Epidermal growth factor in gingival crevicular fluid and its binding capacity in inflamed and non-inflamed human gingiva

1996 ◽  
Vol 41 (7) ◽  
pp. 719-724 ◽  
Author(s):  
Kuang-Min Chang ◽  
Nina Lehrhaupt ◽  
Louis M. Lin ◽  
Jian Feng ◽  
Chi-Ying Wu-Wang ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Gingival Crevicular Fluid ◽  
Binding Capacity ◽  
Human Gingiva ◽  
Epidermal Growth ◽  
Crevicular Fluid

scholarly journals 125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts.

1976 ◽  
Vol 71 (1) ◽  
pp. 159-171 ◽  
Author(s):  
G Carpenter ◽  
S Cohen
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Energy Production ◽  
Binding Capacity ◽  
Human Fibroblasts ◽  
Metabolic Energy ◽  
Acid Extraction ◽  
Native Form ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth

125I-labeled human epidermal growth factor (hEGF) binds in a specific and saturable manner to human fibroblasts. At 37 degrees C, the cell-bound 125I-hEGF initially may be recovered in a native form by acid extraction; upon subsequent incubation, the cell-bound 125I-hEGF is degraded very rapidly, with the appearance in the medium of 125I-monoiodotyrosine. At 0 degrees C, cell-bound 125I-hEGF is not degraded but slowly dissociates from the cell. The data are consistent with a mechanism in which 125I-hEGF initially is bound to the cell surface and subsequently is internlized before degradation. The degradation is blocked by inhibitors of metabolic energy production (azide, cyanide, dinitrophenol), some protease inhibitors (Tos-Lys-CH2Cl, benzyl guanidobenzoate), a lysosomotropic agent (chloroquine) various local anesthetics (cocaine, lidocaine, procaine), and ammonium chloride. After the binding and degradation of 125I-hEGF the fibroblasts are no longer able to rebind fresh hormone. The binding capacity of these cells is restored by incubation in a serum-containing medium; this restoration is inhibited by cycloheximide or actinomycin D.

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.

High-Performance Liquid Chromatography of 125I-Labeled Mouse Epidermal Growth Factor Radioiodinated by Six Different Methods

1992 ◽  
Vol 38 (5) ◽  
pp. 681-686 ◽  
Author(s):  
C B Kienhuis ◽  
J J Heuvel ◽  
H A Ross ◽  
J A Foekens ◽  
T J Benraad
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
High Performance ◽  
Binding Capacity ◽  
Reversed Phase ◽  
Iodine Monochloride ◽  
Reversed Phase Hplc ◽  
Hplc Column ◽  
Epidermal Growth ◽  
Chloramine T

Abstract Six different procedures for radioiodination of mouse epidermal growth factor (EGF) all resulted in a heterogeneous 125I-labeled EGF preparation, as analyzed by reversed-phase HPLC. EGF preparations that had been iodinated with Chloramine T, lodogen, or lodo-beads were found mainly to consist of oxidized 125I-labeled EGF moieties. In contrast, the heterogeneous 125I-labeled EGF preparations obtained by using iodine monochloride, Protag-125, or lactoperoxidase-glucose oxidase-coupled beads (Enzymobeads) contained insignificant amounts of oxidized EGF entities. Ligand equivalence analysis (LEA) of distinct HPLC column fractions, obtained after preparative separation of Chloramine T-125I-labeled EGF, showed that the receptor-binding affinity of the tracer in all subfractions was less than the affinity of unlabeled EGF. This implies that HPLC purification of these 125I-labeled EGF preparations does not yield 125I-labeled EGF preparations with ligand equivalence. However, all but one HPLC column fraction of Enzymobeads-125I-labeled EGF showed ligand equivalence. Despite the small amount of the nonequivalent component in the Enzymobeads-labeled tracer, the nonchromatographed 125I-labeled EGF preparation showed ligand equivalence. No significant differences were observed in the maximal binding capacity of the different 125I-labeled EGF preparations.

scholarly journals Spatial Localization of m-Calpain to the Plasma Membrane by Phosphoinositide Biphosphate Binding during Epidermal Growth Factor Receptor-Mediated Activation

