Abstract
Portions of a 125I-iodinated bovine serum albumin preparation were exposed to freezing, acetic acid (pH 3.5, 3.0 or 2.5), urea or formaldehyde, and the effect of these treatments on the rates of pinocytic uptake by yolk sacs from 17.5-day-pregnant rats cultured in vitro and of clearance from the rat bloodstream were studied. Uptake of albumin by the yolk sac was followed by rapid release of [125I]iodo-L-tyrosine into the culture medium. Similarly clearance of albumin in vivo was accompanied by the appearance of trichloroacetic acid-soluble radioactivity in the bloodstream. In both systems the rates of uptake of modified albumin preparations formed a series: formaldehyde or urea greater than acetic acid greater than freezing. The increased rates of uptake of modified albumin preparations could not be ascribed to the formation of aggregates nor, in the yolk-sac system, to an increase in the rate of pinosome formation. It is concluded that the various treatments to which the albumin was subjected increase to varying degrees the affinity of the albumin molecule for binding sites on that region of the plasma membrane from which pinocytic vesicles are formed. Some comparable experiments with native and desialylated human orosomucoid indicate that the rat yolk-sac epithelial cells do not possess the recognition system for uptake of asialoglycoproteins that exists on the surface of hepatic parenchymal cells.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ashwell G., Morell A. G. The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv Enzymol Relat Areas Mol Biol. 1974;41(0):99–128. doi: 10.1002/9780470122860.ch3. [DOI] [PubMed] [Google Scholar]
- Bertini F., Mego J. L., McQueen J. D. Distribution in tissue homogenates, and the nature of the linkage of injected proteins to subcellular particles. J Cell Physiol. 1967 Aug;70(1):105–114. doi: 10.1002/jcp.1040700114. [DOI] [PubMed] [Google Scholar]
- Bocci V. Metabolism of plasma proteins. Arch Fisiol. 1970 Jul 31;67(4):314–444. [PubMed] [Google Scholar]
- Buys C. H., Dejong A. S., Bouma J. M., Gruber M. Rapid uptake by liver sinusoidal cells of serum albumin modified with retention of its compact conformation. Biochim Biophys Acta. 1975 May 5;392(1):95–100. doi: 10.1016/0304-4165(75)90169-5. [DOI] [PubMed] [Google Scholar]
- Buys C. H., Elferink M. G., Bouma J. M., Gruber M., Nieuwenhuis P. Proteolysis of formaldehyde-treated albumin in Kupffer cells and its inhibition by suramin. J Reticuloendothel Soc. 1973 Aug;14(2):209–223. [PubMed] [Google Scholar]
- Gregoriadis G., Morell A. G., Sternlieb I., Scheinberg I. H. Catabolism of desialylated ceruloplasmin in the liver. J Biol Chem. 1970 Nov 10;245(21):5833–5837. [PubMed] [Google Scholar]
- Hudgin R. L., Pricer W. E., Jr, Ashwell G., Stockert R. J., Morell A. G. The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins. J Biol Chem. 1974 Sep 10;249(17):5536–5543. [PubMed] [Google Scholar]
- Kerr M. A., Kenny A. J. The purification and specificity of a neutral endopeptidase from rabbit kidney brush border. Biochem J. 1974 Mar;137(3):477–488. doi: 10.1042/bj1370477. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- LaBadie J. H., Chapman K. P., Aronson N. N., Jr Glycoprotein catabolism in rat liver: Lysosomal digestion of iodinated asialo-fetuin. Biochem J. 1975 Nov;152(2):271–279. doi: 10.1042/bj1520271. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morell A. G., Gregoriadis G., Scheinberg I. H., Hickman J., Ashwell G. The role of sialic acid in determining the survival of glycoproteins in the circulation. J Biol Chem. 1971 Mar 10;246(5):1461–1467. [PubMed] [Google Scholar]
- Moxon L. A., Wild A. E. Localisation of proteins in coated micropinocytotic vesicles during transport across rabbit yolk sac endoderm. Cell Tissue Res. 1976 Aug 20;171(2):175–193. doi: 10.1007/BF00219405. [DOI] [PubMed] [Google Scholar]
- Normann S. J. Kinetics of phagocytosis. 3. Two colloid reactions, competitive inhibition, and degree of inhibition between similar and dissimilar foreign particles. Lab Invest. 1974 Sep;31(3):286–293. [PubMed] [Google Scholar]
- Normann S. J. Kinetics of phagocytosis. II. Analysis of in vivo clearance with demonstration of competitive inhibition between similar and dissimilar foreign particles. Lab Invest. 1974 Aug;31(2):161–169. [PubMed] [Google Scholar]
- Normann S. J. The kinetics of phagocytosis. 1. A study on the clearance of denatured bovine albumin and its competitive inhibition by denatured human albumin. J Reticuloendothel Soc. 1973 Dec;14(6):587–598. [PubMed] [Google Scholar]
- POORTMANS J. [Electrophoretic and immuno-electrophoretic analyses of heat-soluble proteins]. Clin Chim Acta. 1962 May;7:334–345. doi: 10.1016/0009-8981(62)90032-3. [DOI] [PubMed] [Google Scholar]
- Roberts A. V., Nicholls S. E., Griffiths P. A., Williams K. E., Lloyd J. B. A quantitative study of pinocytosis and lysosome function in experimentally induced lysosomal storage. Biochem J. 1976 Dec 15;160(3):621–629. doi: 10.1042/bj1600621. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sherman L. A., Harwig S., Hayne O. A. Macromolecular complexes formed as the result of chloramine-T radioiodination of proteins. Int J Appl Radiat Isot. 1974 Feb;25(2):81–85. doi: 10.1016/0020-708x(74)90103-3. [DOI] [PubMed] [Google Scholar]
- Williams K. E., Kidston E. M., Beck F., Lloyd J. B. Quantitative studies of pinocytosis. I. Kinetics of uptake of (125I)polyvinylpyrrolidone by rat yolk sac cultured in vitro. J Cell Biol. 1975 Jan;64(1):113–122. doi: 10.1083/jcb.64.1.113. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Williams K. E., Kidston E. M., Beck F., Lloyd J. B. Quantitative studies of pinocytosis. II. Kinetics of protein uptake and digestion by rat yolk sac cultured in vitro. J Cell Biol. 1975 Jan;64(1):123–134. doi: 10.1083/jcb.64.1.123. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Williams K. E., Lloyd J. B., Davies M., Beck F. Digestion of an exogenous protein by rat yolk-sac cultured in vitro. Biochem J. 1971 Nov;125(1):303–308. doi: 10.1042/bj1250303. [DOI] [PMC free article] [PubMed] [Google Scholar]