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• W2020180059 endingPage "1730" @default.
• W2020180059 startingPage "1726" @default.
• W2020180059 abstract "Transforming growth factor alpha (TGF-alpha) is generated by cleavage of a membrane-anchored precursor protein, proTGF-alpha. ProTGF-alpha is cleaved at a slow rate and accumulates on the cell surface, thereby mediating cell-cell adhesion and mitogenic stimulation. We show here that cleavage of membrane proTGF-alpha by an elastase-like enzyme constitutes an important regulatory step in the generation of soluble TGF-alpha. Cleavage is activated in response to serum factors and tumor-promoting phorbol esters, leading to depletion of cell surface proTGF-alpha, which disperses as soluble factor. Activation of proTGF-alpha cleavage is mediated by protein kinase C-dependent and -independent mechanisms. The results demonstrate the existence of mechanisms that control the switch of TGF-alpha from a juxtacrine to a paracrine growth factor." @default.
• W2020180059 created "2016-06-24" @default.
• W2020180059 creator A5054921200 @default.
• W2020180059 creator A5055628562 @default.
• W2020180059 date "1991-03-01" @default.
• W2020180059 modified "2023-10-18" @default.
• W2020180059 title "Cleavage of the membrane precursor for transforming growth factor alpha is a regulated process." @default.
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• W2020180059 doi "https://doi.org/10.1073/pnas.88.5.1726" @default.
• W2020180059 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/51097" @default.
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