Mutual relationships between chromogranins A and B and gastrin in individual gastrin cells.

Cetin, Yalcin; Bargsten, Gerhard; Grube, D.

doi:10.1073/pnas.89.7.2912

Cited by 21 publications

(20 citation statements)

References 46 publications

(53 reference statements)

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“…The latter glycoprotein has not been reported earlier in this cell type in humans, but was found in guinea pig (Cetin and Grube 1991;Cetin et al 1992). It is less probable that these CgC-IR gastrin cells correspond to the cell population expressing both gastrin and serotonin; the former were more numerous.…”

Section: Discussionmentioning

confidence: 60%

Complex Co-localization of Chromogranins and Neurohormones in the Human Gastrointestinal Tract

Portela-Gomes

Stridsberg

Johansson

et al. 1997

J Histochem Cytochem.

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SUMMARY Co-localization of chromogranin (Cg) A, B, and C has been studied in different neuroendocrine cell types in histologically normal mucosa from human gastrointestinal tract (corpus, antrum, duodenum, ileum, and colon) using single-, double-, and triple-immunofluorescence stainings. Virtually all enterochromaffin (EC) cells contained CgA, and those in the luminal two thirds of the antral mucosa and villi of small intestine often also contained CgB. A few EC cells in the duodenal crypts contained CgC. Most gastrin cells harbored both CgB and CgA, although rather more CgB than CgA, but some gastrin cells contained all three types, i.e., also CgC. Some CCK cells also contained all three chromogranins. Enteroglucagon cells in the duodenal villi contained CgA and some CgB. CgA (but not B or C) was found in some secretin, GIP, enteroglucagon/peptide YY, and neurotensin cells. A few somatostatin cells contained CgA but neither CgB nor CgC. CgA and C were found mainly in the basal cell region, whereas CgB occurred more diffusely throughout the cytoplasm. This varying distribution suggests that not all secretory granules contain CgA, or that CgB may occur in a nongranular form. The varying composition of the different chromogranins may reflect their complex functional roles in the widespread neuroendocrine system. (J Histochem Cytochem 45:815-822, 1997)

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Section: Discussionmentioning

confidence: 60%

Complex Co-localization of Chromogranins and Neurohormones in the Human Gastrointestinal Tract

Portela-Gomes

Stridsberg

Johansson

et al. 1997

J Histochem Cytochem.

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“…Serial semithin sections were cut at 0.5 Am and mounted individually on microscope slides. Since 20-40 sections pass through the same cells (22), identical cells could be immunostained by different antisera; moreover, the antibody specificities could be checked in identical endocrine cells (see below). Immunohistochemistry.…”

Section: Methodsmentioning

confidence: 99%

“…After removal ofthe epoxy resin by sodium methoxide (22), serial semithin (0.5 pkm) sections were immunostained by the peroxidase-antiperoxidase (PAP) technique (25), which was modified and standardized for use on plastic sections (22). Serial sections were alternatively incubated with various antisera (see Table 1 30 min, (ii) CST antiserum at a dilution of 1:1000 for 24 h at 4°C, and (iii) gold-labeled goat anti-rabbit IgG (Peninsula Laboratories; size of gold particles, 10 nm) diluted 1:20 for 1 h. Between the various incubation steps, the grids were rinsed in Tris-HCl buffer (pH 7.6) for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Chromostatin, a chromogranin A-derived bioactive peptide, is present in human pancreatic insulin (beta) cells.

