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. 1966 Jan 1;49(3):501–516. doi: 10.1085/jgp.49.3.501

The Surface Charge of Isolated Toad Bladder Epithelial Cells

Mobility, effect of pH and divalent ions

Kenneth M Lipman 1, Robert Dodelson 1, Richard M Hays 1
PMCID: PMC2195488  PMID: 5938824

Abstract

The surface charge of epithelial cells isolated from the toad bladder has been determined by the microscope method of cell electrophoresis. The cells possess a net negative charge, and a net surface charge density of 3.6 x 104 electronic charges per square micron at pH 7.3. Estimates of net surface charge over the alkaline pH range indicate (a) that an average distance of the order of 40 A separates the negatively charged groups, and (b) that amino as well as acid groups are present at the electrophoretic surface of shear. A significant increase in mobility following cyanate treatment of the cells suggests that a large proportion of the amino groups are the ε-amino groups of lysine. In view of the known effects of calcium and other divalent ions on cell permeability and cell adhesion, the extent of binding of calcium and magnesium to the cell surface was determined by the electrophoretic technique. Mobility was significantly decreased in the presence of calcium or magnesium, indicating that these ions are bound by surface groups. When the pH was lowered from 7.3 to 5.2, calcium binding was markedly decreased, an observation consistent with competition between calcium and hydrogen ions for a common receptor site.

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Selected References

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  1. CHOI J. K. The fine structure of the urinary bladder of the toad, Bufo marinus. J Cell Biol. 1963 Jan;16:53–72. doi: 10.1083/jcb.16.1.53. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. COOK G. M., HEARD D. H., SEAMAN G. V. The electrokinetic characterization of the Ehrlich ascites carcinoma cell. Exp Cell Res. 1962 Oct;28:27–39. doi: 10.1016/0014-4827(62)90309-9. [DOI] [PubMed] [Google Scholar]
  3. EYLAR E. H., MADOFF M. A., BRODY O. V., ONCLEY J. L. The contribution of sialic acid to the surface charge of the erythrocyte. J Biol Chem. 1962 Jun;237:1992–2000. [PubMed] [Google Scholar]
  4. FARQUHAR M. G., PALADE G. E. Junctional complexes in various epithelia. J Cell Biol. 1963 May;17:375–412. doi: 10.1083/jcb.17.2.375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. HAYS R. M., LEAF A. Studies on the movement of water through the isolated toad bladder and its modification by vasopressin. J Gen Physiol. 1962 May;45:905–919. doi: 10.1085/jgp.45.5.905. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HEARD D. H., SEAMAN G. V. The action of lower aldehydes on the human erythrocyte. Biochim Biophys Acta. 1961 Oct 28;53:366–374. doi: 10.1016/0006-3002(61)90448-6. [DOI] [PubMed] [Google Scholar]
  7. HERRERA F. C., CURRAN P. F. The effect of Ca and antidiuretic hormone on Na transport across frog skin. I. Examination of interrelationships between Ca and hormone. J Gen Physiol. 1963 May;46:999–1010. doi: 10.1085/jgp.46.5.999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hays R. M., Singer B., Malamed S. The effect of calcium withdrawal on the structure and function of the toad bladder. J Cell Biol. 1965 Jun;25(3 Suppl):195–208. doi: 10.1083/jcb.25.3.195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Irons L. I., Perkins D. J. Studies on the interaction of magnesium, calcium and strontium ions with native and chemically modified human serum albumin. Biochem J. 1962 Jul;84(1):152–156. doi: 10.1042/bj0840152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. JAMES A. M., AMBROSE E. J., LOWICK J. H. Differences between the electrical charge carried by normal and homologous tumour cells. Nature. 1956 Mar 24;177(4508):576–577. doi: 10.1038/177576a0. [DOI] [PubMed] [Google Scholar]
  11. KATCHALSKY A., DANON D., NEVO A. Interactions of basic polyelectrolytes with the red blood cell. II. Agglutination of red blood cells by polymeric bases. Biochim Biophys Acta. 1959 May;33(1):120–138. doi: 10.1016/0006-3002(59)90505-0. [DOI] [PubMed] [Google Scholar]
  12. LEAF A. Measurement of the permeability of the two surfaces of a living membrane. Science. 1958 Jul 18;128(3316):144–145. doi: 10.1126/science.128.3316.144. [DOI] [PubMed] [Google Scholar]
  13. MILDVAN A. S., COHN M. MAGNETIC RESONANCE STUDIES OF THE INTERACTION OF THE MANGANOUS ION WITH BOVINE SERUM ALBUMIN. Biochemistry. 1963 Sep-Oct;2:910–919. doi: 10.1021/bi00905a003. [DOI] [PubMed] [Google Scholar]
  14. MOHAMMAD A., OLCOTT H. S., FRAENKEL-CONRAT H. The reaction of proteins with acetaldehyde. Arch Biochem. 1949 Dec;24(2):270–280. [PubMed] [Google Scholar]
  15. MORRILL G. A., KABACK H. R., ROBBINS E. EFFECT OF CALCIUM ON INTRACELLULAR SODIUM AND POTASSIUM CONCENTRATIONS IN PLANT AND ANIMAL CELLS. Nature. 1964 Nov 14;204:641–642. doi: 10.1038/204641a0. [DOI] [PubMed] [Google Scholar]
  16. PEACHEY L. D., RASMUSSEN H. Structure of the toad's urinary bladder as related to its physiology. J Biophys Biochem Cytol. 1961 Aug;10:529–553. doi: 10.1083/jcb.10.4.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. VASSAR P. S. THE ELECTRIC CHARGE DENSITY OF HUMAN TUMOR CELL SURFACES. Lab Invest. 1963 Nov;12:1072–1077. [PubMed] [Google Scholar]
  18. WATANABE I., UI N., NAKAMURA M. The temperature dependence of the electrophoretic mobility of horse serum albumin. J Phys Colloid Chem. 1950 Dec;54(9):1366–1370. doi: 10.1021/j150483a012. [DOI] [PubMed] [Google Scholar]

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