Development of a cell-derived matrix: Effects of epidermal growth factor in chemically defined culture

2009 ◽  
Vol 9999A ◽  
pp. NA-NA ◽  
Author(s):  
Angela M. Throm ◽  
Wai-Ching Liu ◽  
Chi-Hung Lock ◽  
Kristen L. Billiar
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Matrix Effects ◽  
A Cell ◽  
Epidermal Growth ◽  
Defined Culture

A Conjugate of an Anti-Epidermal Growth Factor Receptor (EGFR) VHH and a Cell-Penetrating Peptide Drives Receptor Internalization and Blocks EGFR Activation

ChemBioChem ◽  
2017 ◽  
Vol 18 (24) ◽  
pp. 2390-2394 ◽  
Author(s):  
Sanne A. M. van Lith ◽  
Dirk van den Brand ◽  
Rike Wallbrecher ◽  
Sander M. J. van Duijnhoven ◽  
Roland Brock ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Receptor Internalization ◽  
Cell Penetrating Peptide ◽  
Egfr Activation ◽  
Cell Penetrating ◽  
A Cell ◽  
Epidermal Growth

scholarly journals Epidermal growth factor and renin in mouse submandibular glands.

1981 ◽  
Vol 29 (10) ◽  
pp. 1229-1231 ◽  
Author(s):  
T Tanaka ◽  
E W Gresik ◽  
T Barka
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Secretory Granules ◽  
Small Population ◽  
Thin Sections ◽  
Tubular Cells ◽  
Renin Gene ◽  
A Cell ◽  
Epidermal Growth ◽  
Convoluted Tubules

Epon sections of the submandibular gland of SWF/J male mouse were stained immunocytochemically for epidermal growth factor (EGF) and renin. Most cells of the granular convoluted tubules (GCT) contained both EGF and renin. However, examinations of adjacent semithin or thin sections stained for EGF and renin, respectively, revealed a small population of GCT cells that contained EGF but no renin. Within a cell all secretory granules contained both EGF and renin. The renin-negative/EGF-positive cells may represent a subpopulation of tubular cells that do not express, or carry, the renin gene.

Mechanism regulating nuclear calcium signalingThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell.

2006 ◽  
Vol 84 (3-4) ◽  
pp. 403-422 ◽  
Author(s):  
Anant N. Malviya ◽  
Christian Klein
Keyword(s):  
Endoplasmic Reticulum ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Signaling ◽  
Nuclear Membrane ◽  
Protein Fragment ◽  
Outer Nuclear Membrane ◽  
Nuclear Calcium ◽  
A Cell ◽  
Epidermal Growth

Although the outer nuclear membrane is continuous with the endoplasmic reticulum, it is possible to isolate nuclei both intact and free from endoplasmic reticulum contaminants. The outer and the inner nuclear membranes can be purified free from cross-contamination. Evidence in support of autonomous regulation of nuclear calcium signaling relies upon the investigations with isolated nuclei. Mechanisms for generating calcium signaling in the nucleus have been identified. Two calcium transporting systems, an ATP-dependant nuclear Ca2+-ATPase and an IP4-mediated inositol 1,3,4,5-tetrakisphosphate receptor, are located on the outer nuclear membrane. Thus, ATP and IP4, depending on external free calcium concentrations, are responsible for filling the nuclear envelope calcium pool. The inositol 1,4,5-trisphosphate receptor is located on the inner nuclear membrane with its ligand binding domain facing toward the nucleoplasm. Likewise, the ryanodine receptor is located on the inner nuclear membrane and its ligand cADP-ribose is generated within the nucleus. A 120 kDa protein fragment of nuclear PLC-γ1 is stimulated in vivo by epidermal growth factor nuclear signaling coincident with the time course of nuclear membrane epidermal growth factor receptor activation. Stimulated 120 kDa protein fragment interacts with PIKE, a nuclear GTPase, and together they form a complex with PI[3]kinase serving as a module for nuclear PI[3]K stimulation. Thus, the nucleus has its own IP3 generating system.

