JMV641: A potent bombesin receptor antagonist that inhibits Swiss 3T3 cell proliferation

1996 ◽  
Vol 65 (1) ◽  
pp. 91-97 ◽  
Author(s):  
J. Azay ◽  
D. Gagne ◽  
C. Devin ◽  
M. Llinares ◽  
J.A. Fehrentz ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Receptor Antagonist ◽  
Bombesin Receptor ◽  
Swiss 3T3 ◽  
Swiss 3T3 Cell

scholarly journals Solubilization of the bombesin receptor from Swiss 3T3 cell membranes

FEBS Letters ◽  
1990 ◽  
Vol 263 (1) ◽  
pp. 80-84 ◽  
Author(s):  
Arnold Coffer ◽  
Isabel Fabregat ◽  
James Sinnett-Smith ◽  
Enrique Rozengurt
Keyword(s):  
Cell Membranes ◽  
Bombesin Receptor ◽  
Swiss 3T3 ◽  
Swiss 3T3 Cell

scholarly journals A peptide that inhibits the mitogenic stimulation of Swiss 3T3 cells by bombesin or vasopressin

1985 ◽  
Vol 231 (3) ◽  
pp. 781-784 ◽  
Author(s):  
A N Corps ◽  
L H Rees ◽  
K D Brown
Keyword(s):  
Cell Proliferation ◽  
Synthetic Peptide ◽  
3T3 Cells ◽  
Wide Range ◽  
Vasopressin Receptors ◽  
Bombesin Receptor ◽  
Swiss 3T3 ◽  
Stimulation Of

The synthetic peptide [D-Arg1,D-Pro2,D-Trp7,9,Leu1]substance P inhibits the stimulation of DNA synthesis induced in Swiss 3T3 cells by bombesin or vasopressin, but not that induced by a wide range of other growth factors and mitogens. The stimulation induced by 10 pM-3 nM-bombesin is inhibited by 1-30 microM-antagonist in a manner consistent with competition at the bombesin receptor. The inhibition by the antagonist of the stimulation induced by vasopressin suggests a previously unrecognized interaction of the antagonist with vasopressin receptors. The antagonist should be useful in studies of cell proliferation both in vivo and in vitro.

scholarly journals Differential involvement of ERK1-2and p38MAPKactivation on Swiss 3T3 cell proliferation induced by prostaglandin F2α

FEBS Letters ◽  
2006 ◽  
Vol 580 (10) ◽  
pp. 2512-2516 ◽  
Author(s):  
Andrés Dekanty ◽  
Sebastián Giulianelli ◽  
Omar A. Coso ◽  
Philip S. Rudland ◽  
Luis Jimenez de Asua
Keyword(s):  
Cell Proliferation ◽  
Prostaglandin F2α ◽  
Differential Involvement ◽  
Swiss 3T3 ◽  
Swiss 3T3 Cell

scholarly journals Effect of enzymic (collagenase) harvesting on the intracellular Na+/K+ ratio of Swiss/3T3 cells as revealed by X-ray microanalysis

1988 ◽  
Vol 90 (1) ◽  
pp. 99-104
Author(s):  
Z. Szallasi ◽  
A. Szallasi ◽  
F. Bojan ◽  
I. Zs-Nagy
Keyword(s):  
Cell Cultures ◽  
Freeze Fracture ◽  
Ion Concentration ◽  
Bulk Specimen ◽  
X Ray ◽  
Dependent Cell ◽  
Swiss 3T3 ◽  
K Concentration ◽  
Post Harvesting ◽  
Swiss 3T3 Cell

Swiss/3T3 cell cultures were harvested with 0.05% collagenase and after centrifugation the pellet was prepared by the freeze-fracture/freeze-drying (FFFD) method for bulk-specimen X-ray microanalysis. Time-dependent variations in the intracellular monovalent elemental concentrations (Na+, K+ and Cl-) as well as of the Na+/K+ ratio were followed for 120 min subsequent to harvesting. The quantitative measurements revealed a very considerable increase in the intracellular Na+ and Cl- accompanied by a decrease in the K+ concentration as soon as 5 min after harvesting. The Na+/K+ ratio had increased by this time to about 1.5 on average. These changes indicate a sustained depolarization of the cell membrane. During the first 60 min this depolarization tended to normalize as demonstrated by an exponential decrease in the intracellular Na+ and Cl- and an increase in the K+ content involving a decrease in the Na+/K+ ratio. The total intracellular monovalent ion concentration remained almost constant during this post-harvesting period. These results suggest that harvesting represents a serious depolarizing stimulus to the cells, the consequences of which are restored only after 1–2h. These alterations should be taken into consideration during various experimental designs when using anchorage-dependent cell cultures.

