Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 45: 549-560, 1999;
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (7)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Børglum Jensen, T.
Right arrow Articles by Rehfeld, J. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Børglum Jensen, T.
Right arrow Articles by Rehfeld, J. F.
Related Collections
Right arrow Proteomics and Protein Markers
Right arrow Endocrinology and Metabolism
Right arrow Automation and Analytical Techniques
(Clinical Chemistry. 1999;45:549-560.)
© 1999 American Association for Clinical Chemistry, Inc.

Articles

Library of Sequence-specific Radioimmunoassays for Human Chromogranin A

Tine Børglum Jensen, Linda Hilsted and Jens F. Rehfelda

a Address correspondence to this author at: Department of Clinical Biochemistry (KB3013), Rigshospitalet, Blegdamsvej 9, DK-2100 Copenhagen Ø, Denmark. Fax 45-35454640; e-mail rehfeld{at}rh.dk

Background: Human chromogranin A (CgA) is an acidic protein widely expressed in neuroendocrine tissue and tumors. The extensive tissue- and tumor-specific cleavages of CgA at basic cleavage sites produce multiple peptides.

Methods: We have developed a library of RIAs specific for different epitopes, including the NH2 and COOH termini and three sequences adjacent to dibasic sites in the remaining part of CgA.

Results: The antisera raised against CgA(210–222) and CgA(340–348) required a free NH2 terminus for binding. All antisera displayed high titers, high indexes of heterogeneity (~1.0), and high binding affinities (Keff0 ~ 0.1 x 1012 to 1.0 x 1012 L/mol), implying that the RIAs were monospecific and sensitive. The concentration of CgA in different tissues varied with the assay used. Hence, in a carcinoid tumor the concentration varied from 0.5 to 34.0 nmol/g tissue depending on the specificity of the CgA assay. The lowest concentration in all tumors was measured with the assay specific for the NH2 terminus of CgA. This is consistent with the relatively low concentrations measured in plasma from carcinoid tumor patients by the N-terminal assay, whereas the assays using antisera raised against CgA(210–222) and CgA(340–348) measured increased concentrations.

Conclusion: Only some CgA assays appear useful for diagnosis of neuroendocrine tumors, but the entire library is valuable for studies of the expression and processing of human CgA.© 1999 American Association for Clinical Chemistry




The following articles in journals at HighWire Press have cited this article:


Home page
 Clin. Chem.Home page
T. Borglum, J. F. Rehfeld, L. B. Drivsholm, and L. Hilsted
Processing-Independent Quantitation of Chromogranin A in Plasma from Patients with Neuroendocrine Tumors and Small-Cell Lung Carcinomas
Clin. Chem., March 1, 2007; 53(3): 438 - 446.
[Abstract] [Full Text] [PDF]

Home page
 JNMHome page
M. d'Herbomez, V. Gouze, D. Huglo, M. Nocaudie, F. Pattou, C. Proye, J.-L. Wemeau, and X. Marchandise
Chromogranin A Assay and 131I-MIBG Scintigraphy for Diagnosis and Follow-Up of Pheochromocytoma
J. Nucl. Med., July 1, 2001; 42(7): 993 - 997.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the American Association for Clinical Chemistry.