Mammalian bombesin-like peptides: neuromodulators of gastric function and autocrine regulators of lung cancer growth.

Peptides corresponding closely in structure to the biologically active carboxyl terminal region of the amphibian peptide bombesin have now been isolated from several mammalian species, including man. Two principal forms have been found: one contains 27 amino acids and exhibits variations in amino acid sequence in the amino terminal region; the other is the carboxyl terminal decapeptide and probably does not vary among mammals. These peptides exhibit full immunoreactivity with most bombesin antisera and account for "bombesin-like immunoreactivity" that has been described in mammalian brain, sympathetic ganglia, and nerve fibers in the gut as well as in fetal lung endocrine cells and certain lung tumors, especially small cell lung carcinoma. The name gastrin releasing peptide (GRP) was given to the porcine and avian heptacosapeptides by McDonald and Mutt. The larger and smaller mammalian peptides now often are called GRP27 and GRP10. Both forms exhibit the full spectrum of activity shown by bombesin. Evidence has been obtained that neural release of mammalian bombesin-like peptides is physiologically important in regulation of gastrin release from the stomach. Lung tumors that produce bombesin-like peptides also have receptors for bombesin. These receptors appear to be involved in the autocrine regulation of tumor cell proliferation.