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

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

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...

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Cell cycle variation in 125I-labeled epidermal growth factor binding in chemically transformed cells.

Previous studies have shown that the nontransformed AKR-2B cells when arrested in the G1 phase of the cell cycle due to low-molecule-weight nutrient (amino acid) deficiency exhibit a 5- to 10-fold lower level of epidermal growth factor (EGF) receptor activity than do the same cells in the rapidly growing state or arrested in G1 due to growth factor deficiency. The chemically transformed AKR-MCA...

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Down regulation of epidermal growth factor receptors: direct demonstration of receptor degradation in human fibroblasts

The metabolism of the receptor for epidermal growth factor (EGF) has been measured by labeling the receptor in vivo with radioactive amino acid precursors and then determining, by immunoprecipitation with specific anti-EGF receptor antisera, the rate of degradation of the receptor when the cells are placed in a nonradioactive medium. In human fibroblasts the rate of EGF receptor degradation (t1...

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Quantitative electron microscopic autoradiographic studies on internalization of 125I-labelled epidermal growth factor in term human placenta.

The electron microscopic autoradiographic studies described here revealed the presence of specific silver grains over nuclei, lysosomal vesicles, rough endoplasmic reticulum and Golgi apparatus after incubation of placental tissue for 2 h at 38 degrees C with 1 nM-[125I]EGF. Three-step mask analysis, which corrects for radiation spread, showed that the relative grain density was the highest in ...

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Binding, internalization, and lysosomal association of 125I-human growth hormone in cultured human lymphocytes: a quantitative morphological and biochemical study

125I-human growth hormone (125I-hGH) binds specifically to receptors on cultures human lymphocytes (IM-9). When this process is studied by use of quantitative EM radioautography, under conditions of incubation at 15 degrees C for 5 min, the ligand is localized to the plasma membrane of the cell. At 30 degrees and 37 degrees C, however, 125I-hGH is progressively internalized by the cell as a fun...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 1976

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.71.1.159