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In the industrialized world, polyneuropathy induced by diabetes mellitus (DM) is one of the most prevalent forms of neuropathy. Diabetic neuropathy can result from a direct toxic effect of glucose on nerve cells. Additionally, the damage of the nerve structures (central and peripheral) is accompanied by a microvascular dysfunction, which damages the vasa nervorum. More than 80% of the patients with DM-induced polyneuropathy have a distal and symmetric presentation. The initial symptoms are: signs of diminished sensation, burning feet, which may occur particularly during the night and worsen when touched, and tingling sensation in the feet. Attacks of shooting pain may also occur. Proper control of DM is mandatory. Based on the recently published National Institute for Health and Clinical Excellence guidelines, treatment of painful diabetic neuropathy should start with duloxetine or amitriptyline if duloxetine is contraindicated. If pain relief is inadequate, monotherapy with amitriptyline or pregabalin, or combination therapy with amitriptyline and pregabalin should be considered. If pain relief is still insufficient, tramadol instead of or in combination with a second-line agent should be considered. In patients who are unable to take oral medication, topical lidocaine can be considered for localized pain. There are currently four studies showing that spinal cord stimulation can potentially provide pain alleviation for the longer term in patients with painful diabetic polyneuropathy. Complications are mainly implant related, though infections also occur. The available evidence (2 C+) justifies spinal cord stimulation to be considered, preferably study related.

The ribosomal protein L7/L12 functions in the GTP-dependent reactions of protein synthesis [ 1,2] . A comparison of its primary structure, both in procaryotic and eucaryotic organisms, would be of great interest, not only for localizing active sites involved in protein biosynthesis, but also for tracing evolutionary changes of the protein moiety of the ribosome. Up to now, only the complete primary structure of Escherichia coli L7/L12 protein has been published [3]. Visentin et al. [4] performed sequence studies of the amino-terminal region of the Bacillus stearothermophilus protein, and they found that the first 15 residues are highly homologous with residues 2-16 of the E. coli protein. Oda et al. [S] published partial sequences of an acidic protein, L20, of Halobacterium cutirubrum which appears to be homologous to L7/L12. The amino-terminal region of this protein shows a substantial degree of homology with the region, starting at residue 35 of the E. coli protein. The presence of acidic proteins in 60 S ribosomes of the brine shrimp Artemia salina was previously reported by Moller et al. [6]. These proteins were shown to function in the GTP-dependent reactions in ribosomes [6,7] . We therefore assume that these proteins are equivalent to bacterial L7/L12 and we hereafter call them L7/L12-type proteins. The present communication is concerned with the comparison of the aminoterminal region of the L7/L12-type proteins from Artemia salina and the yeast Saccharomyces cerevisiae. The results indicate a remarkable conservation of this region and a clear relationship to the aminoterminal part of the protein from the halophile.