JOE
HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

DOI: 10.1677/joe.0.1610475
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI 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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (5)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Brar, B.
Right arrow Articles by Lowry, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brar, B.
Right arrow Articles by Lowry, P.
Journal of Endocrinology, Vol 161, Issue 3, 475-484
Copyright © 1999 by Society for Endocrinology

Articles

The differential processing of proenkephalin A in mouse and human breast tumour cell lines

BK Brar and PJ Lowry


We have carried out an investigation into the processing of the enkephalin-like immunoreactivity reported in breast tissue using two human breast tumour cell lines and a mouse tumour cell line. A 46 kDa form of proenkephalin (PE) has been observed in the cell lysates of two human breast tumour cell lines (MCF-7, ZR-75-1) and the mouse androgen-responsive Shionogi breast carcinoma cell line (SC115). PE processing in the cell lysates of these cells was assessed by a specific met-enkephalin RIA. The basal levels of processed PE in the MCF-7, ZR-75-1 and SC115 cell lysates were 30, 30 and 76% respectively. The processing enzymes PC1 and PC2, which have been implicated in the differential processing of PE, were detected by immunoblot analysis in these cells. PC1 was found within the cell extracts of all three cell lines. PC2 was only observed in the SC115 cell line, which may account for the higher percentage of processed PE measured. The cDNA of PC2 has been transfected into ZR-75-1 cells and this was accompanied by an increase in the level of processed PE from 30 to 76%. These breast tumour cell lines may provide a useful insight into the function of enkephalin-containing peptides in breast cancer.


This article has been cited by other articles:


Home page
 GeneticsHome page
L. Y. M. Rayburn, H. C. Gooding, S. P. Choksi, D. Maloney, A. R. Kidd III, D. E. Siekhaus, and M. Bender
amontillado, the Drosophila Homolog of the Prohormone Processing Protease PC2, Is Required During Embryogenesis and Early Larval Development
Genetics, January 1, 2003; 163(1): 227 - 237.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
A.-M. Khatib, G. Siegfried, M. Chretien, P. Metrakos, and N. G. Seidah
Proprotein Convertases in Tumor Progression and Malignancy : Novel Targets in Cancer Therapy
Am. J. Pathol., June 1, 2002; 160(6): 1921 - 1935.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Goumon, K. Lugardon, P. Gadroy, J.-M. Strub, I. D. Welters, G. B. Stefano, D. Aunis, and M.-H. Metz-Boutigue
Processing of Proenkephalin-A in Bovine Chromaffin Cells. IDENTIFICATION OF NATURAL DERIVED FRAGMENTS BY N-TERMINAL SEQUENCING AND MATRIX-ASSISTED LASER DESORPTION IONIZATION-TIME OF FLIGHT MASS SPECTROMETRY
J. Biol. Chem., December 1, 2000; 275(49): 38355 - 38362.
[Abstract] [Full Text] [PDF]


HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the Society for Endocrinology.