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Binding and processing of (125)I-ACTH by isolated rat splenic lymphocytes.

作者信息

Clarke B L

机构信息

School of Medicine, University of Minnesota at Duluth, 10 University Drive, Duluth, Minnesota 55812, USA.

出版信息

Biochem Biophys Res Commun. 1999 Dec 20;266(2):542-6. doi: 10.1006/bbrc.1999.1848.

DOI:10.1006/bbrc.1999.1848
PMID:10600537
Abstract

The effect of incubation temperature and ligand competition was tested for (125)I-ACTH binding to isolated rat lymphocytes. AlphaMSH but not Agouti-like peptide was an effective competitive inhibitor for cell surface binding at 4 degrees C. Cells incubated with (125)I-ACTH at 37 degrees C rapidly associated ligand for 10 min and then gradually lost the radioactivity with time. Cells incubated with (125)I-ACTH at 4 degrees C accumulated ligand to only about half the maximal amount when compared to cells incubated at 37 degrees C for 10 min. Temperatures below 20 degrees C and toxins that block lysosomal degradation blocked the loss of cell-associated radioactivity. These results suggest the lymphocyte ACTH receptor is the Melanocortin 5 receptor and the receptor is internalized by endocytosis to deliver ligand to the lysosome.

摘要

相似文献

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