ArticleEndocrine pathology2003
Chromogranin a processing in human pituitary adenomas and carcinomas: analysis with region-specific antibodies.
Article in Endocrine pathology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
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Who cites it
9 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.
- Genetic aspects of pituitary carcinoma: A systematic review.Medicine · 2016Pooled it
- Characterization of the EM66 Biomarker in the Pituitary and Plasma of Healthy Subjects With Different Gonadotroph Status and Patients With Gonadotroph Tumor.Frontiers in endocrinology · 2019Article
- Immunohistochemical and biochemical studies with region-specific antibodies to chromogranins A and B and secretogranins II and III in neuroendocrine tumors.Cellular and molecular neurobiology · 2010Review
- Article
- Immunohistochemical separation of follicular variant of papillary thyroid carcinoma from follicular adenoma.Endocrine pathology · 2006Article
- Chromogranin A transcription and gene expression in Folliculostellate (TtT/GF) cells inhibit cell growth.Endocrine pathology · 2005Article
- Analysis of Cox-2 and thromboxane synthase expression in pituitary adenomas and carcinomas.Endocrine pathology · 2004Article
- Expression of cyclooxygenase-2 and thromboxane synthase in non-neoplastic and neoplastic thyroid lesions.Endocrine pathology · 2004Article
- Regulation of cell growth and expression of 7B2, PC2, and PC1/3 by TGFbeta 1 and sodium butyrate in a human pituitary cell line (HP75).Endocrine · 2003Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The expression of various chromogranin A (CgA) peptide fragments was examined with region-specific antisera in benign and malignant pituitary tumors. Analysis of the proconvertases responsible for proteolytic processing of CgA, prohormone convertase 1/3 (PC1/3), and PC2 was also performed. Adenomas were studied using tissue microarrays, and a larger tissue section of a subset of the prolactin (PRL) adenomas was used to compare to the tissue microarray analysis. Carcinomas were analyzed using larger tissue sections. There were differences in CgA proteolytic products detected between the functional (PRL, adrenocorticotropic hormone [ACTH], and growth hormone tumors and the nonfunctional (gonadotroph and null cell) tumors, with the former group expressing lower levels of many peptides. These differences were most notable in the PRL adenomas and carcinomas in which the region-specific antisera against vasostatin I and vasostatin II detected these fragments in the lowest percentage of tumors and/or had the weakest immunoreactivity. The CgA peptide fragment detected by CgA 176-195 (chromacin) antiserum was expressed by the highest percentage of most functional and nonfunctional benign and malignant pituitary tumors. ACTH carcinomas (n = 3) were more strongly immunoreactive compared to the ACTH adenomas. These results show that there is differential expression of CgA peptide fragments and PC1/3 among different types of pituitary tumors and that ACTH pituitary carcinomas have higher levels of immunoreactive CgA peptide fragments compared to ACTH adenomas. This study also shows the utility of tissue microarrays in the analysis of a large group of tumors with regionspecific antisera.
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Registered trials
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