2006 ◽  
Vol 26 (14) ◽  
pp. 5481-5496 ◽  
Author(s):  
Hanshuang Shao ◽  
Jeff Chou ◽  
Catherine J. Baty ◽  
Nancy A. Burke ◽  
Simon C. Watkins ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phospholipase C ◽  
Cell Body ◽  
Wound Repair ◽  
Egf Receptor ◽  
Binding Capacity ◽  
Dependent Manner ◽  
Epidermal Growth

ABSTRACT Calpain activity is required for de-adhesion of the cell body and rear to enable productive locomotion of adherent cells during wound repair and tumor invasion. Growth factors activate m-calpain (calpain 2, CAPN2) via ERK/mitogen-activated protein kinases, but only when these kinases are localized to the plasma membrane. We thus hypothesized that m-calpain is activated by epidermal growth factor (EGF) only when it is juxtaposed to the plasma membrane secondary to specific docking. Osmotic disruption of NR6 fibroblasts expressing the EGF receptor demonstrated m-calpain being complexed with the substratum-adherent membrane with this increasing in an EGF-dependent manner. m-Calpain colocalized with phosphoinositide biphosphate (PIP2) with exogenous phospholipase C removal of phosphoinositides, specifically, PI(4,5)P2 but not PI(4)P1 or PIP3, releasing the bound m-calpain. Downregulation of phosphoinositide production by 1-butanol resulted in diminished PIP2 in the plasma membrane and eliminated EGF-induced calpain activation. This PIP2-binding capacity resided in domain III of calpain, which presents a putative C2-like domain. This active conformation of this domain appears to be partially masked in the holoenzyme as both activation of m-calpain by phosphorylation at serine 50 and expression of constitutively active phosphorylation mimic glutamic acid-increased m-calpain binding to the membrane, consistent with blockade of this cascade diminishing membrane association. Importantly, we found that m-calpain was enriched toward the rear of locomoting cells, which was more pronounced in the plasma membrane footprints; EGF further enhanced this enrichment, in line with earlier reports of loss of PIP2 in lamellipodia of motile cells. These data support a model of m-calpain binding to PIP2 concurrent with and likely to enable ERK activation and provides a mechanism by which cell de-adhesion is directed to the cell body and tail as phospholipase C-γ hydrolyzes PIP2 in the protruding lamellipodia.

scholarly journals Epidermal Growth Factor Is Associated with Loss of Mucosae Sealing and Peri-Implant Mucositis: A Pilot Study

Healthcare ◽  
2021 ◽  
Vol 9 (10) ◽  
pp. 1277
Author(s):  
José Jorge Schoichet ◽  
Carlos Fernando de Almeida Barros Mourão ◽  
Edgard de Mello Fonseca ◽  
Carlos Ramirez ◽  
Ricardo Villas-Boas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Detection System ◽  
Quantitative Polymerase Chain Reaction ◽  
Sample Collection ◽  
Egfr Gene ◽  
Epidermal Growth ◽  
Group 2 ◽  
Crevicular Fluid

This study aimed to evaluate the correlation between epidermal growth factor (EGF) and receptor (EGFR) levels in different clinical stages of dental implant rehabilitation and trace mucositis development’s biological profile. Thirty-six participants from the Specialization in Implant Dentistry, Universidade Federal Fluminense, Brazil, were included in the study and underwent sample collection: inside the alveolar socket, immediately before implant placement (Group 1, n = 10); at the peri-implant crevicular fluid (PICF) during reopening (Group 2, n = 10); PICF from healthy peri-implant in function (Group 3, n = 8); and PICF from mucositis sites (Group 4, n = 18). Quantitative polymerase chain reaction (PCR) evaluated EGF/EGFR gene expression using the SYBR Green Master Mix detection system. The results showed that EGF expression in the peri-implant crevicular fluid was statistically different. There was a higher EGF expression for group C (peri-implant health) (p = 0.04) than for the other groups. Regarding EGFR, there was no statistical difference among the groups (p = 0.56). It was concluded that low levels of EGF gene expression in the peri-implant crevicular fluid are related to the development of peri-implant mucositis and the absence of mucosae sealing. There was no correlation between EGFR gene expression with health or mucositis.

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