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: Z Tao, C Sakurada, H Yokosawa
• Journal: Neuropeptides (Neuropeptides) Vol. 20 Issue 2 Pg. 125-31 (Oct 1991) ISSN: 0143-4179 [Print] Netherlands
• PMID: 1798438 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Peptide Fragments
• Sulfhydryl Compounds
• Gonadotropin-Releasing Hormone
• Captopril
• Metalloendopeptidases

Topics

• Amino Acid Sequence
• Animals
• Captopril (pharmacology)
• Cell Membrane (enzymology)
• Chromatography, High Pressure Liquid
• Glioma (enzymology)
• Gonadotropin-Releasing Hormone (metabolism)
• Metalloendopeptidases (antagonists & inhibitors, chemistry, metabolism)
• Molecular Sequence Data
• Molecular Weight
• Peptide Fragments (chemistry, metabolism)
• Rats
• Sulfhydryl Compounds (pharmacology)
• Tumor Cells, Cultured