Hormone binding and catecholamine secretion studies on PC12 cells
[摘要] Specific binding sites for atrial natriuretic peptide (ANP) secreted from the heart of several species have been identified in cultured PC12 phaeochromocytoma cells, a cell line derived from a tumour of the rat adrenal medulla. The 125I-labelled ANP bound specifically to PC 12 cells with a dissociation constant (Kd) of 794 pM and a receptor density (B[max]) of 256 femtomole/mg protein. Fiscus et al., (1987) demonstrated that ANP stimulated the accumulation and efflux of cGMP in cultured PC12 cells. This observation lends strong support to the present study and suggests ANP acts via specific cell surface receptors to exert its second messenger action. Binding of 125I-ANP (99-126) to a plasma membrane preparation from PC 12 cells increased with increasing protein concentration and remained linear up to 100 mug protein /100mul. The kinetics of ligand binding to the membrane suggested that ANP was degraded in studies performed at 37
[发布日期] [发布机构] University:University of Glasgow
[效力级别] [学科分类]
[关键词] Molecular biology [时效性]