IMMUNOHISTOCHEMICAL LOCALIZATION OF MU-OPIOID RECEPTORS IN RAT-BRAIN USING ANTIBODIES GENERATED AGAINST A PEPTIDE SEQUENCE PRESENT IN A PURIFIED MU-OPIOID BINDING-PROTEIN
Jm. Hiller et al., IMMUNOHISTOCHEMICAL LOCALIZATION OF MU-OPIOID RECEPTORS IN RAT-BRAIN USING ANTIBODIES GENERATED AGAINST A PEPTIDE SEQUENCE PRESENT IN A PURIFIED MU-OPIOID BINDING-PROTEIN, Neuroscience, 62(3), 1994, pp. 829-841
Light microscope visualization in rat brain of a pattern of distributi
on of immunoreactivity, which included immunolabeled perikarya and bea
ded processes, was achieved using an immunoaffinity purified polyclona
l antibody, Ab165, which recognizes the amino acid sequence, IRNLRQDRS
KYY, found in the mu-opioid binding protein purified in our laboratory
. Immunohistochemical staining with Ab165 was carried out by the avidi
n-biotin procedure. Antibody, preabsorbed with antigen, served as cont
rol. Extensive immunoreactivity was seen in the hippocampal formation,
the amygdaloid complex, the striatal complex, cortical regions, selec
t areas of the thalamus and hypothalamus and in laminae I and II of th
e dorsal horn in spinal cord. The distribution of immunoreactivity in
the rat brain of antibody 165, which mu-opioid binding protein, is con
cordant with the distribution of mu-opioid binding sites as determined
by other laboratories in autoradiographic, electrophysiological and i
mmunocytochemical studies. These findings have enabled us to distingui
sh areas possessing large fields of mu-opioid receptor containing cell
bodies from areas possessing dense networks of immunolabeled neuronal
processes or mixtures of both.