Conversion of high molecular weight human epidermal growth factor (hEGF)/urogastrone (UG) to small molecular weight hEGF/UG by mouse EGF-associated arginine esterase.
Human epidermal growth factor (hEGF) has previously been isolated from urine and appears to be identical to beta-urogastrone (UG), an inhibitor of stimulated gastric acid secretion. A high molecular weight (HMW) form of hEGF/UG has recently been found in human urine which is fully immunoreactive but is less bioactive as measured by receptor binding activity. A specific arginine esterase, the EGF-binding protein from mouse submandibular glands, was capable of cleaving HMW-hEGF to yield a small molecular weight (SMW)-hEGF with full immunoreactivity and bioactivity, whereas trypsin produced a SMW-hEGF with much less bioactivity. SMW-hEGF produced by the arginine esterase appeared to be immunologically, biologically (both by receptor binding and mitogenic activity) and chromatographically similar to highly purified hEGF. These data suggest that HMW-hEGF may play a precursor role in the biosynthesis of hEGF/UG in man.
D000818:Animals; D001120:Arginine; D001667:Binding, Competitive; D004247:DNA / Q000096:biosynthesis; D004815:Epidermal Growth Factor / Q000378:metabolism* / Q000494:pharmacology; D004950:Esterases / Q000378:metabolism*; D005768:Gastrointestinal Hormones / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D005768:Gastrointestinal Hormones; D010455:Peptides; D004815:Epidermal Growth Factor; D004247:DNA; D001120:Arginine; D004950:Esterases; D014357:Trypsin