ABSTRACT
The biological effects of epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha) are mediated by an interaction with a specific cell surface receptor having both intra- and extracellular domains. The structure of the intracellular domain can be closely aligned with retroviral protein tyrosine kinases. Upon ligand-binding there is a change in conformation of the extracellular domain, the receptor being converted to dimeric. Dimeric receptor has a higher rate of catalysis than monomeric and rapidly becomes phosphorylated. This form of the receptor now associates with and phosphorylates enzymes such as phospholipase-C, altering their catalytic activity and subcellular distribution This system appears to stimulate the effects of epidermal growth factor receptor(EGFr) activation, notably proliferation, morphology, paracrine effects and differentation.
Subject(s)
ErbB Receptors/physiology , Animals , Cell Division/physiology , ErbB Receptors/chemistry , Humans , Protein Structure, Tertiary , Signal Transduction/physiologyABSTRACT
Following delivery, our patient presented acutely with a painful swelling in the groin. Diagnosis could only be established by exploration. Thrombosed veins of the round ligament were found on histology of the swelling. Exploration was necessary to rule out an acute inguinal hernia.
