Phospholipids involved in specific binding of 12-O-(5-azido-2-nitrobenzoyl)phorbol-13-acetate to epidermal microsomes, a photolabeling study

Cancer Lett. 1985 Feb;26(1):97-111. doi: 10.1016/0304-3835(85)90178-8.

Abstract

The preparation of 12-O-(5-azido-2-nitro)benzoylphorbol-13-acetate (NABPA) is described. It is used as a photoaffinity probe to study the biochemical components involved in the specific binding of phorbol esters to an epidermal particulate fraction (microsomes) from NMRI mice: without irradiation NABPA binds in a saturable and high affinity manner (KD = 12 nM; Rt = 2.6 pmol/mg protein) to microsomes; after irradiation (at 350 nm) specific photolabeling (representing specific binding of NABPA) is found of phospholipids (phosphatidyl-serine (PS) and -ethanolamine(PE)), but not of protein. The results are discussed in the context of protein kinase C being a receptor for phorbol esters.

MeSH terms

  • Affinity Labels
  • Animals
  • Azides / metabolism*
  • Carcinogens / metabolism*
  • Female
  • In Vitro Techniques
  • Mice
  • Mice, Inbred Strains
  • Microsomes / metabolism*
  • Phorbol Esters / metabolism*
  • Phorbols / metabolism*
  • Phospholipids / physiology*
  • Photolysis
  • Skin / metabolism*
  • Tritium

Substances

  • Affinity Labels
  • Azides
  • Carcinogens
  • Phorbol Esters
  • Phorbols
  • Phospholipids
  • Tritium
  • 12-O-(5-azido-2-nitrobenzoylphorbol)-13-acetate