scholarly journals Transmembrane delivery of polypeptide growth factors bypassing the intrinsic cell surface receptors: Synthesis and biological activity of a conjugate of epidermal growth factor with .ALPHA.2-macroglobulin.

1984 ◽  
Vol 9 (2) ◽  
pp. 105-115 ◽  
Author(s):  
Fumiaki Ito ◽  
Sachiko Ito ◽  
Nobuyoshi Shimizu
Keyword(s):  
Biological Activity ◽  
Growth Factors ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Polypeptide Growth Factors ◽  
Epidermal Growth ◽  
Transmembrane Delivery

scholarly journals The Na+/H+ Exchanger Regulatory Factor Stabilizes Epidermal Growth Factor Receptors at the Cell Surface

2004 ◽  
Vol 15 (12) ◽  
pp. 5470-5480 ◽  
Author(s):  
Cheri S. Lazar ◽  
Catherine M. Cresson ◽  
Douglas A. Lauffenburger ◽  
Gordon N. Gill
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Growth Factor Receptors ◽  
Cell Surface Receptors ◽  
Epidermal Growth Factor Receptors ◽  
Regulatory Factor ◽  
Down Regulation ◽  
Surface Receptors ◽  
Epidermal Growth

Ligand binding to cell surface receptors initiates both signal transduction and endocytosis. Although signaling may continue within the endocytic compartment, down-regulation is the major mechanism that controls the concentration of cell surface receptors, their ability to receive environmental signals, and the ultimate strength of biological signaling. Internalization, recycling, and trafficking of receptor tyrosine kinases (RTKs) within the endosome compartment are each regulated to control the overall process of down-regulation. We have identified the Na+/H+ exchanger regulatory factor (NHERF) as an important molecular component that stabilizes epidermal growth factor receptors (EGFRs) at the cell surface to restrict receptor down-regulation. The NH2-terminal PDZ domain (PDZ 1) of NHERF specifically binds to an internal peptide motif located within the COOH-terminal regulatory domain of EGFR. Expression of NHERF slows the rate of EGF-induced receptor degradation. A point mutation that abolishes the PDZ 1 recognition sequence of EGFR enhances the rate of ligand-induced endocytosis and down-regulation of EGFR. Similarly, expression of a dominant negative mutant of NHERF enhances EGF-induced receptor down-regulation. In contrast to β-adrenergic receptors where NHERF enhances recycling of internalized receptors, NHERF stabilizes EGFR at the cell surface and slows the rate of endocytosis without affecting recycling. Although the mechanisms differ, for both RTKs and G protein-coupled receptors, the overall effect of NHERF is to enhance the fraction of receptors present at the cell surface.

Thrombin and epidermal growth factor become linked to cell surface receptors during mitogenic stimulation

Nature ◽  
1979 ◽  
Vol 278 (5706) ◽  
pp. 743-745 ◽  
Author(s):  
JOFFRE B. BAKER ◽  
ROBERT L. SIMMER ◽  
KEVIN C. GLENN ◽  
DENNIS D. CUNNINGHAM
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Cell Surface Receptors ◽  
Mitogenic Stimulation ◽  
Surface Receptors ◽  
Epidermal Growth

Effects of growth hormone on rat renal epidermal growth factor expression

1994 ◽  
Vol 267 (2) ◽  
pp. F208-F214 ◽  
Author(s):  
S. A. Rogers ◽  
J. Rasmussen ◽  
S. B. Miller ◽  
M. R. Hammerman
Keyword(s):  
Growth Hormone ◽  
Growth Factors ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Polypeptide Growth Factors ◽  
Factor Expression ◽  
Igf I ◽  
Hypophysectomized Rats ◽  
Epidermal Growth ◽  
Growth Factor Expression

The kidney is a site of synthesis for several polypeptide growth factors including epidermal growth factor (EGF) and insulin-like growth factor I (IGF-I). Interactions between growth hormone (GH) and growth factors have been described that regulate renal growth factor expression. For example, GH and EGF each enhances the expression of IGF-I in kidney. To further define interrelationships in this renal GH-growth factor axis, we characterized the effect of GH on renal EGF expression in hypophysectomized, pituitary-intact (normal) rats, and hypersomatotropic rats. Levels of extractable immunoreactive mature EGF, levels of a 142-kDa EGF-precursor present in renal membrane fractions, and levels of EGF mRNA were significantly reduced in kidneys from hypophysectomized rats compared with levels in normal rats. Each was increased significantly after the administration of GH to hypophysectomized rats. In contrast, induction of hypersomatotropism in normal rats by injection of GH for 17 days did not affect levels of extractable mature EGF or EGF mRNA measured in kidneys. We conclude that GH enhances the renal synthesis of EGF in hypopituitary, but not in hypersomatotropic states.

Sign in / Sign up

Export Citation Format

Share Document