S-100 protein and annexin II2-p11(2) (calpactin I) act in concert to regulate the state of assembly of GFAP intermediate filaments

Biochem Biophys Res Commun. 1995 Mar 28;208(3):910-8. doi: 10.1006/bbrc.1995.1421.

Abstract

S-100 protein and annexin II2-p11(2) were reported to inhibit and to stimulate the assembly of glial fibrillary acidic protein (GFAP), respectively, in a Ca(2+)-dependent manner. Here we show by a number of experimental approaches that S-100 protein contrasts all the effects of annexin II2-p11(2) on GFAP assembly and, conversely, that annexin II2-p11(2) contrasts the inhibitory effects of S-100 protein on GFAP assembly, in a dose-dependent manner in both cases. Altogether, these data suggest that two specific Ca2+ effectors, i.e., annexin II2-p11(2) and S-100 protein, might regulate the state of assembly of glial filaments in a concerted manner.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Annexin A2 / pharmacology*
  • Calcium / pharmacology
  • Cattle
  • Glial Fibrillary Acidic Protein / drug effects
  • Glial Fibrillary Acidic Protein / metabolism*
  • Glial Fibrillary Acidic Protein / ultrastructure
  • Intermediate Filaments / drug effects
  • Intermediate Filaments / ultrastructure*
  • Kinetics
  • Microscopy, Electron
  • S100 Proteins / pharmacology*

Substances

  • Annexin A2
  • Glial Fibrillary Acidic Protein
  • S100 Proteins
  • Calcium

Grants and funding