Pharmacological, functional, and biochemical characterization of a high-affinity angiotensin receptor on differentiated NG108-15 cells

In the first part of these studies, the binding characteristics of $\sp{125}$I-angiotensin II (ANG II) to membranes prepared from undifferentiated and differentiated neuroblastoma x glioma hybrid cells (NG108-15) were investigated. Scatchard analysis revealed the existence of high and low affinity sites in differentiated cells, but only a low affinity site in undifferentiated cells. Similarly, self-displacement studies revealed competition to a single low affinity site in undifferentiated cells, and to high and low affinity sites in differentiated cells. Angiotensin III (ANG III) displaced high affinity binding in differentiated cells but did not displace low affinity binding in either differentiated or undifferentiated cells. Furthermore, GPP(NH)P inhibited $\sp{125}$I-ANG II binding to differentiated cells, in a dose dependent fashion, but had no effect on binding to undifferentiated cells.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Carrithers, Michael Dennis

Contributors dc:contributor

• Weyhenmeyer, James A.

• Biology, Neuroscience

Statement dc:rights

• Copyright 1991 Carrithers, Michael Dennis

Language dc:language

eng

Identifier

AAI9136560
(UMI)AAI9136560

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22826