Ecto-ATPases: identities and functions

Int Rev Cytol. 1995;158:141-214. doi: 10.1016/s0074-7696(08)62487-0.

Abstract

Ecto-ATPases are ubiquitous in eukaryotic cells. They hydrolyze extracellular nucleoside tri- and/or diphosphates, and, when isolated, they exhibit E-type ATPase activity, (that is, the activity is dependent on Ca2+ or Mg2+, and it is insensitive to specific inhibitors of P-type, F-type, and V-type ATPases; in addition, several nucleotide tri- and/or diphosphates are hydrolysed, but nucleoside monophosphates and nonnucleoside phosphates are not substrates). Ecto-ATPases are glycoproteins; they do not form a phosphorylated intermediate during the catalytic cycle; they seem to have an extremely high turnover number; and they present specific experimental problems during solubilization and purification. The T-tubule Mg2+-ATPase belongs to this group of enzymes, which may serve at least two major roles: they terminate ATP/ADP-induced signal transduction and participate in adenosine recycling. Several other functions have been discussed and identity to certain cell adhesion molecules and the bile acid transport protein was suggested on the basis of cDNA clone isolation and immunological work.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphatases* / antagonists & inhibitors
  • Adenosine Triphosphatases* / chemistry
  • Adenosine Triphosphatases* / metabolism
  • Animals
  • Cell Membrane / enzymology
  • Detergents / pharmacology
  • Extracellular Space / enzymology
  • Glycoproteins / chemistry
  • Humans
  • Solubility
  • Substrate Specificity
  • Tissue Distribution

Substances

  • Detergents
  • Glycoproteins
  • Adenosine Triphosphatases