Characterization of [125I]beta-endorphin binding sites in the rat caudal dorsomedial medulla.

Abstract:

:[125I]beta-endorphin bound to high affinity (Kd = 0.25 nM) receptors in the caudal dorsomedial medulla of rats with a Bmax of 97 fmol/mg protein. The relative potency for displacement of [125I]beta-endorphin binding was: beta-endorphin(1-31) > beta-endorphin(1-27) > DAMGO > naloxone > N-acetyl-beta-endorphin(1-31) > U50488 > DPDPE. The Bmax for [3H]DAMGO binding was 81 fmol/mg protein, indicating that most [125I]beta-endorphin binding corresponds to mu-opioid receptors. [3H]DAMGO binding was not influenced by lesioning noradrenergic nerve terminals in the caudal dorsomedial medulla. Our findings indicate that beta-endorphin interacts primarily with mu-opioid receptors in the caudal dorsomedial medulla. These receptors are not affected by noradrenergic denervation.

journal_name

Peptides

journal_title

Peptides

authors

D'Souza MM,Carr JA

doi

10.1016/s0196-9781(98)00024-2

subject

Has Abstract

pub_date

1998-01-01 00:00:00

pages

931-7

issue

5

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(98)00024-2

journal_volume

19

pub_type

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