EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF

Article Abstract:

It has been established that metalloproteinase-dependent cleavage of proHB-epidermal growth factor (EGF) is quickly induced upon activation of G-protein-coupled receptors (GPCR). This process seems to play a critical and general part in EGF receptor (EGFR) transactivation. The HB-EGF precursor and metalloproteinase activity were identified as critical pathway elements between GPCR signals and activation of the EGFR. This research has given a new insight into the significance of membrane-associated proteinases as targets for disease intervention strategies.

Proteins, Cell receptors

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Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors

Article Abstract:

Stimulation of Rat-1 fibroblasts with the G-protein-coupled receptor (GPCR) antagonists results in tyrosine-phosphorylation of epidermal growth factor receptor (EFGR), indicating an intracellular mechanism for transactivation. The suppression of EGFR activity inhibits mitogen activated protein kinase, fos gene expression and DNA synthesis. Receptor tyrosine kinases (RTKs) appear to mediate GPCR-dependent mitogenic signaling. The activation of RTK is ligand-independent and occurs through intracellular signal crosstalk.

Research, Observations, Gene expression, Protein kinases

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A family of proteins that inhibit signalling through tyrosine kinase receptors

Article Abstract:

A new gene family designated as the signal-regulatory proteins (SIRPs) were produced by means of peptide sequencing and complementary DNA cloning. They consists of two subtypes which can be identified by the absence or the presence of a cytoplasmic SHP-2 binding domain. Results revealed that proteins which are members of the SIRP family regulate signals involved in different normal or abnormal processes

Analysis, Protein tyrosine kinase, Protein-tyrosine kinase

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