Abstract
Molecular cloning of secretogranin II (SgII) in different species has revealed the existence of a highly conserved 66-amino acid peptide (EM66) flanked by preserved pairs of basic residues. In the present study we have localized and characterized EM66 in the human adrenal gland. A fusion protein containing the human EM66 peptide was produced in E. coli and used to raise polyclonal antibodies in rabbits. Immunohistochemical staining of human adrenal slices revealed intense labeling of adrenochromaffin cells in the adult and fetal gland. HPLC analysis of adrenal extracts showed the presence of an immunoreactive peak exhibiting the same retention time as recombinant. EM66 in both adult and fetus. These data demonstrate that post-translational processing of SgII actually generates a novel peptide in the human adrenal gland. The conservation of the sequence of EM66 in vertebrates and the occurrence of the mature peptide during early ontogenesis of the human adrenal gland strongly suggest that EM66 could exert physiological activities.
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