scholarly journals Effects of pertussis toxin on growth factor-stimulated inositol phosphate formation and DNA synthesis in Swiss 3T3 cells

1988 ◽  
Vol 249 (3) ◽  
pp. 917-920 ◽  
Author(s):  
C W Taylor ◽  
D M Blakeley ◽  
A N Corps ◽  
M J Berridge ◽  
K D Brown
Keyword(s):  
Growth Factor ◽  
Dna Synthesis ◽  
Pertussis Toxin ◽  
Inositol Phosphates ◽  
Inositol Phosphate ◽  
Phosphoinositide Hydrolysis ◽  
Polypeptide Growth Factors ◽  
Swiss 3T3 ◽  
Swiss 3T3 Cell ◽  
Stimulation Of

We have compared the effects of pretreatment of Swiss 3T3 cell with pertussis toxin on the stimulation of DNA synthesis and phosphoinositide hydrolysis in response to a wide variety of mitogens. The toxin substantially inhibited the stimulation of DNA synthesis in response to a phorbol ester or various peptide and polypeptide growth factors irrespective of their ability to activate phosphoinositidase C. Production of inositol phosphates in response to platelet-derived growth factor, fibroblast growth factor and prostaglandin F2 alpha were unaffected by the toxin while bombesin- and vasopressin-stimulated formation of inositol phosphates were inhibited by only 27 and 23% respectively. These results argue against a major role for a pertussis toxin-sensitive G protein in coupling any of these mitogen receptors to activation of a phosphoinositidase C. Furthermore, the results suggest that the widespread inhibitory effects of pertussis toxin on mitogen-stimulated DNA synthesis may be unrelated to the toxin's limited actions on phosphoinositide hydrolysis.

Gastrin-releasing peptide directly releases pepsinogen from guinea pig chief cells

1990 ◽  
Vol 259 (5) ◽  
pp. G760-G766 ◽  
Author(s):  
S. Fiorucci ◽  
K. E. McArthur
Keyword(s):  
Substance P ◽  
Guinea Pig ◽  
Receptor Antagonist ◽  
Fold Increase ◽  
Chief Cells ◽  
Gastrin Releasing Peptide ◽  
Basal Release ◽  
Substance P Receptor ◽  
Bombesin Receptor ◽  
Muscarinic Agents

Gastrin-releasing peptide (GRP) and bombesin can stimulate pepsinogen release by both gastrin-dependent and -independent mechanisms. Using isolated guinea pig gastric chief cells, we determined that GRP can act directly on the guinea pig chief cell to cause pepsinogen release. GRP and bombesin stimulated a 2.5- to 3-fold increase in pepsinogen release above basal release. Substance P also stimulated a small but significant increase in pepsinogen release. No gastrin immunoreactivity was detected in the supernatants of cells stimulated with up to 1 microM GRP or bombesin or 1 mM carbachol. GRP-stimulated pepsinogen release was completely inhibited by GRP/bombesin receptor agonists as well as substance P receptor antagonist but not by antagonists to receptors for gastrin, the octapeptide of cholecystokinin (CCK-8), secretin, vasoactive intestinal peptide (VIP), or muscarinic agents. Substance P-stimulated pepsinogen release was completely inhibited by substance P receptor antagonist but not by GRP/bombesin receptor antagonists. An additive effect on pepsinogen release was seen when GRP was combined with maximally effective concentrations of adenosine 3',5'-cyclic monophosphate (cAMP)-mediated agents (VIP, secretin, 8-BrcAMP) but not with calcium-mediated agents (carbachol, CCK-8, gastrin). These results indicate that GRP can directly stimulate pepsinogen release from guinea pig chief cells by a specific GRP receptor that mobilizes intracellular calcium.

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