Cetin¹,

Aunis²,

Bader³

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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Chromogranin A (CGA) is a secretory protein present in the adrenal medulla and in a variety ofendocrine organs. This protein may serve as precursor for pancreastatin (PST) and for other biologically active peptides. Recently, chromostatin (CST), a CGA derivative, has been identified that possesses high biological activity. The cellular distribution of CST in various endocrine organs is completely unknown. Using immunohistochemistry on plastic sections, we investigated the occurrence and cellular distribution of CST, PST, and CGA in human endocrine pancreas of healthy and diseased states and in the adrenal medulla. In the normal and diabetic pancreas, CST immunoreactivity was localized exclusively in 13 cells, which were mostly unreactive for PST and CGA. Both latter peptides were confined mainly to glucagon (a) cells. Insulinoma cells displayed strong insulin, PST, and CGA immunoreactivities, but they were faintly immunoreactive for CST or unreactive. Adrenal chromaffm cells exhibited strong immunoreactivity for CGA but lacked CST and PST immunoreactivities. Based on the peculiar distributive pattern of CST, PST, and CGA, we suggest that CGA is differentially processed in chromaffin and islet tissues and in insulinoma cells. The unique cellular localization of CST in the endocrine pancreas ofnormal and pathological conditions may indicate that CST is involved in 13-cell function.Chromogranin A (CGA) is an acidic glycoprotein originally detected in the adrenal medulla but more recently found also in a variety of peptide hormone-producing cells (see refs. 1 and 2 for review). Despite its widespread distribution, the physiological function of CGA is still largely unknown.The primary amino acid sequence of CGA, elucidated by cDNA analysis, includes several pairs of basic residues, which by analogy with other peptide hormone precursors constitute potential sites of proteolytic cleavage (3-5). Thus, it was speculated that CGA may be a putative precursor of biologically active peptides (2, 6, 7). Pancreastatin (PST), a peptide fully contained in the porcine CGA sequence (3, 7), was isolated from the porcine pancreas (8). This peptide inhibits insulin secretion (8). Moreover, tryptic digestion of CGA yielded various peptides that were able to modulate catecholamine secretion (7). Recently, chromostatin (CST) has been identified as a CGA derivative, which is localized between amino acids 124 and 143 in the bovine CGA sequence (9). In contrast to PST, CST had potent inhibitory action on chromaffin cell secretion (9).Previous studies demonstrated that pancreatic islet cells and islet cell tumors contain various CGA-derived peptides (10)(11)(12)(13)(14)(15)(16)(17). In the human pancreas, CGA has been localized mainly to glucagon (a) cells (18). The cellular distribution of PST, however, is still a matter of controversy (see ref. 19 for review), which in part may be due to species specificities (20). Data on tissue distribution of CST are completely lacking.Using specific antisera against CST, PST, and CGA, we inves...

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“…After removal of paraffin by xylene and subsequent descending ethanol series, the sections were alternatively immunostained for guanylin (antiserum K42, diluted 1:1000; antiserum K605, diluted 1:1000), serotonin (diluted 1:20,000), and chromogranin A (diluted 1:8000) by the avidinbiotin-peroxidase complex (ABC) technique with incubation sequences as described (7). Specificity of immunostaining was verified by appropriate controls (7,16,17).…”

mentioning

confidence: 99%

“…7 and 15). In addition, antisera against serotonin and chromogranin A (7,16,17) were used for the identification of endocrine cells.…”

mentioning

confidence: 99%

Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

Hill¹,

Kühn²,

Zucht³

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The complete cell biological analysis of human guanylin, a recently discovered regulatory peptide, is offered in this investigation: (i) the nucleotide sequence of the gene, (ii) the isolation and characterization of its circulating molecular form, and (iii) its localization in enterochromaffin cells of the gut. As determined by molecular cloning, DNA sequencing, and comparison with the known cDNA sequence, the approximately 2.6-kbp large gene consists of three exons interrupted by two introns. The putative promoter region contains a TTTAAAA sequence motif and several potential binding sites for transcription factors such as AP-1, AP-2, Sp 1, and glucocorticoid receptors. The isolated hormonal form of guanylin is a 94-amino acid peptide with a molecular mass of 10.3 kDa. Western blot analysis of RP-HPLC fractions from blood plasma confirms this molecular form. Thus, guanylin is synthesized by gut enterochromaffin cells as a prohormone of 115 amino acids and is processed to the molecular form of 94 amino acids circulating in the blood.

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Mutual relationships between chromogranins A and B and gastrin in individual gastrin cells.

Cited by 21 publications

References 46 publications

Complex Co-localization of Chromogranins and Neurohormones in the Human Gastrointestinal Tract

Complex Co-localization of Chromogranins and Neurohormones in the Human Gastrointestinal Tract

Chromostatin, a chromogranin A-derived bioactive peptide, is present in human pancreatic insulin (beta) cells.

Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

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