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Journal of Histochemistry and Cytochemistry, Vol. 51, 1083-1095, August 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Biochemical Characterization and Immunocytochemical Localization of EM66, a Novel Peptide Derived from Secretogranin II, in the Rat Pituitary and Adrenal Glands

Maité Montero–Hadjadjea, Georges Pelletierb, Laurent Yona, Songyun Lib, Johann Guillemota, Rabia Magoulc, Yves Tilletd, Hubert Vaudrya, and Youssef Anouara
a European Institute for Peptide Research (IFRMP 23), Laboratory of Cellular and Molecular Neuroendocrinology, INSERM U413, UA CNRS, University of Rouen, Mont-Saint-Aignan, France
b Laboratory of Molecular Endocrinology, Laval University Medical Center, Quebec, Canada
c Laboratory of Animal Physiology, University Sidi Mohamed Ben Abdellah, Fes-Atlas, Morocco
d Laboratory of Neuroendocrinology, INRA-CNRS, Nouzilly, France

Correspondence to: Hubert Vaudry, European Institute for Peptide Research (IFRMP23), Lab. of Cellular and Molecular Neuroendocrinology, INSERM U413, UA CNRS, University of Rouen, 76821 Mont-Saint-Aignan, France. E-mail: hubert.vaudry@univ-rouen.fr

Characterization of secretogranin II (SgII) mRNA in various vertebrates has revealed selective conservation of the amino acid sequences of two regions of the protein, i.e., the bioactive peptide secretoneurin and a flanking novel peptide that we named EM66. To help elucidate the possible role of EM66, we examined the occurrence as well as the cellular and subcellular distribution of EM66 in rat pituitary and adrenal glands by using a polyclonal antibody raised against the recombinant human EM66 peptide. High-performance liquid chromatography (HPLC) analysis of rat pituitary and adrenal extracts combined with a radioimmunoassay resolved EM66-immunoreactive material exhibiting the same retention time as recombinant EM66. In the rat pituitary, double-labeling immunohistochemical (IHC) studies showed that EM66 immunoreactivity (IR) was present in gonadotrophs, lactotrophs, thyrotrophs, and melanotrophs, whereas corticotrophs were devoid of labeling. EM66-IR was also observed in nerve endings in the neural lobe. Immunocytochemical staining at the electron microscopic level revealed that EM66-IR is sequestered in the secretory granules within gonadotrophs and lactotrophs. In the adrenal medulla, double IHC labeling showed that EM66-IR occurs exclusively in epinephrine-synthesizing cells. At the ultrastructural level, EM66-IR was seen in chromaffin vesicles of adrenomedullary cells. These results demonstrate that post-translational processing of SgII generates a novel peptide that exhibits a cell-specific distribution in the rat pituitary and adrenal glands where it is stored in secretory granules, supporting the notion that EM66 may play a role in the endocrine system. (J Histochem Cytochem 51:1083–1095, 2003)

Key Words: secretogranin II, chromogranins, novel peptides, EM66, pituitary cells, adrenal medulla, immunohistochemistry, electron microscopy, HPLC analysis


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