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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Epidermal growth factor (EGF) receptor is expressed selectively by human melanoma cells which show the presence of an extra copy of chromosome 7. None of the cells of benign pigmented lesions (nevi) or radial growth phase (nonmetastatic) primary melanoma expressed EGF receptor and none of these cells showed an extra copy of chromosome 7. The results indicate that a single extra dose of a gene (for EGF receptor) may provide a selective advantage to cells in the late stages of tumorigenesis.
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PMID:Expression of the receptor for epidermal growth factor correlates with increased dosage of chromosome 7 in malignant melanoma. 298 38

We have tested the hypothesis that the mechanism of platelet-derived growth factor (PDGF) and phorbol diester action to decrease the apparent affinity of the epidermal growth factor (EGF) receptor is the phosphorylation of the EGF receptor at the Ca2+/phospholipid-dependent protein kinase (protein kinase C) phosphorylation site, threonine 654. Protein kinase C-deficient cells were prepared by prolonged incubation of human fibroblasts with phorbol diester. Addition of phorbol diesters to these cells fails to regulate EGF receptor affinity or threonine 654 phosphorylation. In contrast, PDGF treatment of both control and protein kinase C-deficient fibroblasts causes a decrease in the apparent affinity of the EGF receptor and an increase in threonine 654 phosphorylation. Thus, the ability of PDGF or phorbol diester to modulate EGF receptor affinity occurs only when threonine 654 phosphorylation is increased. The stoichiometry of threonine 654 phosphorylation associated with a 50% decrease in the binding of 125I-EGF to high affinity sites was 0.15 versus 0.3 mol of phosphate per mole of EGF receptor when 32P-labeled fibroblasts are treated with PDGF or phorbol diester, respectively. It is concluded that EGF receptor phosphorylation at threonine 654 can be regulated by PDGF independently of protein kinase C, substoichiometric phosphorylation of the total EGF receptor pool at threonine 654 is caused by maximally effective concentrations of PDGF, and different extents of phosphorylation of EGF receptors at threonine 654 are observed for maximally effective concentrations of PDGF and phorbol diester, respectively. The data are consistent with the hypothesis that a specific subpopulation of EGF receptors that exhibit high affinity for EGF are regulated by threonine 654 phosphorylation.
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PMID:Stimulation of epidermal growth factor receptor threonine 654 phosphorylation by platelet-derived growth factor in protein kinase C-deficient human fibroblasts. 310 61

Stimulation of epidermal growth factor (EGF) receptor by ligands such as transforming growth factor (TGF) alpha may be associated with cell proliferation or transformation in both nevocytes and keratinocytes. Previously, EGF receptors have been identified within a variety of pigmented lesions, suggesting a possible responsiveness to ligands such as TGF alpha. In the present study, we characterize the intralesional expression and distribution of immunoreactive TGF alpha protein by avidin-biotin immunoperoxidase localization in benign nevi, congenital nevi, dysplastic nevi, and malignant melanomas. In situ hybridization techniques with TGF alpha riboprobes confirmed the constitutive production of TGF alpha in all types of pigmented lesions. The localization of TGF alpha expression to nevocytes when coupled with the previous reports of expression in basal keratinocytes suggests the possibility of either an autocrine mechanism of action for TGF alpha or a paracrine interplay of TGF alpha between keratinocytes and nevocytes within melanocytic lesions. An increase in immunoreactive TGF alpha in nevocytes was noted in both benign and dysplastic nevi from dysplastic nevus patients, as compared to benign nevi from normal patients. Congenital nevi and malignant melanomas showed an intermediate and variable level of TGF alpha immunoreactivity. When coupled with previous studies the data suggest linkage of the TGF alpha/EGF receptor pathway in the evolution of melanocytic lesions.
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PMID:Expression and distribution of transforming growth factor-alpha within melanocytic lesions. 796 61

Dermatofibroma (DF) refers to a spectrum of firm, nodular, nonencapsulated lesions that occur commonly on the extremities. Histologically, DF is composed of spindle cells with variable differentiation toward histiocytic and vascular elements, often associated with epithelial hyperplasia and basilar keratinocyte pigmentation that histologically may simulate basal cell carcinoma (BCC). The characteristic epithelial changes are likely to be mesenchyma-mediated and probably represent a host reparative response otherwise known as the inductive phenomenon. Epidermal-mesenchymal cellular interactions, including induction, occur in various stages of embryonic skin development and in response to injury with tissue repair. Cellular interaction is mediated by direct apposition of cells or by soluble protein hormones produced directly by the cell (autocrine effect) or adjacent cells (paracrine effect). Among the important soluble mediators are epidermal growth factor (EGF), which is known to stimulate the proliferation and differentiation of a variety of transformed and benign tissues. We investigated the possible etiologic association between EGF receptor (EGF-R) expression and epithelial induction in a prospective series of 20 cases of DF compared to entities such as granular cell tumor, scar tissue, and nevus sebaceus similarly showing epithelial hyperplasia. Immunohistochemical staining for EGF-R showed strong dermal staining of dendritic spindle cells and overlying hyperplastic keratinocytes in each of the DF cases. Immunohistochemical staining for EGF-R was absent within all dermal loci of granular cell tumor (n = 3), nevus sebaceus (n = 6), and scar tissue (n = 12).
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PMID:Epithelial induction in dermatofibroma: a role for the epidermal growth factor (EGF) receptor. 905 52