Cell motility is induced by many growth factors acting through cognate receptors with intrinsic tyrosine kinase activity (RPTK). However, most of the links between receptor activation and the biophysical processes of cell motility remain undeciphered. We have focused on the mechanisms by which the E
Diminished epidermal growth factor binding by neurofibromatosis fibroblasts
β Scribed by Marvin Zelkowitz; Joseph Stambouly
- Publisher
- John Wiley and Sons
- Year
- 1980
- Tongue
- English
- Weight
- 402 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0364-5134
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β¦ Synopsis
Abstract
Neurofibromatosis (NF) is an autosomal dominant disease characterized by growth abnormalities of epithelial, mesothelial, and endothelial elements. We recently reported abnormal growth and morphology of NF fibroblasts in tissue culture. Because epidermal growth factor (EGF) is known to stimulate the growth of fibroblasts in tissue culture, we studied the binding of commercial iodine 125βlabeled EGF to ageβ and passageβmatched confluent NF (N = 6) and normal (N = 4) fibroblasts. Fibroblasts were maintained at 37Β°C for 2, 30, 60, 120, and 240 minutes in a medium in which the cells grow slowly (Dulbecco's Eagle medium) and one in which they grow normally (Ham's Fβ12 medium). Binding assays were done in both serumβfree media according to accepted procedures. The EGF binding did not differ in the two media, and pooled data are presented. These data demonstrate no significant differences in the early binding of EGF to normal and NF fibroblasts (4,682 Β± 1,092 versus 3,441 Β± 826 cpm/10^6^ cells; 20,000 cpm/ng; p > 0.15 at 30 minutes). At one hour, however, differences suggestive of abnormal EGF binding become apparent (12,495 Β± 1,989 versus 3,172 Β± 853 cpm/10^6^ cells; 20,000 cpm/ng; p < 0.0025). We conclude that there may be a membrane defect in NF which is reflected by diminished EGF binding.
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