Parathyroid hormone-degrading enzyme of high molecular weight in the cytosol of rat renal cortical cells
Abstract
Using unlabeled bovine parathyroid hormone (b-PTH) as the substrate, the PTH-degrading activity in the 100,000 x g supernatant of rat renal cortex was examined. The PTH-degrading activity showed the highest peak at pH 7.25, along with 3 minor peaks at pH 4.5, 6.0 and 8.5. The neutral PTH-degrading activity of the 100,000 x g supernatant (pH 7.25) was eluted at V0 in Sephadex G-200 gel filtration corresponding to a high molecular weight. The neutral PTH-degrading activity was inhibited by ATP and calcium, but the acid PTH-degrading activity (pH 4.5) was slightly activated by ATP and was uninfluenced by calcium. The cytosolic neutral PTH-degrading activity was not inhibited by PMSF, trypsin inhibitor, E-64, chymostatin, leupeptin or pepstatin, whereas the acid PTH-degrading activity was inhibited by pepstatin, leupeptin, trypsin inhibitor and chymostatin. The neutral and acid PTH-degrading activities most probably depend on different enzymes. The neutral PTH-degrading enzyme is unlike any of the PTH-degrading enzymes so far reported.
Read the paper
Related studies
- Development of a crushable foam model for human trabecular bone
- Data-driven motion compensation in HR-pQCT.
- Modeling of structure, quality, and function in the orthodontic patient
- Exploring the mechanism of Heidihuang Pill in the treatment of osteoporosis based on network pharmacology, molecular docking, and experimental validation
- Effect of fabric on the accuracy of computed tomography-based finite element analyses of the vertebra
- Use of interventions involving virtual reality tasks during the climacteric: a systematic review
Go deeper in Evidence Hub
Evidence Hub adds a study data sheet (design, sample size, evidence level, key numbers), an AI summary and a chat grounded in the paper's text.