Is the sigma2 receptor a histone binding protein?

Abstract

Starting from the high affinity sigma(2) receptor ligand 2, (PB28), we synthesized amino derivative 4 and coupled it to an NHS-ester activated sepharose stationary phase column to elute a crude protein prepared by lysed human SK-N-SH neuroblastoma cells. We characterized the SDS-PAGE gel electrophoresis stained bands by MALDI-MS and LC-MS-MS analysis. The MASCOT MS-MS ion search program led to the identification of the protein components. The six eluted proteins had a molecular weight ranging from 13 kDa to 26 kDa and were human histone proteins. A human 40S ribosomal protein S3 (SwissProt accession number: P23396) was also identified as a comigrated band. The human histone proteins that were characterized were H3.3A histone (NCBI accession number: 51859376), H2B histone (NCBI accession number: 1568557), H2A.5 histone (NCBI accession number: 70686), H1 (NCBI accession number: 22770677), and H2.1 histone (SwissProt accession number: P16403). These results disclosed a dual hypothesis about the sigma(2) receptor, that is, that it is formed by histones or that the sigma(2) ligands also bind histone proteins.