Category: Growth factor.
PHARMACOLOGY: Pharmacodynamics: EGF is part of a complex network of growth factors and receptors that together help to moderate the growth of cells. EGF is released by cells, and then is pecked up either by the cell itself, stimulating its own growth, or by neighboring cells, stimulating their ability to divide. Receptors on the surface of the cell bind to EGF and relay the signal inside. When the receptor binds to EGF, it is activated by forming a dimer with other receptors.
EGF is essential for mediating the de-differentiation of keratinocytes to an epithelial linage and to reestablish the epithelial barrier. EGF binds to the EGFR, a protein tyrosine kinase receptor, expressed on the majority of cells in the skin. Activation of EGFR leads to a number of biological responses, including migration, proliferation, cytoprotection, cellular differentiation, and apoptosis. In wound healing EGFR plays an important role in re-epithelialization and dermal maturation. Topical use of recombinant human EGF has been shown to increase re-epithelialization and enhance wound healing.
Pharmacokinetics: Subjects were followed up for various periods of time to evaluate the systemic absorption of REGEN-D 150 in blood. Sera was analyzed for anti-EGF titers by Indirect ELISA method. The test serum absorbance was less than the seroconversion cut-off value, hence these samples were negative for anti r-human EGF antibody.
Patients with wounds were tested for the presence of rhEGF by collecting the samples from the site of application, the result clearly shows that rhEGF is available at the site of application. Protease enzyme present in the body degrades rhEGF at the site of application, however when REGEN-D 150 was applied, there was sufficient high concentration of rhEGF locally.
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