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 language | English (US) |
|---|---|
| Pages (from-to) | 5639-5643 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 85 |
| Issue number | 15 |
| State | Published - 1988 |
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ASJC Scopus subject areas
- General
- Genetics
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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 journal › Article
}
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.
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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 -