Comparative tissue distribution of the processing enzymes "prohormone thiol protease," and prohormone convertases 1 and 2, in human PTHrP-producing cell lines and mammalian neuroendocrine tissues.
- 1 January 2001
- journal article
- research article
- Published by Springer Nature in Endocrine
- Vol. 15 (2) , 217-224
- https://doi.org/10.1385/endo:15:2:217
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Evidence for Functional Localization of the Proenkephalin-Processing Enzyme, Prohormone Thiol Protease, to Secretory Vesicles of Chromaffin Cells*Endocrinology, 1999
- In Vitro Cleavage of Internally Quenched Fluorogenic Human Proparathyroid Hormone and Proparathyroid-related Peptide Substrates by FurinPublished by Elsevier ,1998
- The proprotein convertasesCurrent Opinion in Chemical Biology, 1998
- Incomplete Processing of Proinsulin to Insulin Accompanied by Elevation of Des-31,32 Proinsulin Intermediates in Islets of Mice Lacking Active PC2Journal of Biological Chemistry, 1998
- Purification and Characteristics of the Candidate Prohormone Processing Proteases PC2 and PC1/3 from Bovine Adrenal Medulla Chromaffin GranulesPublished by Elsevier ,1995
- Parathyroid hormone-related protein in the cardiovascular system.Endocrinology, 1994
- A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidaseBiochemical Journal, 1992
- Identification of the type 2 proinsulin processing endopeptidase as PC2, a member of the eukaryote subtilisin family.Journal of Biological Chemistry, 1992
- All Major Lung Cancer Cell Types Produce Parathyroid Hormone-Like Protein: Heterogeneity Assessed by High Performance Liquid Chromatography*Endocrinology, 1991
- Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles.Journal of Biological Chemistry, 1985