S-100 protein and annexin II2-p11(2) (calpactin I) act in concert to regulate the state of assembly of GFAP intermediate filaments.
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.
Bianchi
R
R
Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
Garbuglia
M
M
Verzini
M
M
Giambanco
I
I
Spreca
A
A
Donato
R
R
D000818:Animals; D017306:Annexin A2 / Q000494:pharmacology*; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D005904:Glial Fibrillary Acidic Protein / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D007382:Intermediate Filaments / Q000187:drug effects / Q000648:ultrastructure*; D007700:Kinetics; D008854:Microscopy, Electron; D009418:S100 Proteins / Q000494:pharmacology*
D017306:Annexin A2; D005904:Glial Fibrillary Acidic Protein; D009418:S100 Proteins; D002118:Calcium