. Rosales, J. Dietz, T. Shimada, N.-q. Li, and A. C. Ross Regulation of Hepatic Vitamin A Storage in a Rat Model of Controlled Vitamin A Status during Aging J. Nutr., May 1, 2000; 130(5): 1280 - 1286. [Abstract] [Full Text]

				F. J. Rosales and A. C. Ross A Low Molar Ratio of Retinol Binding Protein to Transthyretin Indicates Vitamin A Deficiency during Inflammation: Studies in Rats and A Posteriori Analysis of Vitamin A-Supplemented Children with Measles J. Nutr., October 1, 1998; 128(10): 1681 - 1687. [Abstract] [Full Text]

				F. J. Rosales and A. C. Ross Acute Inflammation Induces Hyporetinemia and Modifies the Plasma and Tissue Response to Vitamin A Supplementation in Marginally Vitamin A-Deficient Rats J. Nutr., June 1, 1998; 128(6): 960 - 966. [Abstract] [Full Text]