Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1980 Jun 15;188(3):649–656. doi: 10.1042/bj1880649

Different handling of parathyrin by basal-lateral and brush-border membranes of the bovine kidney cortex.

H Mohr, R D Hesch
PMCID: PMC1161945  PMID: 7470025

Abstract

The two parts of the bovine kidney cortex plasma membrane, the basal-lateral and the brush-border membrane, were simultaneously prepared from the same organ. Both types of membrane bound parathyrin, but only from the basal-lateral fraction was the hormone displaceable by its bioactive N-terminal fragment. In parallel, parathyrin-stimulated adenylate cyclase was predominantly found in basal-lateral membranes. The hormone was fragmented by both membrane types. Basal-lateral membranes generated fragments with a rather uniform size distribution (somewhat smaller than the intact peptide) and apparently preferred the hormone itself as a substrate. In contrast, the fragments produced by brush-border membranes were numberous small peptides.

Full text

PDF
649

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barrett P. Q., Neuman W. F. The cleavage and adsorption of parathyroid hormone at high dilution: implications for receptor binding studies. Biochim Biophys Acta. 1978 Jun 15;541(2):223–233. doi: 10.1016/0304-4165(78)90395-1. [DOI] [PubMed] [Google Scholar]
  2. Di Bella F. P., Dousa T. P., Miller S. S., Arnaud C. D. Parathyroid hormone receptors of renal cortex: specific binding of biologically active, 125I-labeled hormone and relationship to adenylate cyclase activation. Proc Natl Acad Sci U S A. 1974 Mar;71(3):723–726. doi: 10.1073/pnas.71.3.723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Duckworth W. C. Insulin and glucagon binding and degradation by kidney cell membranes. Endocrinology. 1978 Jun;102(6):1766–1774. doi: 10.1210/endo-102-6-1766. [DOI] [PubMed] [Google Scholar]
  4. Fass S. J., Hammerman M. R., Sacktor B. Transport of amino acids in renal brush border membrane vesicles. Uptake of the neutral amino acid L-alanine. J Biol Chem. 1977 Jan 25;252(2):583–590. [PubMed] [Google Scholar]
  5. George S. G., Kenny J. Studies on the enzymology of purified preparations of brush border from rabbit kidney. Biochem J. 1973 May;134(1):43–57. doi: 10.1042/bj1340043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [DOI] [PubMed] [Google Scholar]
  7. Hehrmann R., Wilke R., Nordmeyer J. P., Hesch R. D. Hochsensitiver, C-terminal-spezifischer Radioimmunoassay für menschliches Parathormon als Routinemethode. Dtsch Med Wochenschr. 1976 Nov 19;101(47):1726–1729. [PubMed] [Google Scholar]
  8. Hendler E. D., Torretti J., Epstein F. H. The distribution of sodium-potassium--activated adenosine triphosphatase in medulla and cortex of the kidney. J Clin Invest. 1971 Jun;50(6):1329–1337. doi: 10.1172/JCI106612. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hesch R. D., Ebel H., Hehrmann R., Jüppner H. Endocrinological aspects of PTH metabolism in the kidney. Contrib Nephrol. 1978;13:104–114. doi: 10.1159/000402138. [DOI] [PubMed] [Google Scholar]
  10. Hruska K. A., Martin K., Mennes P., Greenwalt A., Anderson C., Klahr S., Slatopolsky E. Degradation of parathyroid hormone and fragment production by the isolated perfused dog kidney. The effect of glomerular filtration rate and perfusate CA++ concentrations. J Clin Invest. 1977 Sep;60(3):501–510. doi: 10.1172/JCI108802. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kessler M., Acuto O., Storelli C., Murer H., Müller M., Semenza G. A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport systems. Biochim Biophys Acta. 1978 Jan 4;506(1):136–154. doi: 10.1016/0005-2736(78)90440-6. [DOI] [PubMed] [Google Scholar]
