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• W2132917966 abstract "Proteolysis of the GHR (growth hormone receptor) occurs at the cell surface and results in the release of its extracellular domain, the GHBP (growth hormone-binding protein). TACE (tumour necrosis factor-alpha-converting enzyme) has been identified as a putative protease responsible for GHR cleavage. However, GHR-TACE interaction has not been observed until now. Here, we identified TACE in Chinese hamster cells and confirmed processing and cell-surface expression. Interaction between GHR and TACE was only observed after growth hormone binding. As the growth hormone-GHR(2) complex is a poor substrate for TACE, we conclude that the GHR-TACE interaction precedes proteolysis, and is transient. Furthermore, we demonstrate that TACE is present in endosomes, where it partly co-localizes with endocytosed growth hormone ligand." @default.
• W2132917966 created "2016-06-24" @default.
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• W2132917966 date "2004-01-15" @default.
• W2132917966 modified "2023-10-14" @default.
• W2132917966 title "The growth hormone receptor interacts with its sheddase, the tumour necrosis factor-alpha-converting enzyme (TACE)" @default.
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• W2132917966 doi "https://doi.org/10.1042/bj20031321" @default.
• W2132917966 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1223864" @default.
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