NDLI: Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor

Content Provider	PubMed Central
Author	Swindle, C. Scott Tran, Kien T. Johnson, Terry D. Banerjee, Pallab Mayes, Anne M. Griffith, Linda Wells, Alan
Abstract	Signaling through growth factor receptors controls such diverse cell functions as proliferation, migration, and differentiation. A critical question has been how the activation of these receptors is regulated. Most, if not all, of the known ligands for these receptors are soluble factors. However, as matrix components are highly tissue-specific and change during development and pathology, it has been suggested that select growth factor receptors might be stimulated by binding to matrix components. Herein, we describe a new class of ligand for the epidermal growth factor (EGF) receptor (EGFR) found within the EGF-like repeats of tenascin-C, an antiadhesive matrix component present during organogenesis, development, and wound repair. Select EGF-like repeats of tenascin-C elicited mitogenesis and EGFR autophosphorylation in an EGFR-dependent manner. Micromolar concentrations of EGF-like repeats induced EGFR autophosphorylation and activated extracellular signal–regulated, mitogen-activated protein kinase to levels comparable to those induced by subsaturating levels of known EGFR ligands. EGFR-dependent adhesion was noted when the ligands were tethered to inert beads, simulating the physiologically relevant presentation of tenascin-C as hexabrachion, and suggesting an increase in avidity similar to that seen for integrin ligands upon surface binding. Specific binding to EGFR was further established by immunofluorescence detection of EGF-like repeats bound to cells and cross-linking of EGFR with the repeats. Both of these interactions were abolished upon competition by EGF and enhanced by dimerization of the EGF-like repeat. Such low affinity behavior would be expected for a matrix-“tethered” ligand; i.e., a ligand which acts from the matrix, presented continuously to cell surface EGF receptors, because it can neither diffuse away nor be internalized and degraded. These data identify a new class of “insoluble” growth factor ligands and a novel mode of activation for growth factor receptors.
Related Links	http://dx.doi.org/10.1083/jcb.200103103
Starting Page	459
File Format	PDF
ISSN	15408140
e-ISSN	15408140
Journal	The Journal of Cell Biology
Issue Number	2
Volume Number	154
Language	English
Publisher	The Rockefeller University Press
Publisher Date	2001-07-23
Access Restriction	Open
Rights Holder	The Rockefeller University Press
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine

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Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor

Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor

Melanoma cell invasiveness is promoted at least in part by the Epidermal Growth Factor-like repeats of Tenascin-C

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Melanoma cell invasiveness is promoted at least in part by the Epidermal Growth Factor-like repeats of Tenascin-C

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Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor

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