Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 6 March 1987:
Vol. 235. no. 4793, pp. 1224 - 1226
DOI: 10.1126/science.2881352
Prev | Table of Contents | Next

Articles

Science, Vol 235, Issue 4793, 1224-1226
Copyright © 1987 by American Association for the Advancement of Science

articles

Coexistence of guanylate cyclase and atrial natriuretic factor receptor in a 180-kD protein

AK Paul, RB Marala, RK Jaiswal, and RK Sharma

Atrial natriuretic factor (ANF) is a peptide hormone that is released from atria and regulates a number of physiological processes, including steroidogenesis in adrenal cortex and testes. The parallel stimulation of membrane guanylate cyclase and corticosterone production in isolated fasciculata cells of rat adrenal cortex has supported the hypothesis of a mediatory role for cyclic guanosine monophosphate (cyclic GMP) in signal transduction. A novel particulate guanylate cyclase tightly coupled with ANF receptor was purified approximately 273,000-fold by two-step affinity chromatography. The enzyme had a molecular size of 180 kilodaltons and was acidic in nature with a pI of 4.7. Its specific activity was 1800 nanomoles of cyclic GMP formed per minute per milligram of protein. The purified enzyme bound ANF with a specific binding activity of 4.01 nanomoles per milligram of protein, a value that is close to the theoretical binding activity of 5.55 nanomoles per milligram of protein for 1 mole of the ligand binding 1 mole of the receptor protein. These results indicate that the guanylate cyclase-coupled ANF receptor exists in a 180-kilodalton protein of rat adrenocortical carcinoma and represent a step toward the elucidation of the basic mechanism of cyclic GMP-mediated transmembrane signal transduction in response to a hormone.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Calcium-Modulated Rod Outer Segment Membrane Guanylate Cyclase Type 1 Transduction Machinery in the Testes.
A. Jankowska, B. Burczynska, T. Duda, J. B. Warchol, and R. K. Sharma (2007)
J Androl 28, 50-58
   Abstract »    Full Text »    PDF »
Natriuretic Peptides, Their Receptors, and Cyclic Guanosine Monophosphate-Dependent Signaling Functions.
L. R. Potter, S. Abbey-Hosch, and D. M. Dickey (2006)
Endocr. Rev. 27, 47-72
   Abstract »    Full Text »    PDF »
Amylin potently activates AP neurons possibly via formation of the excitatory second messenger cGMP.
T. Riediger, H. A. Schmid, T. Lutz, and E. Simon (2001)
Am J Physiol Regulatory Integrative Comp Physiol 281, R1833-R1843
   Abstract »    Full Text »    PDF »
Guanylyl Cyclases and Signaling by Cyclic GMP.
K. A. Lucas, G. M. Pitari, S. Kazerounian, I. Ruiz-Stewart, J. Park, S. Schulz, K. P. Chepenik, and S. A. Waldman (2000)
Pharmacol. Rev. 52, 375-414
   Abstract »    Full Text »    PDF »
The Membrane Form of Guanylate Cyclase.
D.L. Garbers, D.G. Lowe, L.J. Dangott, M. Chinkers, D.S. Thorpe, J.K. Bentley, C.S. Ramarao, D.V. Goeddel, and S. Singh (1988)
Cold Spring Harb Symp Quant Biol 53, 993-1003
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)