scholarly journals Lack of association of epidermal growth factor-, insulin-, and serum-induced mitogenesis with stimulation of phosphoinositide degradation in BALB/c 3T3 fibroblasts.

1986 ◽  
Vol 261 (2) ◽  
pp. 723-727
Author(s):  
J M Besterman ◽  
S P Watson ◽  
P Cuatrecasas
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
3T3 Fibroblasts ◽  
Epidermal Growth ◽  
Stimulation Of

Synergistic stimulation of Swiss mouse 3T3 fibroblasts by epidermal growth factor and other factors in human mammary secretions

1987 ◽  
Vol 112 (1) ◽  
pp. 151-159 ◽  
Author(s):  
A. N. Corps ◽  
D. M. Blakeley ◽  
J. Carr ◽  
L. H. Rees ◽  
K. D. Brown
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Protein Concentration ◽  
Gel Filtration ◽  
Functional Class ◽  
Swiss Mouse ◽  
Egf Receptors ◽  
3T3 Fibroblasts ◽  
Epidermal Growth ◽  
Stimulation Of

ABSTRACT The concentration of epidermal growth factor (EGF) in human mammary secretions was about 50 nmol/l for several weeks prepartum. It then fell to about 13 nmol/l within 4 days after parturition, in parallel with the decrease in protein concentration which is associated with the onset of lactation. In contrast, the concentration of EGF in urine samples from the same donors remained constant throughout this period. All the immunoreactive EGF in mammary secretions competed at the EGF receptors on Swiss mouse 3T3 fibroblasts. The stimulation of these cells by samples of mammary secretions was, however, much greater than that induced by EGF alone, indicating the presence of other factors which synergize with EGF. Gel filtration of mammary secretions revealed two major peaks of mitogenic activity, corresponding to EGF and a factor of higher molecular weight. The latter could synergize with added EGF, insulin or bombesin, and thus falls into a different functional class from any of these factors. J. Endocr. (1987) 112, 151–159

scholarly journals Stimulation of prostaglandin E2 synthesis in cloned osteoblastic cells of mouse (MC3T3-E1) by epidermal growth factor.

1986 ◽  
Vol 261 (33) ◽  
pp. 15410-15415
Author(s):  
K Yokota ◽  
M Kusaka ◽  
T Ohshima ◽  
S Yamamoto ◽  
N Kurihara ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Prostaglandin E2 ◽  
Osteoblastic Cells ◽  
Epidermal Growth ◽  
Stimulation Of

Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP

1992 ◽  
Vol 12 (12) ◽  
pp. 5816-5823
Author(s):  
D Park ◽  
S G Rhee
Keyword(s):  
Monoclonal Antibodies ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Immunoglobulin M ◽  
Rat Tissues ◽  
A431 Cells ◽  
Sh3 Domains ◽  
Epidermal Growth ◽  
Stimulation Of

The 47-kDa protein coimmunoprecipitated with phospholipase C (PLC)-gamma 1 by anti-PLC-gamma 1 monoclonal antibodies is proved to be Nck, a protein composed almost exclusively of one SH2 and three SH3 domains. Nck and PLC-gamma 1 are recognized by certain anti-PLC-gamma 1 monoclonal antibodies because Nck and PLC-gamma 1 share an epitope that likely is located in their SH3 domains. Nck is widely distributed in rat tissues, with an especially high level of expression in testes. The expression levels of Nck remains unchanged during the development of rat brain, whereas PLC-gamma 1 decreases during the same developmental period. Stimulation of A431 cells with epidermal growth factor elicits the tight association of Nck with the epidermal growth factor receptor and phosphorylation of Nck on both serine and tyrosine residues. The phosphorylation of Nck is also enhanced in response to stimulation of the nerve growth factor receptor in PC12 cells, the T-cell receptor complex in Jurkat cells, the membrane immunoglobulin M in Daudi cells, and the low-affinity immunoglobulin G receptor (Fc gamma RII) in U937 cells. The phosphorylation of Nck was also enhanced following treatment of A431 cells with phorbol 12-myristate 13-acetate or forskolin. These results suggest that Nck is a target for a variety of protein kinases that might modulate the postulated role of Nck as an adaptor for the physical and functional coordination of signalling proteins.

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