ArticleCell and tissue research1991
Immunoreactivities for chromogranin A and B, and secretogranin II in the guinea pig entero-endocrine system: cellular distributions and intercellular heterogeneities.
Article in Cell and tissue research, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 41 citations in OpenAlex.
- Dual regulatory role for phosphatase and tensin homolog in specification of intestinal endocrine cell subtypes.World journal of gastroenterology · 2012Article
- Article
- Ontogeny, distribution and amine/peptide content of chromogranin A- and B-immunoreactive endocrine cells in the small and large intestine of the chicken.Anatomy and embryology · 1996Article
- Ontogeny, distribution and amine/peptide colocalization of chromogranin A- and B-immunoreactive cells in the chicken gizzard and antrum.Anatomy and embryology · 1995Article
- Plasma chromogranin A marks emesis and serotonin release associated with dacarbazine and nitrogen mustard but not with cyclophosphamide-based chemotherapies.British journal of cancer · 1995Article
- Analysis of the human guanylin gene and the processing and cellular localization of the peptide.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Immunohistochemical localization of chromogranin A and B in the endocrine cells of the alimentary tract of the green frog, Rana esculenta.Cell and tissue research · 1994Article
- Enterochromaffin cells of the digestive system: cellular source of guanylin, a guanylate cyclase-activating peptide.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Enterochromaffin-like cells in the rat stomach: effect of alpha-fluoromethylhistidine-evoked histamine depletion. A chemical, histochemical and electron-microscopic study.Cell and tissue research · 1992Article
- The chromogranins A and B: the first 25 years and future perspectives.Neuroscience · 1992Review
- Mutual relationships between chromogranins A and B and gastrin in individual gastrin cells.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Chromogranin A immunoreactivity and Grimelius' argyrophilia. A correlative study in mammalian endocrine cells.Anatomy and embryology · 1992Article
- Topology of chromogranins in secretory granules of endocrine cells.Histochemistry · 1991Article
- The biology and physiology of the ECL cell.The Yale journal of biology and medicineReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family of the chromogranin/secretogranin proteins consists of three major subtypes: chromogranin A (CgA), chromogranin B (CgB) and secretogranin II (SgII). These proteins are present in various endocrine cells and organs. Using immunohistochemistry on serial semithin sections, we have investigated ten endocrine cell types of the guinea pig gastro-intestinal tract for their content of chromogranin/secretogranin proteins. The gastrin cell was the only cell type containing immunoreactivities for all three chromogranin subtypes. The majority of entero-endocrine cells showed immunoreactivities for CgA and SgII. Somatostatin cells lacked immunoreactivities for any of the chromogranins. Moreover, the densities of the corresponding immunoreactivities varied among the different endocrine cell types or even among endocrine cells of a given population. Aminergic endocrine cells (e.g., enterochromaffin and enterochromaffin-like cells) regularly exhibited strong immunoreactivities for CgA but failed to react for SgII. In peptidergic endocrine cells, the immunoreactivities for both CgA and SgII ranged from dense to faint. This was also true for CgB in gastrin cells. Hence, only CgA and SgII can be considered as regular constituents of entero-endocrine cells. The intercellular differences in immunoreactivities for all three chromogranin subtypes indicate that every endocrine cell has its own composition of chromogranin/secretogranin proteins. This may be due to differences in the regulation of biosynthesis or processing of the chromogranins in individual endocrine cells; this in turn might be related to the functional states of endocrine cells.
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