help button home button Endocrine Society JCEM JCEM Call for Nominations for EIC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Submit a related Letter to the Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vangsted, A. J.
Right arrow Articles by Schwartz, T. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vangsted, A. J.
Right arrow Articles by Schwartz, T. W.

Journal of Clinical Endocrinology & Metabolism, Vol 70, 1586-1593, Copyright © 1990 by Endocrine Society

ARTICLES

Production of gastrin-releasing peptide-(18-27) and a stable fragment of its precursor in small cell lung carcinoma cells

AJ Vangsted and TW Schwartz
Laboratory of Molecular Endocrinology, University Department of Clinical Chemistry, Rigshospitalet, Copenhagen, Denmark.

The production and postsecretory stability of gastrin-releasing peptide (GRP) and the C-terminal part of the GRP precursor were studied in small cell lung cancer cell lines using RIAs developed against these two parts of the precursor. In three otherwise different cell lines (NIC-H345, NIC-H69, and NIC-H510), similar chromatographic patterns of mainly GRP-(18-27) and some GRP-(14-27) along with large fragments of the C-terminal counterpart of the precursor were found to be stored in the cells. In tissue culture medium, gel filtration chromatography indicated that postsecretory limited proteolysis of the GRP precursor fragments occurred. The amount of accumulated immunoreactivity varied among the three cell lines and between the two parts of the precursor. In medium in which only low amounts of GRP immunoreactivity accumulated, the radiolabeled GRP was degraded rapidly. When incubated with plasma, GRP-(14-27) disappeared within a few hours, whereas the C- terminal precursor fragments were stable. It is concluded that the postsecretory stability of peptides excised from the GRP precursor in small cell lung cancer cells varies under tissue culture conditions, but epitopes in the C-terminal part of the precursor are more stable in plasma than the small GRP peptides and, thus, may serve as a better indicator than GRP itself for expression of the GRP precursor in cancer cells.


This article has been cited by other articles:


Home page
 EndocrinologyHome page
O. Patel, C. Dumesny, A. Shulkes, and G. S. Baldwin
C-Terminal Fragments of the Gastrin-Releasing Peptide Precursor Stimulate Cell Proliferation via a Novel Receptor
Endocrinology, March 1, 2007; 148(3): 1330 - 1339.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
C. Dumesny, O. Patel, S. Lachal, A. S. Giraud, G. S. Baldwin, and A. Shulkes
Synthesis, Expression and Biological Activity of the Prohormone for Gastrin Releasing Peptide (ProGRP)
Endocrinology, January 1, 2006; 147(1): 502 - 509.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1990 by The Endocrine Society