title: Evidence for thiol-dependent metallo-endopeptidase involved in degradation of luteinizing hormone-releasing hormone in glioma cells.
abstract: An endopeptidase generating a peptide comprised of the first five amino acids of luteinizing hormone-releasing hormone (LHRH) was isolated form the membranes of glioma C6 cells by a procedure including Brij extraction, p-mercuribenzoate-Sepharose chromatography, and Mono Q high-performance liquid chromatography. The molecular weight of the enzyme was estimated to be 64,000. The glial enzyme shows a similar inhibitor susceptibility to that of the enzyme of neuronal origin, and also to that of endopeptidase-24.15 (EC 3.4.24.15). Angiotensin-converting enzyme (EC 3.4.15.11) is suggested to be involved in the secondary cleavage of LHRH by the glioma cells.
authors.affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
authors.forename: Z
authors.initials: Z
authors.lastname: Tao
authors.forename: C
authors.initials: C
authors.lastname: Sakurada
authors.forename: H
authors.initials: H
authors.lastname: Yokosawa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002216:Captopril / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D005910:Glioma / Q000201:enzymology*; D007987:Gonadotropin-Releasing Hormone / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D051381:Rats; D013438:Sulfhydryl Compounds / Q000494:pharmacology*; D014407:Tumor Cells, Cultured
chemical_list: D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D007987:Gonadotropin-Releasing Hormone; D002216:Captopril; D008666:Metalloendopeptidases