Peptidylglycine α-amidating monooxygenase in neuroendocrine tumors: Its identification, characterization, quantification, and relation to the grade of morphologic differentiation, amidated peptide content, and granin immunocytochemistry

Lucio Scopsi, Rita Lee, Maria Gullo, Paola Collini, E. Jean Husten, Betty A. Eipper

Research output: Contribution to journalArticle

Abstract

One hundred forty-seven human neuroendocrine tumors were immunocytochemically screened with antibodies directed against several portions of peptidylglycine α-amidating monooxygenase, the enzyme responsible for the amidation of neurohormonal peptides. A subset of 23 tumors was then studied by enzyme assay and immunoblotting. Although the enzyme was present in all neuroendocrine cell types, the specimens with the highest content were from well-differentiated tumors known to produce amidated peptides, such as intestinal and bronchial carcinoids, gastrinomas, medullary thyroid carcinomas, and pancreatic polypeptide-producing tumors. A high enzyme content also was observed in well-differentiated tumors not known to contain amidated products (e.g., gastric carcinoids). A good correlation was observed between staining intensity of the enzyme on protein blots and immunocytochemical signal. Tumor-specific differences in cleavage of the less active high-molecular-weight forms may contribute to discrepancies between enzyme activity level and immunochemical expression. Although no clear-cut association was found between enzyme immunoreactivity and expression of a single granin, canonic secretory granule markers, all enzyme-reactive tumors were found to contain high levels of at least one of the three granins (chromogranin A, chromogranin B, or secretogranin II).

Original languageEnglish
Pages (from-to)120-132
Number of pages13
JournalApplied Immunohistochemistry
Volume6
Issue number3
DOIs
Publication statusPublished - 1998

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Chromogranins
Neuroendocrine Tumors
Immunohistochemistry
Peptides
Enzymes
Neoplasms
Carcinoid Tumor
Secretogranin II
Chromogranin B
Gastrinoma
Pancreatic Polypeptide
Chromogranin A
Neuroendocrine Cells
Secretory Vesicles
Enzyme Assays
peptidylglycine monooxygenase
Immunoblotting
Stomach
Molecular Weight
Staining and Labeling

Keywords

  • Amidating enzyme
  • Granins
  • Morphologic differentiation
  • Neuroendocrine tumor
  • Regulatory peptides

ASJC Scopus subject areas

  • Anatomy
  • Medical Laboratory Technology

Cite this

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title = "Peptidylglycine α-amidating monooxygenase in neuroendocrine tumors: Its identification, characterization, quantification, and relation to the grade of morphologic differentiation, amidated peptide content, and granin immunocytochemistry",
abstract = "One hundred forty-seven human neuroendocrine tumors were immunocytochemically screened with antibodies directed against several portions of peptidylglycine α-amidating monooxygenase, the enzyme responsible for the amidation of neurohormonal peptides. A subset of 23 tumors was then studied by enzyme assay and immunoblotting. Although the enzyme was present in all neuroendocrine cell types, the specimens with the highest content were from well-differentiated tumors known to produce amidated peptides, such as intestinal and bronchial carcinoids, gastrinomas, medullary thyroid carcinomas, and pancreatic polypeptide-producing tumors. A high enzyme content also was observed in well-differentiated tumors not known to contain amidated products (e.g., gastric carcinoids). A good correlation was observed between staining intensity of the enzyme on protein blots and immunocytochemical signal. Tumor-specific differences in cleavage of the less active high-molecular-weight forms may contribute to discrepancies between enzyme activity level and immunochemical expression. Although no clear-cut association was found between enzyme immunoreactivity and expression of a single granin, canonic secretory granule markers, all enzyme-reactive tumors were found to contain high levels of at least one of the three granins (chromogranin A, chromogranin B, or secretogranin II).",
keywords = "Amidating enzyme, Granins, Morphologic differentiation, Neuroendocrine tumor, Regulatory peptides",
author = "Lucio Scopsi and Rita Lee and Maria Gullo and Paola Collini and Husten, {E. Jean} and Eipper, {Betty A.}",
year = "1998",
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T1 - Peptidylglycine α-amidating monooxygenase in neuroendocrine tumors

T2 - Its identification, characterization, quantification, and relation to the grade of morphologic differentiation, amidated peptide content, and granin immunocytochemistry

AU - Scopsi, Lucio

AU - Lee, Rita

AU - Gullo, Maria

AU - Collini, Paola

AU - Husten, E. Jean

AU - Eipper, Betty A.

PY - 1998

Y1 - 1998

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KW - Regulatory peptides

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