Characterization of epidermal growth factor receptors on plasma membranes isolated from rat gastric mucosa.
The binding of human epidermal growth factor (hEGF), beta-urogastrone, to plasma membranes isolated from rat gastric mucosa was studied to characterize gastric EGF receptors. The binding of [125I]hEGF was temperature dependent, reversible, and saturable. A single class of binding sites for EGF with a dissociation constant of 0.42 nM and maximal binding capacity of 42 fmol/mg protein was suggested. There was little change in the binding of [125I]hEGF upon addition of peptide hormones (secretin, insulin), antiulcer drugs (cimetidine), or an ulcer-inducing reagent (aspirin). Cross-linking of [125I]hEGF to gastric plasma membranes with the use of disuccinimidyl suberate resulted in the labeling of a protein of 150 kDa. These results indicate the presence of EGF receptors on plasma membranes of rat gastric mucosa.
Department of Pharmacy, Kyoto University Hospital, Faculty of Medicine, Japan.
R
R
Hori
H
H
Nomura
S
S
Iwakawa
K
K
Okumura
D000818:Animals; D002462:Cell Membrane / Q000032:analysis / Q000378:metabolism*; D002927:Cimetidine / Q000494:pharmacology; D003432:Cross-Linking Reagents; D004285:Dogs; D004815:Epidermal Growth Factor / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D066246:ErbB Receptors / Q000032:analysis / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D005753:Gastric Mucosa / Q000032:analysis / Q000378:metabolism*; D006207:Half-Life; D006801:Humans; D066298:In Vitro Techniques; D007328:Insulin / Q000494:pharmacology; D007457:Iodine Radioisotopes; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D012633:Secretin / Q000494:pharmacology
D003432:Cross-Linking Reagents; D007328:Insulin; D007457:Iodine Radioisotopes; D011994:Recombinant Proteins; D012633:Secretin; D004815:Epidermal Growth Factor; D002927:Cimetidine; D066246:ErbB Receptors