[Dependence of epidermal growth factor activation on its affinity and oligomerization].
Epidermal growth factor receptor (EGF-R) oligomerization has been followed on A-431 cells using covalent labeling by 125I-EGF and EGF-dependent autophosphorylation of receptor-kinase. High molecular weight complexes corresponding to monomeric, dimeric, and trimeric forms of EGF-R are detected. The process of oligomerization occurs effectively at 37 degrees C while at 4 degrees C no oligomer formation is detected. PMA or ATP treatment reduces the number of high-affinity EGF-binding sites but has no influence on dimer formation. Dimerisation of the EGF-R in the absence of the ligand has been established on formalin-fixed A-431 cells.
Ivashchenko
Iu D
IuD
Kulik
G A
GA
Fil'chenkov
A A
AA
D000255:Adenosine Triphosphate / Q000494:pharmacology; D001665:Binding Sites; D002460:Cell Line; D003470:Culture Media; D004586:Electrophoresis; D004789:Enzyme Activation; D066246:ErbB Receptors / Q000378:metabolism; D006801:Humans; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000096:biosynthesis
D003470:Culture Media; D000255:Adenosine Triphosphate; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases