title: Neo-kyotorphin, an analgesic peptide isolated from human lung carcinoma.
abstract: A pentapeptide with analgesic activity has been isolated from human lung squamous cell carcinoma and from three other types of propagated tumors of human lung small-cell carcinoma (SCC), adenoma (AD) and large-cell carcinoma (LCC) in nude mice. The amino acid sequence of the peptide has been revealed to be H-Thr-Ser-Lys-Tyr-Arg-OH, which is exactly the same as that of neo-kyotorphin, an analgesic peptide originally isolated from bovine brain [(1982) Life Sci. 31, 1733]. No neo-kyotorphin could be isolated from normal lung tissue using the same procedures as those used for carcinomas. The results suggest that the presence of neo-kyotorphin in the lung carcinoma may represent the ectopic expression of peptide hormone. Our findings constitute the first example of a human lung carcinoma producing analgesic peptide.
mesh_terms: D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004723:Endorphins / Q000138:chemical synthesis / Q000302:isolation & purification*; D006801:Humans; D008175:Lung Neoplasms / Q000032:analysis*; D013058:Mass Spectrometry; D009363:Neoplasm Proteins / Q000302:isolation & purification*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000302:isolation & purification
chemical_list: D004723:Endorphins; D009363:Neoplasm Proteins; D009842:Oligopeptides; C036450:neo-kyotorphin