Identification of mRNAs encoding two different soluble forms of the human interferon α-receptor

Carolina Abramovich; Edward Ratovitski; Erik Lundgren; Michel Revel

doi:10.1016/0014-5793(94)80287-4

Identification of mRNAs encoding two different soluble forms of the human interferon α-receptor

Carolina Abramovich, Edward Ratovitski, Erik Lundgren, Michel Revel

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

Transcripts of the human IFN α-receptor (IFNAR) gene, lacking the transmembrane (TM) domain were found in human myeloma U266^S cells, in addition to the transmembranal IFNAR cDNA. Two different cDNAs encoding such soluble IFNAR forms were identified. Form 1 has a deletion causing a frameshift toward the end of the extracellular (EC) domain predicting a tail of 7 amino acids. Form 2 has two in-frame deletions and conserves most of the intracytoplasmatic domain of IFNAR. The transcripts for the two soluble forms are still found in U266^r cells which have lost the transmembranal IFNAR transcript. Human cells seem to have independent mechanisms to synthesize soluble IFN receptors, which may act as competitors outside the cells or carry IFN-mediated functions inside the cell.

Original language	English (US)
Pages (from-to)	295-300
Number of pages	6
Journal	FEBS Letters
Volume	338
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(94)80287-4
State	Published - Feb 7 1994
Externally published	Yes

Keywords

Alternative splicing
Interferon receptor
Myeloma cell
Soluble receptor

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0014-5793(94)80287-4

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title = "Identification of mRNAs encoding two different soluble forms of the human interferon α-receptor",

abstract = "Transcripts of the human IFN α-receptor (IFNAR) gene, lacking the transmembrane (TM) domain were found in human myeloma U266S cells, in addition to the transmembranal IFNAR cDNA. Two different cDNAs encoding such soluble IFNAR forms were identified. Form 1 has a deletion causing a frameshift toward the end of the extracellular (EC) domain predicting a tail of 7 amino acids. Form 2 has two in-frame deletions and conserves most of the intracytoplasmatic domain of IFNAR. The transcripts for the two soluble forms are still found in U266r cells which have lost the transmembranal IFNAR transcript. Human cells seem to have independent mechanisms to synthesize soluble IFN receptors, which may act as competitors outside the cells or carry IFN-mediated functions inside the cell.",

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AU - Abramovich, Carolina

AU - Ratovitski, Edward

AU - Lundgren, Erik

AU - Revel, Michel

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Y1 - 1994/2/7

N2 - Transcripts of the human IFN α-receptor (IFNAR) gene, lacking the transmembrane (TM) domain were found in human myeloma U266S cells, in addition to the transmembranal IFNAR cDNA. Two different cDNAs encoding such soluble IFNAR forms were identified. Form 1 has a deletion causing a frameshift toward the end of the extracellular (EC) domain predicting a tail of 7 amino acids. Form 2 has two in-frame deletions and conserves most of the intracytoplasmatic domain of IFNAR. The transcripts for the two soluble forms are still found in U266r cells which have lost the transmembranal IFNAR transcript. Human cells seem to have independent mechanisms to synthesize soluble IFN receptors, which may act as competitors outside the cells or carry IFN-mediated functions inside the cell.

AB - Transcripts of the human IFN α-receptor (IFNAR) gene, lacking the transmembrane (TM) domain were found in human myeloma U266S cells, in addition to the transmembranal IFNAR cDNA. Two different cDNAs encoding such soluble IFNAR forms were identified. Form 1 has a deletion causing a frameshift toward the end of the extracellular (EC) domain predicting a tail of 7 amino acids. Form 2 has two in-frame deletions and conserves most of the intracytoplasmatic domain of IFNAR. The transcripts for the two soluble forms are still found in U266r cells which have lost the transmembranal IFNAR transcript. Human cells seem to have independent mechanisms to synthesize soluble IFN receptors, which may act as competitors outside the cells or carry IFN-mediated functions inside the cell.

KW - Alternative splicing

KW - Interferon receptor

KW - Myeloma cell

KW - Soluble receptor

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Identification of mRNAs encoding two different soluble forms of the human interferon α-receptor

Abstract

Keywords

ASJC Scopus subject areas

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