Ultrastructural localization of lectin binding sites in human melanocytes

Arch Dermatol Res. 1990;282(8):520-5. doi: 10.1007/BF00371947.

Abstract

The ultrastructural localization of carbohydrate residues in human melanocytes of normal epidermis and of one compound naevus was studied. The following lectins were used in a post-embedding technique: 1. peanut agglutinin (PNA), which reacts specifically with N-acetylgalactosamine; 2. Concanavalia ensiformis (Con A) indicating alpha-D-glucose and alpha-D-mannose binding sites; 3. Ulex europaeus agglutinin (UEA I) specific for alpha-L-fucose; 4. Wheat germ agglutinin (WGA), reacting specifically with N-acetyl-glucosamine and neuraminic acid (sialic acid); and 5. Limax flavus agglutinin (LFA), also specific for sialic acid (Neu5Ac-alpha-2,3-Gal and Neu5Ac-alpha-2,6-Gal). When incubated with WGA, Con A and LFA strong labelling was seen within the cytoplasm and in the plasma membrane of melanocytes, whereas incubations with PNA and UEA I revealed an occasional gold particle only. The determination of the distribution of carbohydrate residues in normal melanocytes is a prerequisite for future studies of abnormal melanocytes.

MeSH terms

  • Arachis
  • Concanavalin A / metabolism
  • Humans
  • Lectins / metabolism
  • Melanocytes / chemistry*
  • Melanocytes / ultrastructure
  • Microscopy, Immunoelectron
  • Nevus, Pigmented / chemistry*
  • Peanut Agglutinin
  • Plant Lectins
  • Receptors, Mitogen / analysis*
  • Reference Values
  • Wheat Germ Agglutinins / metabolism

Substances

  • Lectins
  • Limax flavus agglutinin
  • Peanut Agglutinin
  • Plant Lectins
  • Receptors, Mitogen
  • Ulex europaeus lectins
  • Wheat Germ Agglutinins
  • Concanavalin A