cDNA heterogeneity suggests structural variants related to the high-affinity IgE receptor

Fu-Tong Liu, K. Albrandt, M. W. Robertson

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The high-affinity IgE receptor present on mast cells and basophils is responsible for the IgE-mediated activation of these cells. The current model for this receptor depicts a four-subunit structure, αβγ2. A cDNA for the α subunit was recently cloned and predicts a structure consisting of two homologous extracellular domains, a transmembrane segment, and a cytoplasmic tail. Using a synthetic oligonucleotide corresponding to the amino-terminal sequence of the α subunit, we identified a number of cDNA clones from a rat basophilic leukaemia cell cDNA library. Nucleotide sequencing estabished four different forms of cDNA: one is nearly identical to the published cDNA; the second differs from the first in the 5' untranslated sequence; the other two forms use either one or the other of the 5'-end sequences as above and lack 163 base pairs in the region coding for the second extracellular domain. RNase protection analysis with radioactive RNA probes established the heterogeneity of rat basophilic leukemia cell mRNA with regard to both the 5' end and the internal sequences. Our results suggest the existence of at least four different protein forms related to the α subunit of the high-affinity IgE receptor.

Original languageEnglish (US)
Pages (from-to)5639-5643
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number15
StatePublished - 1988

Fingerprint

IgE Receptors
Complementary DNA
Leukemia
RNA Probes
Basophils
Ribonucleases
Gene Library
Mast Cells
Oligonucleotides
Base Pairing
Immunoglobulin E
Tail
Nucleotides
Clone Cells
Messenger RNA
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

cDNA heterogeneity suggests structural variants related to the high-affinity IgE receptor. / Liu, Fu-Tong; Albrandt, K.; Robertson, M. W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 15, 1988, p. 5639-5643.

Research output: Contribution to journalArticle

@article{b03a03a67cc7432cb1fc5caa644b84b1,
title = "cDNA heterogeneity suggests structural variants related to the high-affinity IgE receptor",
abstract = "The high-affinity IgE receptor present on mast cells and basophils is responsible for the IgE-mediated activation of these cells. The current model for this receptor depicts a four-subunit structure, αβγ2. A cDNA for the α subunit was recently cloned and predicts a structure consisting of two homologous extracellular domains, a transmembrane segment, and a cytoplasmic tail. Using a synthetic oligonucleotide corresponding to the amino-terminal sequence of the α subunit, we identified a number of cDNA clones from a rat basophilic leukaemia cell cDNA library. Nucleotide sequencing estabished four different forms of cDNA: one is nearly identical to the published cDNA; the second differs from the first in the 5' untranslated sequence; the other two forms use either one or the other of the 5'-end sequences as above and lack 163 base pairs in the region coding for the second extracellular domain. RNase protection analysis with radioactive RNA probes established the heterogeneity of rat basophilic leukemia cell mRNA with regard to both the 5' end and the internal sequences. Our results suggest the existence of at least four different protein forms related to the α subunit of the high-affinity IgE receptor.",
author = "Fu-Tong Liu and K. Albrandt and Robertson, {M. W.}",
year = "1988",
language = "English (US)",
volume = "85",
pages = "5639--5643",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "15",

}

TY - JOUR

T1 - cDNA heterogeneity suggests structural variants related to the high-affinity IgE receptor

AU - Liu, Fu-Tong

AU - Albrandt, K.

AU - Robertson, M. W.

PY - 1988

Y1 - 1988

N2 - The high-affinity IgE receptor present on mast cells and basophils is responsible for the IgE-mediated activation of these cells. The current model for this receptor depicts a four-subunit structure, αβγ2. A cDNA for the α subunit was recently cloned and predicts a structure consisting of two homologous extracellular domains, a transmembrane segment, and a cytoplasmic tail. Using a synthetic oligonucleotide corresponding to the amino-terminal sequence of the α subunit, we identified a number of cDNA clones from a rat basophilic leukaemia cell cDNA library. Nucleotide sequencing estabished four different forms of cDNA: one is nearly identical to the published cDNA; the second differs from the first in the 5' untranslated sequence; the other two forms use either one or the other of the 5'-end sequences as above and lack 163 base pairs in the region coding for the second extracellular domain. RNase protection analysis with radioactive RNA probes established the heterogeneity of rat basophilic leukemia cell mRNA with regard to both the 5' end and the internal sequences. Our results suggest the existence of at least four different protein forms related to the α subunit of the high-affinity IgE receptor.

AB - The high-affinity IgE receptor present on mast cells and basophils is responsible for the IgE-mediated activation of these cells. The current model for this receptor depicts a four-subunit structure, αβγ2. A cDNA for the α subunit was recently cloned and predicts a structure consisting of two homologous extracellular domains, a transmembrane segment, and a cytoplasmic tail. Using a synthetic oligonucleotide corresponding to the amino-terminal sequence of the α subunit, we identified a number of cDNA clones from a rat basophilic leukaemia cell cDNA library. Nucleotide sequencing estabished four different forms of cDNA: one is nearly identical to the published cDNA; the second differs from the first in the 5' untranslated sequence; the other two forms use either one or the other of the 5'-end sequences as above and lack 163 base pairs in the region coding for the second extracellular domain. RNase protection analysis with radioactive RNA probes established the heterogeneity of rat basophilic leukemia cell mRNA with regard to both the 5' end and the internal sequences. Our results suggest the existence of at least four different protein forms related to the α subunit of the high-affinity IgE receptor.

UR - http://www.scopus.com/inward/record.url?scp=0023730721&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023730721&partnerID=8YFLogxK

M3 - Article

VL - 85

SP - 5639

EP - 5643

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

SN - 0027-8424

IS - 15

ER -