  12. Liang C. T., Sacktor B. Preparation of renal cortex basal-lateral and bursh border membranes. Localization of adenylate cyclase and guanylate cyclase activities. Biochim Biophys Acta. 1977 May 2;466(3):474–487. doi: 10.1016/0005-2736(77)90340-6. [DOI] [PubMed] [Google Scholar]
  13. Maack T., Mackensie D. D., Kinter W. B. Intracellular pathways of renal reabsorption of lysozyme. Am J Physiol. 1971 Dec;221(6):1609–1616. doi: 10.1152/ajplegacy.1971.221.6.1609. [DOI] [PubMed] [Google Scholar]
  14. Martin K. J., Hruska K. A., Lewis J., Anderson C., Slatopolsky E. The renal handling of parathyroid hormone. Role of peritubular uptake and glomerular filtration. J Clin Invest. 1977 Oct;60(4):808–814. doi: 10.1172/JCI108834. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Marx S. J., Fedak S. A., Aurbach G. D. Preparation and characterization of a hormone-responsive renal plasma membrane fraction. J Biol Chem. 1972 Nov 10;247(21):6913–6918. [PubMed] [Google Scholar]
  16. McIntosh C. H., Hesch R. D. Characterization of the parathyrin receptor in renal plasma membranes by labelled hormone and labelled antibody binding techniques. Biochim Biophys Acta. 1976 Mar 19;426(3):535–546. doi: 10.1016/0005-2736(76)90397-7. [DOI] [PubMed] [Google Scholar]
  17. Miles L. E., Hales C. N. The preparation and properties of purified 125-I-labelled antibodies to insulin. Biochem J. 1968 Jul;108(4):611–618. doi: 10.1042/bj1080611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PENNINGTON R. J. Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase. Biochem J. 1961 Sep;80:649–654. doi: 10.1042/bj0800649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pfeuffer T. GTP-binding proteins in membranes and the control of adenylate cyclase activity. J Biol Chem. 1977 Oct 25;252(20):7224–7234. [PubMed] [Google Scholar]
  20. Quirk S. J., Robinson G. B. Isolation and characterization of rabbit kidney brush borders. Biochem J. 1972 Aug;128(5):1319–1328. doi: 10.1042/bj1281319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rick W., Fritsch W. P., Szasz G. Fortschritte der klinischen Enzymologie. Dtsch Med Wochenschr. 1972 Nov 24;97(47):1828–1834. doi: 10.1055/s-0028-1107659. [DOI] [PubMed] [Google Scholar]
  22. Rothstein T. L., Blum J. J. Lysosomal physiology in Tetrahymena. I. Effect of glucose, acetate, pyruvate, and carmine on intracellular content and extracellular release of three acid hydrolases. J Cell Biol. 1973 Jun;57(3):630–641. doi: 10.1083/jcb.57.3.630. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Schmitz J., Preiser H., Maestracci D., Ghosh B. K., Cerda J. J., Crane R. K. Purification of the human intestinal brush border membrane. Biochim Biophys Acta. 1973 Sep 27;323(1):98–112. doi: 10.1016/0005-2736(73)90434-3. [DOI] [PubMed] [Google Scholar]
  24. Silverman R., Yalow R. S. Heterogeneity of parathyroid hormone. Clinical and physiologic implications. J Clin Invest. 1973 Aug;52(8):1958–1971. doi: 10.1172/JCI107380. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sutcliffe H. S., Martin T. J., Eisman J. A., Pilczyk R. Binding of parathyroid hormone to bovine kidney-cortex plasma membranes. Biochem J. 1973 Aug;134(4):913–921. doi: 10.1042/bj1340913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wilfong R. F., Neville D. M., Jr The isolation of a brush border membrane fraction from rat kidney. J Biol Chem. 1970 Nov 25;245(22):6106–6112. [PubMed] [Google Scholar]
  27. Zull J. E., Malbon C. C., Chuang J. Binding of tritiated bovine parathyroid hormone to plasma membranes from bovine kidney cortex. J Biol Chem. 1977 Feb 10;252(3):1071–1078. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES