CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jones, C. L.
Right arrow Articles by Kane, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jones, C. L.
Right arrow Articles by Kane, M. A.

Cell Growth & Differentiation, Vol 6, Issue 12 1627-1634, Copyright © 1995 by American Association of Cancer Research


ARTICLES

Properties of classic protein kinase C in human small cell lung carcinoma NCI-H345 cells

CL Jones, LK Beck, JP Brozna, M Holley, EJ Dempsey and MA Kane
Medical Oncology Section, Denver Veterans Affairs Medical Center, Colorado 80220, USA.

Bombesin-like peptides (BLPs) activate protein kinase C (PKC), which leads to proliferation in nonmalignant Swiss 3T3 cells. The purpose of this study was to determine if PKC expression in the classic human small cell lung carcinoma NCI-H345 cell line, which has an autocrine growth loop involving BLPs, exhibited unique properties that could result in malignant behavior. PKC activity and phorbol dibutyrate binding in NCI-H345 cells had properties similar to other reports. PKC activity in the cytosolic fraction increased to 100% as cells proliferated through lag, log, and plateau growth states. However, during the first 3 days after plating (lag growth state), 40-50% of the PKC activity was membrane associated, indicating a substantial portion in an activated form, possibly a result of BLP autocrine stimulation. NCI-H345 cells expressed the PKC isoenzymes alpha, beta, delta, sigma, and eta, but not gamma or epsilon, a pattern different from Swiss 3T3 cells or normal brain. further characterization of the Ca2+/phospholipid-dependent (classic) PKC isoenzymes, alpha and beta, showed that PKC beta was predominantly cytosolic (80%) as expected, but PKC alpha was primarily membrane associated (80-90%). Exposure of NCI-H345 cells to 200 nm phorbol 12-myristyl 13-acetate rapidly (within 2 min) decreased cytosolic PKC activity, with no change in the particulate activity, but did not alter [3H]-thymidine incorporation or subcellular distribution of PKC alpha or beta by Western blot. These results suggest altered PKC regulation in human small cell lung carcinoma NCI-H345 cells, which could contribute to their malignant behavior.


This article has been cited by other articles:


Home page
Mol. Cell. Biol.Home page
A. Vallentin, T.-C. Lo, and D. Joubert
A Single Point Mutation in the V3 Region Affects Protein Kinase C{alpha} Targeting and Accumulation at Cell-Cell Contacts
Mol. Cell. Biol., May 15, 2001; 21(10): 3351 - 3363.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
L. Paolucci and E. Rozengurt
Protein Kinase D in Small Cell Lung Cancer Cells: Rapid Activation through Protein Kinase C
Cancer Res., February 1, 1999; 59(3): 572 - 577.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1995 by the American Association of Cancer Research.