Isolation and Characterization of 5′-Nucleotidase from Avian Muscle Sources and its Interaction with Filamentous Actin

  • J. Dieckhoff
  • M. Heidemann
  • R. Lietzke
  • H. G. Mannherz
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

5′-Nucleotidase has been known for a long time to be an ectoenzyme concentrated in the plasma membrane of many eukaryotic cells. DePierre and Karnovsky (1974) first demonstrated its nature as an ectoenzyme and since then a vast amount of literature has been compiled concerning its enzymatic properties and presumed functional significance. In spite of efforts in many laboratories it has been impossible to assign a definitive function to this enzyme. It has been found, however, that adenosine, the product formed by its enzymatic action on 5′-AMP, can act as a local modulator of cellular functions in a number of different tissues, such as the vascular and central nervous systems (for a review see Arch and Newsholme 1978).

Keywords

Adenosine Polypeptide Polyacrylamide Catalase Hepes 

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References

  1. Arch JRS, Newsholme EA (1978) The control of the metabolism and the hormonal role of adenosine. Essays Biochem 14: 82 - 123PubMedGoogle Scholar
  2. Burger RM, Lowenstein JM (1970) Preparation and properties of 5′-nucleotidase from smooth muscle of small intestine. J Biol Chem 245: 6274 - 6279PubMedGoogle Scholar
  3. Carraway KL, Carraway CA (1975) Cooperative effects in the perturbation of membrane enzymes by concanavalin A. Biochem Biophys Res Commun 67: 1301 - 1306PubMedCrossRefGoogle Scholar
  4. Carraway KL, Doss RC, Huggins JW, Chesnut RW, Carraway CAC (1979) Effect of cytoskeletal perturbant drugs on ecto-5′-nucleotidase, a concanavalin A receptor. J Cell Biol 83: 529 - 543PubMedCrossRefGoogle Scholar
  5. De Pierre JW, Karnovsky ML (1974) Ecto-enzymes of granulocytes: 5′-nucleotidase. Science (Wash DC) 183: 1096 - 1098CrossRefGoogle Scholar
  6. Dieckhoff J, Heidemann M, Mannherz HG (1984) The isolation of 5′-nucleotidase from avian sources and its interaction with polymeric actin. J Submicrosc Cytol 16: 33 - 34Google Scholar
  7. Dornand J, Bonnafous JC, Mani JC (1978) Purification and properties of 5′-nucleotidase from lymphocyte plasma membranes. Eur J Biochem 87: 459 - 465PubMedCrossRefGoogle Scholar
  8. Drenckhahn D, Mannherz HG (1983) Distribution of actin and the actin-associated proteins myosin, tropomyosin, alpha-actinin, vinculin, and villin in rat and bovine exocrine glands. Eur J Cell Biol 30: 167 - 176PubMedGoogle Scholar
  9. Eadie CS (1942) The inhibition of cholesterase by physostigmine and prostigmine. J Biol Chem 146: 85 - 93Google Scholar
  10. Gunther GR, Wong JL, Yakara I, Cunningham BA, Edelman GM (1973) Concanavalin A deri-vatives with altered biological activities. Proc Natl Acad Sci USA 70: 1012 - 1016PubMedCrossRefGoogle Scholar
  11. Jarrett L, Smith RM (1974) The stimulation of adipocyte plasma membrane magnesium ion- stimulated adenosine triphosphatase by insulin and concanavalin A. J Biol Chem 249: 5195 - 5199Google Scholar
  12. Hawkes R (1982) Identification of concanavalin A binding proteins after sodium dodecylsulfate-gelelectrophoresis and transblotting. Anal Biochem 123: 143 - 146PubMedCrossRefGoogle Scholar
  13. Hoffstee BHJ (1952) Specificity of esterases I. Identification of two pancreatic aliesterases. B Biol Chem 199: 357 - 364Google Scholar
  14. Lengsfeld AM, Low I, Wieland T, Danker P, Hasselbach W(1974) Interaction of phalloidin with actin. Proc Natl. Acad Sci USA 71: 2803 - 2807Google Scholar
  15. Mannherz HG, Goody RS (1976) Proteins of contractile systems. Annu Rev Biochem 45: 427 - 465PubMedCrossRefGoogle Scholar
  16. Mannherz HG, Magener M (1979) Concanavalin A inhibits the interaction of snake venom 5′-nucleotidase and actin. FEBS Lett 103: 77 - 80PubMedCrossRefGoogle Scholar
  17. Mannherz HG, Rohr G (1978) 5′-Nucleotidase reverses the inhibitory action of actin on pancreatic deoxyribnuclease I. FEBS Lett 95: 284 - 289Google Scholar
  18. Riordan JR, Slavik M (1974) Interactions of lectins with membrane glycoproteins. Effects of concanavalin A on 5′-nucleotidase. Biochim Biophys Acta 373: 356 - 360PubMedCrossRefGoogle Scholar
  19. Rohr G, Mannherz HG (1979) The activation of actin-DNAse I complex with rat liver plasma membranes, the possible role of 5′-nucleotidase. FEBS Lett 99: 351 - 356PubMedCrossRefGoogle Scholar
  20. Slavik M, Kartner N, Riordan JR (1977) Lectin-induced inhibition of plasma membrane 5′-nucleotidase. Sensitivity of purified enzyme. Biochem Biophys Res Commun 75: 342 - 349PubMedCrossRefGoogle Scholar
  21. Towbin H, Staehlin T, Fordin J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350 - 4354PubMedCrossRefGoogle Scholar
  22. Zachowski A, Evans HW, Paraf A (1981) Immunological evidence that plasma-membrane 5′- nucleotidase is a transmembrane protein. Biochim Biophys Acta 664: 121 - 126Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • J. Dieckhoff
  • M. Heidemann
  • R. Lietzke
  • H. G. Mannherz
    • 1
  1. 1.Institut für Anatomie und ZellbiologieMarburgGermany

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