scholarly journals Multiple sources of sn-1,2-diacylglycerol in platelet-derived-growth-factor-stimulated Swiss 3T3 fibroblasts. Evidence for activation of phosphoinositidase C and phosphatidylcholine-specific phospholipase D

1991 ◽  
Vol 279 (2) ◽  
pp. 559-565 ◽  
Author(s):  
R Plevin ◽  
S J Cook ◽  
S Palmer ◽  
M J O Wakelam
Keyword(s):  
Growth Factor ◽  
Phospholipase D ◽  
Lag Time ◽  
Water Soluble ◽  
Platelet Derived Growth Factor ◽  
Second Phase ◽  
Multiple Sources ◽  
3T3 Fibroblasts ◽  
Swiss 3T3 ◽  
Swiss 3T3 Fibroblasts

Platelet-derived growth factor (PDGF) stimulated sn-1,2-diacylglycerol (DAG) mass formation in Swiss 3T3 fibroblasts with a lag time of some 30 s. The response was biphasic, with the second phase being sustained over time. PDGF also stimulated the formation of Ins(1,4,5)P3 with a similar lag time to the DAG response, suggesting that DAG is derived from PtdIns(4,5)P2 hydrolysis at this time point. PDGF-stimulated phosphatidylcholine (PtdCho) hydrolysis in Swiss 3T3 fibroblasts, as measured by the formation of water-soluble choline metabolites and phosphatidylbutanol (PtdBut) accumulation, was by a phospholipase D (PLD)-catalysed pathway which was kinetically downstream of initial PtdIns(4,5)P2 hydrolysis. Accumulation of PtdBut increased up to 15 min, suggesting that PLD activity is not rapidly densitized in response to PDGF. The kinetics of PtdCho hydrolysis closely paralleled the second phase of DAG formation, strongly suggesting that during prolonged stimulation periods PtdCho is a major source of DAG in these cells. However, since PtdIns(4,5)P2 breakdown was also prolonged, PDGF-stimulated DAG may be derived from both phospholipids. Down-regulation of protein kinase C (PKC), by pre-treatment with phorbol 12-myristate 13-acetate, abolished both [3H]choline and [3H]PtdBut formation, suggesting that PLD-catalysed PtdCho hydrolysis may be dependent on PKC activation, supporting its dependence on prior PtdIns(4,5)P2 hydrolysis.

scholarly journals Effect of the different dimeric forms of the platelet-derived growth factor on cellular responses in mouse Swiss 3T3 fibroblasts

FEBS Letters ◽  
1989 ◽  
Vol 255 (1) ◽  
pp. 191-195 ◽  
Author(s):  
E. Sturani ◽  
R. Brambilla ◽  
L. Morello ◽  
M.G. Cattaneo ◽  
R. Zippel ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cellular Responses ◽  
Platelet Derived Growth Factor ◽  
3T3 Fibroblasts ◽  
Swiss 3T3 ◽  
Swiss 3T3 Fibroblasts

scholarly journals Partial purification and characterization of a growth factor present in goat's colostrum. Similarities with platelet-derived growth factor

1984 ◽  
Vol 219 (2) ◽  
pp. 609-617 ◽  
Author(s):  
K D Brown ◽  
D M Blakeley
Keyword(s):  
Growth Factor ◽  
Dna Synthesis ◽  
Biological Properties ◽  
Exchange Chromatography ◽  
Platelet Derived Growth Factor ◽  
Partial Purification ◽  
A431 Cells ◽  
3T3 Fibroblasts ◽  
Swiss 3T3 ◽  
Swiss 3T3 Fibroblasts

A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C for 5 min) polypeptide with Mr approx. 35000. The polypeptide resists denaturation by guanidinium chloride or urea but is totally inactivated by treatment with reducing agents. The factor, which we have termed colostric basic growth factor (CBGF), inhibits the binding of 125I-labelled epidermal growth factor (125I-EGF) to Swiss 3T3 fibroblasts but does not inhibit 125I-EGF binding to epidermoid A431 cells. CBGF interacts synergistically with plasma in stimulating DNA synthesis in quiescent Swiss 3T3 cells. The chemical and biological properties of CBGF are thus very similar to the properties reported for the human platelet-derived growth factor. Although high concentrations of CBGF are present in the colostrum of goats, cows, and sheep, the milk of these species contains little or no factor. The origin and possible functions of CBGF are unknown.

scholarly journals Functional Proteomic Analysis of Long-term Growth Factor Stimulation and Receptor Tyrosine Kinase Coactivation in Swiss 3T3 Fibroblasts

2012 ◽  
Vol 11 (12) ◽  
pp. 1690-1708 ◽  
Author(s):  
Kohji Nagano ◽  
Akunna Akpan ◽  
Gayathri Warnasuriya ◽  
Steven Corless ◽  
Nick Totty ◽  
...  
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Proteomic Analysis ◽  
3T3 Fibroblasts ◽  
Swiss 3T3 ◽  
Swiss 3T3 Fibroblasts

scholarly journals Inhibition of mitogen-induced DNA synthesis by bafilomycin A1 in Swiss 3T3 fibroblasts

1996 ◽  
Vol 313 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Andrew J. SAURIN ◽  
Jane HAMLETT ◽  
Michael J. CLAGUE ◽  
Stephen R. PENNINGTON
Keyword(s):  
Growth Factor ◽  
Dna Synthesis ◽  
Kinase Activity ◽  
Bafilomycin A1 ◽  
Tyrosine Kinase Activity ◽  
3T3 Fibroblasts ◽  
Mitogenic Signalling ◽  
Epidermal Growth ◽  
Swiss 3T3 ◽  
Swiss 3T3 Fibroblasts

Quiescent cells (in G0) can be stimulated to enter the cell cycle and proceed to DNA synthesis in S-phase by a wide range of growth factors and mitogens. Activation of cell-surface growth factor receptors with intrinsic protein tyrosine kinase activity initiates autophosphorylation of the receptors and subsequent activation of signal transduction cascades. After activation the receptors undergo ligand-induced internalization to endosomes, which become acidified by the action of a vacuolar H+-ATPase (V-ATPase). The extent to which vesicular acidification plays a role in mitogenic signalling by receptors with intrinsic tyrosine kinase activity remains unknown. Here we have shown that bafilomycin A1, a specific inhibitor of V-ATPase, inhibits endosome acidification and mitogen-induced DNA synthesis in Swiss 3T3 fibroblasts. Addition of bafilomycin A1 at successively later times during G1 progressively decreased the inhibition of DNA synthesis such that no inhibition was observed when bafilomycin A1 was added at the onset of S-phase. Bafilomycin A1 also induced a dramatic but reversible change in the morphology of Swiss 3T3 cells. However, the rapid activation of c-fos mRNA accumulation by epidermal growth factor and insulin was unaffected by bafilomycin A1. Together, the results suggest that activation of the V-ATPase plays an important role in the mitogenic signalling pathways that occur during the G1 phase of the cell cycle but is not required for the initial epidermal growth factor and insulin-evoked signalling events that lead to c-fos mRNA expression.

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