Galanin message-associated peptide (GMAP), a 60 amino acid fragment of galanin precursor protein, is present in dorsal root ganglion cells and upon intrathecal (i.t.) administration influences the spinal nociceptive flexor reflex in rat in a complex manner. The present study assessed the effects on spinal cord excitability of N-terminal fragment GMAP (1-30) and C-terminal fragments GMAP (34-60) or GMAP (35-60), which were formed from GMAP following enzymatic degradation. The effect of the fragments was compared with the effects of the complete peptide sequence. The GMAP fragments slightly facilitated the flexor reflex and dose-dependently blocked hyperexcitability following C-fiber conditioning stimulation. The potency of the blocking effect of GMAP (1-30) was comparable to GMAP (1-60) and was one order of magnitude higher than the potency of the C-terminal fragments. The results indicated that both naturally formed N- and C-terminal fragments of GMAP are pharmacologically active and produce effects which are similar to the full peptide sequence.