The alpha2delta auxiliary subunit reduces affinity of omega-conotoxins for recombinant N-type (Cav2.2) calcium channels

J Biol Chem. 2004 Aug 13;279(33):34705-14. doi: 10.1074/jbc.M310848200. Epub 2004 May 27.

Abstract

The omega-conotoxins from fish-hunting cone snails are potent inhibitors of voltage-gated calcium channels. The omega-conotoxins MVIIA and CVID are selective N-type calcium channel inhibitors with potential in the treatment of chronic pain. The beta and alpha(2)delta-1 auxiliary subunits influence the expression and characteristics of the alpha(1B) subunit of N-type channels and are differentially regulated in disease states, including pain. In this study, we examined the influence of these auxiliary subunits on the ability of the omega-conotoxins GVIA, MVIIA, CVID and analogues to inhibit peripheral and central forms of the rat N-type channels. Although the beta3 subunit had little influence on the on- and off-rates of omega-conotoxins, coexpression of alpha(2)delta with alpha(1B) significantly reduced on-rates and equilibrium inhibition at both the central and peripheral isoforms of the N-type channels. The alpha(2)delta also enhanced the selectivity of MVIIA, but not CVID, for the central isoform. Similar but less pronounced trends were also observed for N-type channels expressed in human embryonic kidney cells. The influence of alpha(2)delta was not affected by oocyte deglycosylation. The extent of recovery from the omega-conotoxin block was least for GVIA, intermediate for MVIIA, and almost complete for CVID. Application of a hyperpolarizing holding potential (-120 mV) did not significantly enhance the extent of CVID recovery. Interestingly, [R10K]MVIIA and [O10K]GVIA had greater recovery from the block, whereas [K10R]CVID had reduced recovery from the block, indicating that position 10 had an important influence on the extent of omega-conotoxin reversibility. Recovery from CVID block was reduced in the presence of alpha(2)delta in human embryonic kidney cells and in oocytes expressing alpha(1B-b). These results may have implications for the antinociceptive properties of omega-conotoxins, given that the alpha(2)delta subunit is up-regulated in certain pain states.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium Channels / chemistry*
  • Calcium Channels, N-Type / chemistry*
  • Calcium Channels, N-Type / metabolism
  • Cell Line
  • Dose-Response Relationship, Drug
  • Electrophysiology
  • Exons
  • Humans
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Oocytes / metabolism
  • Pain
  • Peptides / chemistry
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • RNA, Complementary / metabolism
  • Rats
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Time Factors
  • Up-Regulation
  • Xenopus laevis
  • omega-Conotoxins / chemistry*
  • omega-Conotoxins / metabolism

Substances

  • Calcium Channels
  • Calcium Channels, N-Type
  • Peptides
  • RNA, Complementary
  • Recombinant Proteins
  • omega-Conotoxins

Associated data

  • PDB/1TR6
  • PDB/1TT3
  • PDB/1TTK
  • PDB/1TTL