Regulation and expression of type V (tartrate-resistant) acid phosphatase in human mononuclear phagocytes

Mol Biol Med. 1991 Feb;8(1):135-40.

Abstract

Human type V (tartrate-resistant) acid phosphatase belongs to a unique group of iron-binding proteins that includes uteroferrin and other purple phosphatases. The enzyme is normally restricted to osteoclasts and certain phagocytic cells but its rôle is unknown. We show that phosphatase mRNA is abundant in cells of monohistiocytic phenotype and that enzyme expression in cultured human monocyte-derived macrophages is depressed by gamma-interferon and bacterial lipopolysaccharide, agents that promote functional differentiation in these cells. In contrast, phorbol ester, which stimulates intracellular calcium-mediated events, greatly enhances type V phosphatase expression and mRNA abundance. Lymphokine and phorbol ester-modulated expression of type V acid phosphatase expression thus represents a model system for investigating proliferative responses that are specific to cells of the mononuclear macrophage system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase / genetics*
  • Acid Phosphatase / metabolism*
  • Cell Differentiation / drug effects
  • Cells, Cultured
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Interferon-gamma / pharmacology
  • Lipopolysaccharides
  • Macrophages / drug effects
  • Macrophages / enzymology
  • Monocytes / drug effects
  • Monocytes / enzymology
  • Phagocytes / drug effects
  • Phagocytes / enzymology*
  • RNA, Messenger / genetics
  • Tartrates / pharmacology

Substances

  • Lipopolysaccharides
  • RNA, Messenger
  • Tartrates
  • Interferon-gamma
  • Acid Phosphatase
  • tartaric acid