Activation of a calcium-permeable cation channel by insulin-like growth factor II in BALB/c 3T3 cells

1988 ◽  
Vol 255 (4) ◽  
pp. C442-C446 ◽  
Author(s):  
H. Matsunaga ◽  
I. Nishimoto ◽  
I. Kojima ◽  
N. Yamashita ◽  
K. Kurokawa ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Influx ◽  
Cation Channel ◽  
Dependent Manner ◽  
Insulin Like Growth Factor ◽  
3T3 Cells ◽  
Patch Clamp Technique ◽  
Factor Ii ◽  
Epidermal Growth

Insulin-like growth factor II (IGF II) is a member of somatomedin family and is a potent mitogen in various types of mammalian cells. We have recently reported that IGF II stimulates calcium influx in competent BALB/c 3T3 cells primed with epidermal growth factor (J. Biol. Chem. 262: 12120-12126, 1987). Using patch-clamp technique, we show here an IGF II-sensitive cation channel in BALB/c 3T3 cell plasma membrane. Calcium is permeable to this cation channel and its opening behavior is independent of membrane potential. IGF II increases the opening probability of the identical channel in cells pretreated sequentially with platelet-derived growth factor and epidermal growth factor, whereas IGF II does not affect the opening of the channel in G0-arrested cells. This cation channel activity is observed only when IGF II is included in the patch pipette, indicating direct regulation of the channel by IGF II. We suggest that IGF II stimulates calcium influx by opening this cation channel and that IGF II activates the channel in a unique cell cycle-dependent manner.

Calcium Signalling System Triggered by INsulin-Like Growth Factor II

Physiology ◽  
1989 ◽  
Vol 4 (3) ◽  
pp. 94-97
Author(s):  
I Nishimoto ◽  
I Kojima
Keyword(s):  
Growth Factors ◽  
Dna Replication ◽  
Growth Factor ◽  
Calcium Influx ◽  
Calcium Signalling ◽  
Insulin Like Growth Factor ◽  
Permeable Channel ◽  
Signalling System ◽  
Factor Ii ◽  
Epidermal Growth

In BALB/c 3T3 fibroblast, the insulin-like growth factor (IGF-II) stimulates DNA replication when added to cells pretreated sequentially with platelet-derived and epidermal growth factors. In these cells, IGF-II increases calcium influx by opening a voltage-independent calcium-permeable channel, and calcium influx is an intracellular message of the IGF-II action.

The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment

1992 ◽  
Vol 12 (12) ◽  
pp. 5843-5856
Author(s):  
J Meisenhelder ◽  
T Hunter
Keyword(s):  
Monoclonal Antibodies ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phospholipase C ◽  
Platelet Derived Growth Factor ◽  
Dependent Manner ◽  
3T3 Cells ◽  
Epidermal Growth ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

In the course of our investigation of phospholipase C (PLC)-gamma 1 phosphorylation by using a set of anti-PLC-gamma 1 monoclonal antibodies (P.-G. Suh, S. H. Ryu, W. C. Choi, K.-Y. Lee, and S. G. Rhee, J. Biol. Chem. 263:14497-14504, 1988), we found that some of these antibodies directly recognize a 47-kDa protein. We show here that this 47-kDa protein is identical to the SH2/SH3-containing protein Nck (J. M. Lehmann, G. Riethmuller, and J. P. Johnson, Nucleic Acids Res. 18:1048, 1990). Nck was found to be constitutively phosphorylated on serine in resting NIH 3T3 cells. Platelet-derived growth factor (PDGF) treatment led to increased Nck phosphorylation on both tyrosine and serine. Nck was also found to be phosphorylated on tyrosine in epidermal growth factor (EGF)-treated A431 cells and in v-Src-transformed NIH 3T3 cells. Multiple sites of serine phosphorylation were detected in Nck from resting cells, and no novel sites were found upon PDGF or EGF treatment. A single major tyrosine phosphorylation site was found in Nck in both PDGF- and EGF-treated cells and in v-Src-transformed cells. This same tyrosine was phosphorylated in vitro by purified PDGF and EGF receptors and also by pp60c-src. We compared the phosphorylation of Nck and PLC-gamma 1 in several cell lines transformed by oncogenes with different modes of transformation. Although PLC-gamma 1 and Nck have significant amino acid identity, particularly in their SH3 regions, and both associate with growth factor receptors in a ligand-dependent manner, they were not always phosphorylated on tyrosine in a coincident manner.

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