Properties of chicken lens MIP channels reconstituted into planar lipid bilayers

J Membr Biol. 1996 Dec;154(3):239-49. doi: 10.1007/s002329900148.


Membrane fractions highly enriched in chicken lens MIP (MIP28) were found to form ion channels when incorporated into planar lipid bilayers. The channels displayed prominent unitary conductances of about 60 and 290 pS in symmetric 150 mm KCl solution and were slightly anion selective. For both depolarizing and hyperpolarizing voltages, voltage sensitivity of the MIP28-induced conductance could be fit by a Boltzmann relation, symmetric around zero mV, with V0 = 18.5 mV, n = 4.5 and gmin/gmax = 0.17. Channel properties were not appreciably altered by pH in the range of 5.8 to 7, although channel incorporation was observed to occur more frequently at lower pH values. Calcium, at millimolar concentrations, decreased the channel mean open time. Partial proteolysis of MIP28 to yield MIP21 did not appreciably affect single-channel conductance or voltage sensitivity of the reconstituted channels. MIP28 was not phosphorylated by cAMP dependent protein kinase (PKA). Although unitary conductance and selectivity of the chicken MIP channel are similar to those reported for the bovine MIP (MIP26), the voltage sensitivity of MIP28 was higher than that of the bovine homologue, and voltage sensitivity of MIP28 was not modulated by treatments previously shown to affect MIP26 voltage gating (partial proteolysis and protein phosphorylation by PKA: (Ehring et al., 1990). The existence of such strikingly different functional properties in highly homologous channel isoforms may provide a useful system for exploration of the structure-function relations of MIP channels.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Aquaporins
  • Calcium / pharmacology
  • Cattle
  • Chickens
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Eye Proteins / metabolism*
  • Eye Proteins / physiology
  • Hydrogen-Ion Concentration
  • Ion Channel Gating / physiology*
  • Ion Channels / metabolism*
  • Lens, Crystalline / chemistry*
  • Lipid Bilayers*
  • Membrane Glycoproteins*
  • Membrane Potentials
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Structure-Activity Relationship
  • Trypsin / metabolism


  • Aquaporins
  • Eye Proteins
  • Ion Channels
  • Lipid Bilayers
  • Membrane Glycoproteins
  • aquaporin 0
  • lens intrinsic protein MIP 28
  • Cyclic AMP-Dependent Protein Kinases
  • Trypsin
  • Calcium