Epidermal growth factor treatment of A431 cells alters the binding capacity and electrophoretic mobility of the cytoskeletally associated epidermal growth factor receptor

Journal Article · Tue Jan 01 04:00:00 EST 1991 · Journal of Cellular Physiology; (USA)

DOI:https://doi.org/10.1002/jcp.1041460109· OSTI ID:6010581

Roy, L M; Gittinger, C K; Landreth, G E ^[1]

---

1. Medical Univ. of South Carolina, Charleston (USA)

Epidermal growth factor receptor interacts with structural elements of A431 cells and remains associated with the cytoskeleton following extraction with nonionic detergents. Extraction of cells with 0.15% Triton X-100 resulted in detection of only approximately 40% of the EGF binding sites on the cytoskeleton. If the cells were exposed to EGF prior to extraction, approximately twofold higher levels of low-affinity EGF binding sites were detected. The difference in number of EGF binding sites was not a consequence of differences in numbers of EGF receptors associated with the cytoskeleton; equal amounts of 35S-labeled receptor were immunoprecipitated from the cytoskeletons of both control and EGF-treated cells. The effect of EGF pretreatment on binding activity was coincident with a change in the mobility of the receptor from a doublet of Mr approximately 160-180 kDa to a single sharp band at 180 kDa. The alteration in receptor mobility was not a simple consequence of receptor phosphorylation in that the alteration was not reversed by alkaline phosphatase treatment, nor was the shift produced by treatment of the cells with phorbol ester. The two EGF receptor species demonstrated differential susceptibility to V8 proteinase digestion. The EGF-induced 180 kDa species was preferentially digested by the proteinase relative to the 160 kDa species, indicating that EGF binding results in a conformational change in the receptor. The EGF-mediated preservation of binding activity and altered conformation may be related to receptor oligomerization.

• OSTI ID: 6010581
• Journal Information: Journal of Cellular Physiology; (USA), Journal Name: Journal of Cellular Physiology; (USA) Vol. 146:1; ISSN 0021-9541; ISSN JCLLA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
560300 -- Chemicals Metabolism & Toxicology
59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ANIMAL CELLS
ANIMAL TISSUES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BODY
CARCINOGENS
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
ELECTROPHORESIS
ENZYMES
EPIDERMIS
EPITHELIUM
ESTERS
EVEN-ODD NUCLEI
GROWTH FACTORS
HYDROLASES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LIGHT NUCLEI
MEMBRANE PROTEINS
MITOGENS
NUCLEI
ORGANIC COMPOUNDS
ORGANS
PEPTIDE HYDROLASES
PHORBOL ESTERS
PHOSPHORYLATION
PROTEINS
RADIOISOTOPES
REACTION KINETICS
RECEPTORS
SKIN
SULFUR 35
SULFUR ISOTOPES
TISSUES
TRACER TECHNIQUES
TUMOR CELLS