Atrial natriuretic factor (ANF), a recently discovered polypeptide hormone, is one of the most potent naturally occurring natriuretic and diuretic agents. By analogy to other hormones, its cellular effects are probably mediated by ANF-receptor interactions.
The aims of this research are to characterize biochemically, physicochemically, and immunologically ANF receptor from human placenta. We will also characterize the ANF-induced phosphorylation of an endogenous substrate which we have recently observed in placental membranes and establish its relationship to the receptor. We will purify the receptor by affinity chromatography; establish optimal conditions and structural requirements for binding of the hormone to its receptors; determine its physicochemical structure; investigate the possibility of multiple binding site & prepare antibodies against receptor protein. Availability of purified receptor and antireceptor antibodies will enable us to fulfill our long-term goals of determining tissue, cellular, and subcellular distribution of atrial natriuretic factor receptors; elucidating its biosynthesis in human tissues; detecting structural differences in it associated with physiological or pathophysiological conditions such as pregnancies complicated with hypertension, and perhaps intervening therapeutically in the pathogenic process to which it contributes.
| Sen, I; Samanta, H; Livingston 3rd, W et al. (1991) Establishment of transfected cell lines producing testicular angiotensin-converting enzyme. Structural relationship between its secreted and cellular forms. J Biol Chem 266:21985-90 |
| Sen, I; Rajasekaran, A K (1991) Angiotensin II-binding protein in adult and neonatal rat heart. J Mol Cell Cardiol 23:563-72 |
| Roy, P; Naik, U; Sen, I (1988) Multiple forms of atrial natriuretic factor receptor in human placenta. Biochem Biophys Res Commun 153:1-6 |
