Solubilization of the Neuropeptide Y Receptor from Rat Brain Membranes

1991 ◽  
Vol 56 (5) ◽  
pp. 1804-1809 ◽  
Author(s):  
Peter J. Mannon ◽  
Sabrena J. Mervin ◽  
Ian L. Taylor
1989 ◽  
Vol 256 (3) ◽  
pp. G637-G643 ◽  
Author(s):  
P. J. Mannon ◽  
I. L. Taylor ◽  
L. M. Kaiser ◽  
T. D. Nguyen

The receptor for neuropeptide Y (NPY) was identified on rat brain membranes after covalent labeling with 125I-NPY using the homobifunctional cross-linkers disuccinimido suberate and disuccinimido dithiobis(propionate) and the heterobifunctional photoactive cross-linker succinimido 4-azidobenzoate. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography revealed the presence of two bands at Mr 62,000 and 39,000. Both species showed the same high affinity for 125I-NPY. Exposure to reducing agents did not change the migration of these bands. When the NPY receptor complex was solubilized from the membranes with 1% Triton X-100 and analyzed by gel filtration chromatography, it eluted from a Fractogel TSK 55F column as a peak at approximately 65 kDa. This peak was asymmetric with a shoulder of radioactivity that probably reflects the smaller receptor species. These data indicate that the NPY receptor on rat brain membranes is a monomeric 58-kDa unit (62 kDa minus the mass of the cross-linked NPY) without covalently or noncovalently linked subunits. The smaller 39-kDa species may be an immature form of the 62-kDa species, a second distinct receptor, or a degradation product of the 62-kDa band.


1989 ◽  
Vol 264 (1) ◽  
pp. 354-362
Author(s):  
L H Lazarus ◽  
A Guglietta ◽  
W E Wilson ◽  
B J Irons ◽  
R de Castiglione

2000 ◽  
Vol 165 (1) ◽  
pp. 90-100 ◽  
Author(s):  
Margaret M. Durkin ◽  
Mary W. Walker ◽  
Kelli E. Smith ◽  
Eric L. Gustafson ◽  
Christophe Gerald ◽  
...  

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