On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain

Kai Liu, Clare M Bergson, Robert Levenson, Claudia Schmauss

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

A truncated dopamine D3-receptor-like mRNA, named D3nf, predicts a protein that differs from the D3-receptor only in the carboxyl terminus. However, such a protein has lost the predicted membrane topology typically found for G protein-coupled receptors. Results presented here show that D3nf, mRNA arises from the D3-encoded primary transcript via alternative splicing. This splicing, however, appears to involve cleavage of an unusual 3′ splice site. Therefore, we tested the possibility that D3nf mRNA results from a splicing error. If this were the case, D3nf, mRNA would be expected to be present in the cytoplasm only at very low amounts, and it would not be expected to be translated into protein. However, the relative abundance of cytoplasmic D3/D3nfJmRNA in human cortical tissues was found to be similar. Furthermore, we raised polyclonal antisera against the predicted carboxyl-terminal peptide sequence ofD3nf that reacts specifically with a protein expressed in stably D3nf mRNA-expressing COS 7 cells. The use of this antiserum also revealed the presence of a ∼68 kDa D3nf-like immunoreactive protein in human brain, suggesting that the atypically processed D3nf mRNA is translated.

Original languageEnglish (US)
Pages (from-to)29220-29226
Number of pages7
JournalJournal of Biological Chemistry
Volume269
Issue number46
StatePublished - Nov 18 1994
Externally publishedYes

Fingerprint

Dopamine D3 Receptors
Brain
Messenger RNA
Proteins
Immune Sera
RNA Splice Sites
COS Cells
Alternative Splicing
G-Protein-Coupled Receptors
Cytoplasm
Topology
Tissue
Membranes
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain. / Liu, Kai; Bergson, Clare M; Levenson, Robert; Schmauss, Claudia.

In: Journal of Biological Chemistry, Vol. 269, No. 46, 18.11.1994, p. 29220-29226.

Research output: Contribution to journalArticle

@article{fba53e9add7344a285768adb0eda4c88,
title = "On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain",
abstract = "A truncated dopamine D3-receptor-like mRNA, named D3nf, predicts a protein that differs from the D3-receptor only in the carboxyl terminus. However, such a protein has lost the predicted membrane topology typically found for G protein-coupled receptors. Results presented here show that D3nf, mRNA arises from the D3-encoded primary transcript via alternative splicing. This splicing, however, appears to involve cleavage of an unusual 3′ splice site. Therefore, we tested the possibility that D3nf mRNA results from a splicing error. If this were the case, D3nf, mRNA would be expected to be present in the cytoplasm only at very low amounts, and it would not be expected to be translated into protein. However, the relative abundance of cytoplasmic D3/D3nfJmRNA in human cortical tissues was found to be similar. Furthermore, we raised polyclonal antisera against the predicted carboxyl-terminal peptide sequence ofD3nf that reacts specifically with a protein expressed in stably D3nf mRNA-expressing COS 7 cells. The use of this antiserum also revealed the presence of a ∼68 kDa D3nf-like immunoreactive protein in human brain, suggesting that the atypically processed D3nf mRNA is translated.",
author = "Kai Liu and Bergson, {Clare M} and Robert Levenson and Claudia Schmauss",
year = "1994",
month = "11",
day = "18",
language = "English (US)",
volume = "269",
pages = "29220--29226",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "46",

}

TY - JOUR

T1 - On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain

AU - Liu, Kai

AU - Bergson, Clare M

AU - Levenson, Robert

AU - Schmauss, Claudia

PY - 1994/11/18

Y1 - 1994/11/18

N2 - A truncated dopamine D3-receptor-like mRNA, named D3nf, predicts a protein that differs from the D3-receptor only in the carboxyl terminus. However, such a protein has lost the predicted membrane topology typically found for G protein-coupled receptors. Results presented here show that D3nf, mRNA arises from the D3-encoded primary transcript via alternative splicing. This splicing, however, appears to involve cleavage of an unusual 3′ splice site. Therefore, we tested the possibility that D3nf mRNA results from a splicing error. If this were the case, D3nf, mRNA would be expected to be present in the cytoplasm only at very low amounts, and it would not be expected to be translated into protein. However, the relative abundance of cytoplasmic D3/D3nfJmRNA in human cortical tissues was found to be similar. Furthermore, we raised polyclonal antisera against the predicted carboxyl-terminal peptide sequence ofD3nf that reacts specifically with a protein expressed in stably D3nf mRNA-expressing COS 7 cells. The use of this antiserum also revealed the presence of a ∼68 kDa D3nf-like immunoreactive protein in human brain, suggesting that the atypically processed D3nf mRNA is translated.

AB - A truncated dopamine D3-receptor-like mRNA, named D3nf, predicts a protein that differs from the D3-receptor only in the carboxyl terminus. However, such a protein has lost the predicted membrane topology typically found for G protein-coupled receptors. Results presented here show that D3nf, mRNA arises from the D3-encoded primary transcript via alternative splicing. This splicing, however, appears to involve cleavage of an unusual 3′ splice site. Therefore, we tested the possibility that D3nf mRNA results from a splicing error. If this were the case, D3nf, mRNA would be expected to be present in the cytoplasm only at very low amounts, and it would not be expected to be translated into protein. However, the relative abundance of cytoplasmic D3/D3nfJmRNA in human cortical tissues was found to be similar. Furthermore, we raised polyclonal antisera against the predicted carboxyl-terminal peptide sequence ofD3nf that reacts specifically with a protein expressed in stably D3nf mRNA-expressing COS 7 cells. The use of this antiserum also revealed the presence of a ∼68 kDa D3nf-like immunoreactive protein in human brain, suggesting that the atypically processed D3nf mRNA is translated.

UR - http://www.scopus.com/inward/record.url?scp=0028113535&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028113535&partnerID=8YFLogxK

M3 - Article

VL - 269

SP - 29220

EP - 29226

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 46

ER -