TY - JOUR
T1 - The κ-opioid receptor is primarily postsynaptic
T2 - Combined immunohistochemical localization of the receptor and endogenous opioids
AU - Arvidsson, Ulf
AU - Riedl, Maureen
AU - Chakrabarti, Sumita
AU - Vulchanova, Lucy
AU - Lee, Jang Hern
AU - Nakano, Albert H.
AU - Lin, Xiaoqin
AU - Loh, Horace H.
AU - Law, Ping Yee
AU - Wessendorf, Martin W.
AU - Elde, Robert
PY - 1995/5/23
Y1 - 1995/5/23
N2 - Antisera were raised against a synthetic peptide corresponding to the carboxyl terminus of the κ-opioid receptor (KOR1). Specificity of the antisera was verified by staining of COS-7 cells transfected with KOR1 and epitope-tagged KOR1 cDNAs, by recognition by the antisera of proteins on Western blots of both transfected cells and brain tissue, by the absence of staining of both brain tissue and transfected cells after preabsorption of the antisera with the cognate peptide, and on the strong correlation between the distribution of KOR1 immunoreactivity and that of earlier ligand binding and in situ hybridization studies. Results indicate that KOR1 in neurons is targeted into both the axonal and somatodendritic compartments, but the majority of immunostaining was seen in the somatodendritic compartment. In sections from rat and guinea pig brain, prominent KOR1 staining was seen in the ventral forebrain, hypothalamus, thalamus, posterior pituitary, and midbrain. While the staining pattern was similar in both species, distinct differences were also observed. The distribution of preprodynorphin and KOR1 immunoreactivity was complementary in many brain regions, suggesting that KOR1 is poised to mediate the physiological actions of dynorphin. However, the distribution of KOR1 and enkephalin immunoreactivity was complementary in some regions as well. These results suggest that the KOR1 protein is primarily, but not exclusively, deployed to postsynaptic membranes where it mediates the effects of products of preprodynorphin and possibly preproenkephalin.
AB - Antisera were raised against a synthetic peptide corresponding to the carboxyl terminus of the κ-opioid receptor (KOR1). Specificity of the antisera was verified by staining of COS-7 cells transfected with KOR1 and epitope-tagged KOR1 cDNAs, by recognition by the antisera of proteins on Western blots of both transfected cells and brain tissue, by the absence of staining of both brain tissue and transfected cells after preabsorption of the antisera with the cognate peptide, and on the strong correlation between the distribution of KOR1 immunoreactivity and that of earlier ligand binding and in situ hybridization studies. Results indicate that KOR1 in neurons is targeted into both the axonal and somatodendritic compartments, but the majority of immunostaining was seen in the somatodendritic compartment. In sections from rat and guinea pig brain, prominent KOR1 staining was seen in the ventral forebrain, hypothalamus, thalamus, posterior pituitary, and midbrain. While the staining pattern was similar in both species, distinct differences were also observed. The distribution of preprodynorphin and KOR1 immunoreactivity was complementary in many brain regions, suggesting that KOR1 is poised to mediate the physiological actions of dynorphin. However, the distribution of KOR1 and enkephalin immunoreactivity was complementary in some regions as well. These results suggest that the KOR1 protein is primarily, but not exclusively, deployed to postsynaptic membranes where it mediates the effects of products of preprodynorphin and possibly preproenkephalin.
KW - guinea pig
KW - preprodynorphin
KW - preproenkephalin
KW - rat
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U2 - 10.1073/pnas.92.11.5062
DO - 10.1073/pnas.92.11.5062
M3 - Article
C2 - 7539141
AN - SCOPUS:0028979004
SN - 0027-8424
VL - 92
SP - 5062
EP - 5066
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 11
ER -