Targeting human epidermal growth factor receptor 2 by a cell-penetrating peptide–affibody bioconjugate

Biomaterials ◽  
2012 ◽  
Vol 33 (8) ◽  
pp. 2570-2582 ◽  
Author(s):  
Srinath Govindarajan ◽  
Jeyarajan Sivakumar ◽  
Prathyusha Garimidi ◽  
Nandini Rangaraj ◽  
Jerald M. Kumar ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Cell Penetrating Peptide ◽  
Human Epidermal Growth Factor ◽  
Cell Penetrating ◽  
A Cell ◽  
Epidermal Growth

scholarly journals A rapid decrease in epidermal growth factor-binding capacity accompanies the terminal differentiation of mouse myoblasts in vitro.

1984 ◽  
Vol 98 (2) ◽  
pp. 739-747 ◽  
Author(s):  
R W Lim ◽  
S D Hauschka
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Binding Capacity ◽  
Growth Factor Receptor ◽  
Terminal Differentiation ◽  
Growth Stimulation ◽  
Cycle Arrest ◽  
A Cell ◽  
Epidermal Growth

Specific mitogens stimulate the proliferation and repress the differentiation of mouse myoblasts (MM14). When mitogens are depleted, MM14 cells cease proliferation, commit to terminal differentiation, and become refractory to growth stimulation. The behavior of mitogen receptors during the transition from a proliferative to a permanently postmitotic state was examined using the epidermal growth factor receptor (EGFR) as a model system. Whereas proliferating myoblasts bound substantial amounts of EGF, their binding capacity declined rapidly upon exposure to low-mitogen medium. The decline became irreversible when a cell differentiated. Within 24 h, less than 5% of the original EGF binding capacity remained. Since the ability to internalize and degrade bound EGF was unaffected, the change presumably reflected a decrease in EGFR availability. Several observations indicated that loss of EGFR following mitogen removal is related to differentiation rather than the result of starvation or cell-cycle arrest. First, the decline is correlated with the absence of a single mitogen (fibroblast growth factor) and is independent of serum concentrations. Second, myoblasts that are either cycling through G1 or arrested at G0, but prevented from differentiating, all bind large amounts of EGF. These findings suggest that specific reduction in mitogen receptors could be part of a mechanism whereby terminally differentiating cells become refractory to mitogenic stimulation.

scholarly journals Epidermal growth factor induces phosphorylation of extracellular signal-regulated kinase 2 via multiple pathways.

1993 ◽  
Vol 13 (12) ◽  
pp. 7248-7256 ◽  
Author(s):  
B M Burgering ◽  
A M de Vries-Smits ◽  
R H Medema ◽  
P C van Weeren ◽  
L G Tertoolen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Influx ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Alternative Pathways ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
A Cell ◽  
Epidermal Growth

Expression of p21rasAsn-17, a dominant negative mutant of p21ras that blocks p21ras activation by growth factors, inhibits activation of extracellular signal-regulated kinase 2 (ERK2) by insulin and platelet-derived growth factor in rat-1 cells [A. M. M. de Vries-Smits, B. M. T. Burgering, S. J. Leevers, C. J. Marshall, and J. L. Bos, Nature (London) 357:602-604, 1992]. Here we report that expression of p21rasAsn-17 does not abolish epidermal growth factor (EGF)-induced phosphorylation of ERK2 in fibroblasts. Since EGF activates p21ras in these cells, this indicates that EGF induces a p21ras-independent pathway for the phosphorylation of ERK2 as well. We investigated whether activation of protein kinase C (PKC) or increase in intracellular calcium could be involved in p21ras-independent signaling. In rat-1 cells, inhibition of either PKC, by prolonged 12-O-tetradecanoylphorbol-13-acetate (TPA) pretreatment, or calcium influx, by ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) pretreatment, did not abolish EGF-induced ERK2 phosphorylation. However, a combined inhibition of both p21ras and calcium influx, but not PKC, resulted in a complete inhibition of EGF-induced ERK2 phosphorylation. In contrast, in Swiss 3T3 cells, inhibition of both p21ras activation and TPA-sensitive PKC, but not calcium influx, inhibited EGF-induced ERK2 phosphorylation. These results demonstrate that in fibroblasts, EGF induces alternative pathways of ERK2 phosphorylation in a cell-type-specific manner.

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