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EGF is internalized and degraded

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When the pair steeped human fibroblasts in EGF tagged with radioactive iodine, they found that the amount of radioactivity affixed to the cell's surface peaked after ∼30 to 40 min, and then plummeted (Carpenter and Cohen, 1976)... That finding provided strong circumstantial evidence that after EGF binds to a receptor, cells take in the hormone, chop it up, and eject the fragments... To bolster that conclusion, the team added antibodies that target EGF to a solution of cells bathed in the hormone... When they combined EGF-laden cells with chloroquine, which hinders the organelle's protein-slicing enzymes, the breakdown of EGF slowed. “The key experiment was showing that lysosomal inhibitors prevented degradation [of the hormone],” says Carpenter... The team determined that cells required 10 h to regain their full EGF-binding capacity... But the recovery stagnated if the researchers mixed in molecules that inhibit protein or RNA synthesis... Further work showed that cells absorbed and processed more than just protein hormones... For example, research led by Nobel laureates Michael Brown and Joseph Goldstein demonstrated that cells also engulf low-density lipoproteins and recycle the receptors (Anderson et al., 1976, 1977, 1982)... And multiple studies in recent years have emphasized that a lot of signaling occurs even after uptake of receptors into cells.

No MeSH data available.


Labeled EGF binds to cells but is then taken up and degraded.CARPENTER
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uro1: Labeled EGF binds to cells but is then taken up and degraded.CARPENTER


EGF is internalized and degraded
Labeled EGF binds to cells but is then taken up and degraded.CARPENTER
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2254875&req=5

uro1: Labeled EGF binds to cells but is then taken up and degraded.CARPENTER

View Article: PubMed Central

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

When the pair steeped human fibroblasts in EGF tagged with radioactive iodine, they found that the amount of radioactivity affixed to the cell's surface peaked after ∼30 to 40 min, and then plummeted (Carpenter and Cohen, 1976)... That finding provided strong circumstantial evidence that after EGF binds to a receptor, cells take in the hormone, chop it up, and eject the fragments... To bolster that conclusion, the team added antibodies that target EGF to a solution of cells bathed in the hormone... When they combined EGF-laden cells with chloroquine, which hinders the organelle's protein-slicing enzymes, the breakdown of EGF slowed. “The key experiment was showing that lysosomal inhibitors prevented degradation [of the hormone],” says Carpenter... The team determined that cells required 10 h to regain their full EGF-binding capacity... But the recovery stagnated if the researchers mixed in molecules that inhibit protein or RNA synthesis... Further work showed that cells absorbed and processed more than just protein hormones... For example, research led by Nobel laureates Michael Brown and Joseph Goldstein demonstrated that cells also engulf low-density lipoproteins and recycle the receptors (Anderson et al., 1976, 1977, 1982)... And multiple studies in recent years have emphasized that a lot of signaling occurs even after uptake of receptors into cells.

No MeSH data available.