Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda

Hum Mol Genet. 2003 Nov 15;12(22):3017-24. doi: 10.1093/hmg/ddg320. Epub 2003 Sep 23.

Abstract

Mal de Meleda is an autosomal recessive inflammatory and keratotic palmoplantar skin disorder due to mutations in the ARS B gene, encoding for SLURP-1 (secreted mammalian Ly-6/uPAR-related protein 1). SLURP-1 belongs to the Ly-6/uPAR superfamily of receptor and secreted proteins, which participate in signal transduction, immune cell activation or cellular adhesion. The high degree of structural similarity between SLURP-1 and the three fingers motif of snake neurotoxins and Lynx1 suggests that this protein interacts with the neuronal acetylcholine receptors. We found that SLURP-1 potentiates the human alpha 7 nicotinic acetylcholine receptors that are present in keratinocytes. These results identify SLURP-1 as a secreted epidermal neuromodulator which is likely to be essential for both epidermal homeostasis and inhibition of TNF-alpha release by macrophages during wound healing. This explains both the hyperproliferative as well as the inflammatory clinical phenotype of Mal de Meleda.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / metabolism
  • Amino Acid Sequence
  • Animals
  • Antigens, Ly / chemistry
  • Antigens, Ly / genetics*
  • Antigens, Ly / isolation & purification
  • Antigens, Ly / pharmacology
  • Cell Line
  • Cell Nucleus / metabolism
  • Clone Cells
  • DNA, Complementary / administration & dosage
  • DNA, Complementary / metabolism
  • Dose-Response Relationship, Drug
  • Epidermis / metabolism*
  • Female
  • Genes, Recessive
  • Humans
  • Keratoderma, Palmoplantar / genetics*
  • Keratoderma, Palmoplantar / metabolism
  • Keratoderma, Palmoplantar / pathology
  • Microinjections
  • Models, Molecular
  • Moths / cytology
  • Mutation
  • Neurotransmitter Agents / metabolism*
  • Oocytes / metabolism
  • Patch-Clamp Techniques
  • Peptides / chemistry
  • Peptides / genetics
  • Peptides / metabolism
  • Phenotype
  • Protein Structure, Tertiary
  • Receptors, Cholinergic / drug effects
  • Receptors, Cholinergic / metabolism
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Urokinase-Type Plasminogen Activator / chemistry
  • Urokinase-Type Plasminogen Activator / genetics*
  • Urokinase-Type Plasminogen Activator / isolation & purification
  • Urokinase-Type Plasminogen Activator / pharmacology
  • Xenopus laevis / physiology

Substances

  • Antigens, Ly
  • DNA, Complementary
  • Neurotransmitter Agents
  • Peptides
  • Receptors, Cholinergic
  • Recombinant Proteins
  • SLURP1 protein, human
  • Urokinase-Type Plasminogen Activator
  • Acetylcholine