5‘-(p-Fluorosulfonylbenzoyl)-2‘(or 3‘)-(methylanthraniloyl)adenosine, Fluorescent Affinity Labels for Adenine Nucleotide Binding Sites:  Interaction with the Kinase Active Site of the Receptor for Epidermal Growth Factor†

Biochemistry ◽  
1996 ◽  
Vol 35 (28) ◽  
pp. 9197-9203 ◽  
Author(s):  
Robert M. Scoggins ◽  
Ann E. Summerfield ◽  
Richard A. Stein ◽  
Cheryl A. Guyer ◽  
James V. Staros
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Active Site ◽  
Binding Sites ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Affinity Labels ◽  
Nucleotide Binding Sites ◽  
Epidermal Growth

Membrane vesicles of A431 cells contain one class of epidermal growth factor binding sites

1990 ◽  
Vol 1052 (3) ◽  
pp. 453-460 ◽  
Author(s):  
Jos A.M. Berkers ◽  
Paul M.P. van Bergen en Henegouwen ◽  
Arie J. Verkleij ◽  
Johannes Boonstra
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Binding Sites ◽  
Membrane Vesicles ◽  
A431 Cells ◽  
Factor Binding ◽  
Epidermal Growth

Interaction of epidermal growth factor with receptors on human and porcine thyroid membranes

1984 ◽  
Vol 102 (1) ◽  
pp. 57-61 ◽  
Author(s):  
H. Humphries ◽  
S. MacNeil ◽  
D. S. Munro ◽  
S. Tomlinson
Keyword(s):  
Enzyme Activity ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Binding Sites ◽  
Affinity Constant ◽  
Maximal Inhibition ◽  
High Affinity ◽  
Epidermal Growth ◽  
And Function ◽  
Bovine Tsh

ABSTRACT Recent evidence suggests that epidermal growth factor (EGF) may play an important role in the regulation of thyroid growth and function. We have examined the interaction of murine EGF (mEGF) with human and porcine thyroid membranes and compared this with the binding of bovine TSH (bTSH) using 125I-labelled hormones as tracers. The characteristics of the binding of mEGF were found to be similar for human and porcine thyroid membranes. Epidermal growth factor bound with high affinity (affinity constant = 1·4 × 109 l/mol); the density of binding sites was low compared with the TSH receptor. At 37 °C, the binding of 125I-labelled EGF was maximal at 1 h and was saturable in the presence of unlabelled EGF; half-maximal inhibition was at 1 ng EGF/tube (0·5 nmol/l) using 0·5 mg membrane protein/tube. Unlabelled bTSH had no effect on the binding of labelled EGF. Similarly, unlabelled EGF did not affect the binding of labelled TSH; hence it was concluded that mEGF and bTSH bound to independent sites. Epidermal growth factor had no effect on adenylate cyclase activity in membranes prepared from human non-toxic goitre; increasing concentrations of EGF did not affect basal, TSH-stimulated or fluoride-stimulated enzyme activity. J. Endocr. (1984) 102, 57–61

scholarly journals Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras

1993 ◽  
Vol 13 (1) ◽  
pp. 155-162
Author(s):  
R H Medema ◽  
A M de Vries-Smits ◽  
G C van der Zon ◽  
J A Maassen ◽  
J L Bos
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Guanine Nucleotide Exchange Factor ◽  
Nucleotide Binding ◽  
Guanine Nucleotide ◽  
Nucleotide Exchange ◽  
Exchange Factor ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor ◽  
Epidermal Growth

A number of growth factors, including insulin and epidermal growth factor (EGF), induce accumulation of the GTP-bound form of p21ras. This accumulation could be caused either by an increase in guanine nucleotide exchange on p21ras or by a decrease in the GTPase activity of p21ras. To investigate whether insulin and EGF affect nucleotide exchange on p21ras, we measured binding of [alpha-32P]GTP to p21ras in cells permeabilized with streptolysin O. For this purpose, we used a cell line which expressed elevated levels of p21 H-ras and which was highly responsive to insulin and EGF. Stimulation with insulin or EGF resulted in an increase in the rate of nucleotide binding to p21ras. To determine whether this increased binding rate is due to the activation of a guanine nucleotide exchange factor, we made use of the inhibitory properties of a dominant negative mutant of p21ras, p21ras (Asn-17). Activation of p21ras by insulin and EGF in intact cells was abolished in cells infected with a recombinant vaccinia virus expressing p21ras (Asn-17). In addition, the enhanced nucleotide binding to p21ras in response to insulin and EGF in permeabilized cells was blocked upon expression of p21ras (Asn-17). From these data, we conclude that the activation of a guanine nucleotide exchange factor is involved in insulin- and EGF-induced activation of p21ras.

