ISSN:
0730-2312
Keywords:
GRP receptor
;
cytosolic calcium
;
growth
;
arachidonic acid
;
protien kinase C
;
Life Sciences
;
Molecular Cell Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Previously, GRP receptors wer charachterized in sasmll cell lung cancer cells and here non-small cell lung cancer (NSCLC) cells were investigated: (125I-Tyr4) bombesin (BN) or 125I-GRP bound with high affinity to NCI-H720 (lung carcioid) and NCI-H1299 (large cell carcinoma) cells. Binding was specific, time dependent, and saturable. Specific (125I-Tyr4) BN binding to NCI-H1299 cells was inhibited with high affinity by GRP, BN, GRP14-27, (D-Phe6)BN6-13methyl ester, moderate affinity by NMB, and low affinity by NMB, and low, and low affinity by GRP1-16. BN (10nM) transiently elevated cytosolic calcium in a dose dependent manner. BN caused translocation of protein kinase C from the cytosol to the membrane and the translocation caused by BN was reversed by (D-Phe6)BN6-13 methylester. BN stimulated arachidonic acid release and the increase caused by BN was reversed by (D-Phe6)BN6-13 methylester. Using a clonogenic assay, BN stimulated the growth of NCI-H720 cells, and ythe number of colonies was reduced using (D-Phe6)BN6-13 methylester. These data suggest that GRP receptors that are present in lung carcinoid and NSCLC cells may regulate proliferation. © 1996 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jcb.240630520
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