Epidermal growth factor is a constant component of normal human tear fluid

1989 ◽  
Vol 227 (2) ◽  
pp. 184-187 ◽  
Author(s):  
G. -B. van Setten ◽  
L. Viinikka ◽  
T. Tervo ◽  
K. Pesonen ◽  
A. Tarkkanen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Constant Component ◽  
Tear Fluid ◽  
Normal Human ◽  
Epidermal Growth

Effects of epidermal growth factor and 12-O-tetradecanoylphorbol-13-acetate on metabolism of the epidermal growth factor receptor in normal human fibroblasts

1984 ◽  
Vol 4 (9) ◽  
pp. 1718-1724
Author(s):  
S J Decker
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Half Life ◽  
Egf Receptor ◽  
Human Fibroblasts ◽  
Tumor Promoter ◽  
Minor Amount ◽  
Detectable Effect ◽  
Normal Human ◽  
Epidermal Growth

The biosynthesis, phosphorylation, and degradation of the epidermal growth factor (EGF) receptor were examined in normal human fibroblasts. The receptor was initially synthesized as an Mr = 160,000 immature form which matured to an Mr = 170,000 form in a monensin-sensitive manner. Tunicamycin treatment led to the accumulation of an Mr = 130,000 protein. The receptor was phosphorylated on serine and threonine residues in normally growing and quiescent cells, and treatment with EGF or the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) resulted in a two- to threefold increase in receptor-bound phosphate. EGF increased the amount of phosphoserine and phosphothreonine and caused the appearance of a minor amount of phosphotyrosine. TPA increased the levels of phosphoserine and phosphothreonine exclusively. Prior treatment with TPA inhibited the EGF-dependent appearance of phosphotyrosine in the receptor. Analysis of tryptic phosphopeptides revealed that six of the seven major peptides were common to the receptor from cells treated with EGF or TPA. EGF strongly stimulated [3H]thymidine incorporation in confluent cells, increased final saturation density three to fourfold, and increased whole-cell levels of phosphotyrosine about threefold. Treatment of cells with TPA before addition of EGF inhibited all three of these EGF-dependent responses. EGF also decreased the receptor half-life from 15 h to 1 h, but this was not inhibited by TPA. TPA alone had no detectable effect on the receptor half-life.

scholarly journals Effects of epidermal growth factor and 12-O-tetradecanoylphorbol-13-acetate on metabolism of the epidermal growth factor receptor in normal human fibroblasts.

1984 ◽  
Vol 4 (9) ◽  
pp. 1718-1724 ◽  
Author(s):  
S J Decker
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Half Life ◽  
Egf Receptor ◽  
Human Fibroblasts ◽  
Tumor Promoter ◽  
Minor Amount ◽  
Detectable Effect ◽  
Normal Human ◽  
Epidermal Growth

The biosynthesis, phosphorylation, and degradation of the epidermal growth factor (EGF) receptor were examined in normal human fibroblasts. The receptor was initially synthesized as an Mr = 160,000 immature form which matured to an Mr = 170,000 form in a monensin-sensitive manner. Tunicamycin treatment led to the accumulation of an Mr = 130,000 protein. The receptor was phosphorylated on serine and threonine residues in normally growing and quiescent cells, and treatment with EGF or the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) resulted in a two- to threefold increase in receptor-bound phosphate. EGF increased the amount of phosphoserine and phosphothreonine and caused the appearance of a minor amount of phosphotyrosine. TPA increased the levels of phosphoserine and phosphothreonine exclusively. Prior treatment with TPA inhibited the EGF-dependent appearance of phosphotyrosine in the receptor. Analysis of tryptic phosphopeptides revealed that six of the seven major peptides were common to the receptor from cells treated with EGF or TPA. EGF strongly stimulated [3H]thymidine incorporation in confluent cells, increased final saturation density three to fourfold, and increased whole-cell levels of phosphotyrosine about threefold. Treatment of cells with TPA before addition of EGF inhibited all three of these EGF-dependent responses. EGF also decreased the receptor half-life from 15 h to 1 h, but this was not inhibited by TPA. TPA alone had no detectable effect on the receptor half-life.

Ocular disease leads to decreased concentrations of epidermal growth factor in the tear fluid

1991 ◽  
Vol 10 (6) ◽  
pp. 523-527 ◽  
Author(s):  
G. B. van Setten ◽  
T. Tervo ◽  
L. Viinikka ◽  
K. Pesonen ◽  
J. Perheentupa ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ocular Disease ◽  
Tear Fluid ◽  
Epidermal Growth
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