Renal tubular cells are potential targets for epidermal growth factor

1988 ◽  
Vol 255 (6) ◽  
pp. F1191-F1196 ◽  
Author(s):  
P. R. Goodyer ◽  
Z. Kachra ◽  
C. Bell ◽  
R. Rozen
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Line ◽  
Binding Sites ◽  
Collecting Duct ◽  
Primary Cultures ◽  
Kidney Cortex ◽  
Tubular Cells ◽  
Renal Tubular Cells ◽  
Epidermal Growth

Epidermal growth factor (EGF) is a potent polypeptide mitogen with various receptor-mediated growth effects on cells from the skin, breast, and gastrointestinal tract. Recent studies indicate that EGF is produced in the kidney and is excreted in the urine, but the biological significance of renal EGF is uncertain. We demonstrate in vitro mitogenicity of EGF for LLC-PK1 cells, a tubular epithelial cell line derived from pig kidney cortex. Furthermore, when subconfluent monolayers of LLC-PK1 cells are exposed to EGF for 24 h, sodium-dependent phosphate transport is stimulated (209-410% of control). These cells possess EGF-specific high-affinity binding sites at their surface (Kd 300-700 pM) but cannot synthesize the growth factor. EGF binding sites are not a peculiarity of the LLC-PK1 cell line, since similar sites are present on MDCK cells (derived from dog kidney distal tubule or collecting duct), primary cultures of mouse proximal tubular cells, and freshly prepared membrane fractions from mouse kidney. Cortical basolateral membranes are highly enriched in EGF binding sites, whereas EGF binding by brush-border membrane fractions is minimal and is compatible with contamination.

Epidermal growth factor accelerates renal tissue repair in a model of gentamicin nephrotoxicity in rats

1992 ◽  
Vol 263 (5) ◽  
pp. F806-F811 ◽  
Author(s):  
N. J. Morin ◽  
G. Laurent ◽  
D. Nonclercq ◽  
G. Toubeau ◽  
J. A. Heuson-Stiennon ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Binding Sites ◽  
Renal Tissue ◽  
Sprague Dawley ◽  
Renal Tubular Cells ◽  
Sprague Dawley Rats ◽  
Epidermal Growth ◽  
Renal Tubular ◽  
Cessation Of Treatment

Epidermal growth factor (EGF) is a potent mitogen for renal tubular cells that possess specific high-affinity binding sites for this polypeptide. However, actual function of EGF within the kidney remains to be elucidated. We evaluated the effect of exogenous EGF administration on the rate of tubular regeneration in an experimental model of gentamicin (GT) nephrotoxicity. Female Sprague-Dawley rats were anesthetized, and a miniosmotic pump filled with mouse EGF or saline was implanted subcutaneously. Twenty-four hours later, GT (40 mg.kg-1 x 12 h-1 ip) was given for 4 and 8 days. Groups of treated animals and controls were killed either the day after cessation of treatment (days 5 and 9) or 4 and 8 days after the end of 8-day GT administration (days 12 and 16). Cortical GT levels of groups killed at days 5, 9, 12, and 16 were similar in animals infused with saline or EGF. Serum creatinine levels were significantly higher in GT-treated animals infused with EGF or saline and killed at days 9 and 12 compared with saline-treated animals infused with EGF or saline alone (P < 0.01). Blood urea nitrogen (BUN) also increased as a result of GT administration. However, in animals receiving GT and EGF and killed at day 16, mean BUN level was significantly lower (P < 0.01) compared with rats dosed with GT alone. In treated rats, the extent of tubular regeneration, evaluated by the rate of [3H]thymidine incorporation into renal cortical DNA or by the frequency of S-phase cells (histoautoradiography), was increased in a dose- and time-dependent fashion.(ABSTRACT TRUNCATED AT 250 WORDS)

Characterization and autoradiographic localization of the epidermal growth factor receptor in the jejunum of neonatal and weaned pigs

1992 ◽  
Vol 4 (2) ◽  
pp. 183 ◽  
Author(s):  
D Kelly ◽  
M McFadyen ◽  
TP King ◽  
PJ Morgan
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Binding Sites ◽  
Growth Factor Receptor ◽  
Saturation Curve ◽  
Egf Receptors ◽  
Weaned Pigs ◽  
Single Class ◽  
Epidermal Growth

Receptors for epidermal growth factor (EGF) were characterized on the intestinal membranes of newborn, sucking and weaned pigs. 125I-labelled EGF (125I-EGF) binding to membrane homogenates was time-dependent, saturable, linearly correlated to membrane protein and reversible. Analysis of saturation curve data revealed a single class of 125I-EGF binding sites in both newborn and weaned pigs. Receptor levels tended to be higher in weaned than in newborn pigs; the converse was true for the receptor affinity. In contrast, virtually no binding sites were found on the intestinal membranes of sucking pigs. Autoradiography in vitro of jejunal sections of newborn and weaned pigs demonstrated 125I-EGF receptors on both microvillar and basolateral surfaces of enterocytes, suggesting that luminal EGF could influence developmental processes in the intestine either directly or indirectly following transcytosis of the ligand.

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