Metalloproteases: carving out a role in axon guidance

Neuron. 2003 Feb 20;37(4):559-62. doi: 10.1016/s0896-6273(03)00089-8.

Abstract

Two families of metalloproteases, the matrix metalloproteases (MMPs) and the A Disintegrin and Metalloproteases (ADAMs), have recently been implicated in the formation of neural connections in the developing central nervous system. Invertebrate and vertebrate axons fail to extend and/or make pathfinding errors when metalloprotease function is inhibited or absent. Culture studies suggest that this requirement for metalloprotease activity results from their ability to cleave ligands, or their receptors, so as to activate or inhibit specific axon extension or guidance signaling pathways.

Publication types

  • Review

MeSH terms

  • Amyloid Precursor Protein Secretases
  • Animals
  • Aspartic Acid Endopeptidases
  • Axons / physiology*
  • Drosophila
  • Endopeptidases / metabolism
  • Growth Cones / physiology
  • Ligands
  • Matrix Metalloproteinases / metabolism
  • Metalloendopeptidases / antagonists & inhibitors
  • Metalloendopeptidases / metabolism*
  • Mice
  • Nerve Tissue Proteins
  • Receptors, Immunologic / metabolism
  • Roundabout Proteins
  • Signal Transduction / physiology
  • Superior Colliculi / cytology
  • Superior Colliculi / embryology
  • Visual Pathways / cytology
  • Visual Pathways / embryology

Substances

  • Ligands
  • Nerve Tissue Proteins
  • Receptors, Immunologic
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • Bace1 protein, mouse
  • Matrix Metalloproteinases
  • Metalloendopeptidases