Structure and expression of a cloned cDNA for mouse interferon-beta.

Higashi, Youichirou; Sokawa, Yoshihiro; Watanabe, Yoshihiko; Kawade, Yoshimi; Ohno, Susumu; Takaoka, Chikako; Taniguchi, Tooru

doi:10.1016/s0021-9258(17)44698-9

Cited by 150 publications

(5 citation statements)

References 40 publications

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“…Since IFN-aA's antiviral activity is highly sensitive to tertiary structure (Wetzel et al, 1982), the required disulfide may serve to preserve some key conformational feature required for receptor binding; the same bond clearly plays a role in conformational stability at 37 °C (see below). In a recent paper, Higashi et al (1983) showed that mouse IFN-/3, while homologous (48% at amino acid level) with human IFN-/3, contains only one cysteine, at position 17. This indicates that all type I interferons do not require disulfides for activity and suggests that those that do probably utilize this important disulfide for orientation and support of a receptor-binding region, but not its direct composition.…”

Section: Ifn-a As Originally Observed Withmentioning

confidence: 99%

“…This means that the 29-138 disulfide plays a role in the preservation of an important global conformation of the IFN-aA molecule. In this regard it is of interest that disulfide-free mouse IFN-|3 (Higashi et al, 1983; see above) possesses, in place of human IFN-jS's Cys-31, Asn in a recognition sequence for N-linked glycosylation. Glycosylation has been suggested to be another route by which proteins can be stabilized.…”

Section: Ifn-a As Originally Observed Withmentioning

confidence: 99%

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Roles of the 29-138 disulfide bond of subtype A of human .alpha. interferon in its antiviral activity and conformational stability

Morehead¹,

Johnston²,

Wetzel³

1984

Biochemistry

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Human alpha (leukocyte) interferons contain two disulfide bonds between Cys-1 and Cys-98 and between Cys-29 and Cys-138. Reduction of interferon under native conditions leads to irreversible loss of antiviral activity; reduction in denaturant, followed by oxidation in native conditions, leads to restoration of activity. This behavior, unusual for disulfide-containing proteins, was studied by using a thiosulfonate derivative of subtype A of human alpha interferon (IFN-alpha A). The disulfide-free thiosulfonate formed at 25 degrees C has essentially no antiviral activity, while maintaining a conformation related to that of native IFN-alpha A. This species can regain activity after regeneration of its 29-138 disulfide, by thiol-disulfide interchange in native buffer. Incubation of the disulfide-free thiosulfonate under nonreducing conditions at 37 degrees C generates a monomeric species that has lost its native conformation as well as its ability to regain antiviral activity after thiol-disulfide interchange. These results explain the difficulty in obtaining, under native conditions, a reduced species that regains activity upon oxidation; complete reduction of IFN-alpha A in 100 mM 2-mercaptoethanol requires 37 degrees C, a temperature that promotes conformational decay of the disulfide-free form.

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Section: Ifn-a As Originally Observed Withmentioning

confidence: 99%

Section: Ifn-a As Originally Observed Withmentioning

confidence: 99%

Roles of the 29-138 disulfide bond of subtype A of human .alpha. interferon in its antiviral activity and conformational stability

Morehead¹,

Johnston²,

Wetzel³

1984

Biochemistry

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“…Amino acid sequence conservation between mouse and human EPO is significantly higher than for the other hematopoietic regulators that have been studied. Mature EPO protein is 81% conserved between the two species, while for the various interferons (14,17,35), interleukin 2 (21), and GM-CSF (29,42), conservation is generally between 40 and 60%. Features of the mature EPO protein which have been conserved include the glycosylation sites and the absolute amino acid number.…”

Section: Resultsmentioning

confidence: 99%

Murine Erythropoietin Gene: Cloning, Expression, and Human Gene Homology

Shoemaker¹,

Mitsock²

1986

Molecular and Cellular Biology

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The gene for murine erythropoietin (EPO) was isolated from a mouse genomic library with a human EPO cDNA probe. Nucleotide sequence analysis permitted the identification of the murine EPO coding sequence and the prediction of the encoded amino acid sequence based on sequence conservation between the mouse and human EPO genes. Both the coding DNA and the amino acid sequences were 80% conserved between the two species. Transformation of COS-1 cells with a mammalian cell expression vector containing the murine EPO coding region resulted in secretion of murine EPO with biological activity on both murine and human erythroid progenitor cells. The transcription start site for the murine EPO gene in kidneys was determined. This permitted tentative identification of the transcription control region. The region included 140 base pairs upstream of the cap site which was over 90% conserved between the murine and human genes. Surprisingly, the first intron and much of the 5'- and 3'-untranslated sequences were also substantially conserved between the genes of the two species.

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“…Total cytoplasmic RNA was extracted as described above, cDNA synthesis with 15 p,g of RNA and polymerase chain reaction (PCR) of the single-stranded cDNA were done under standard conditions (25 cycles of PCR, with 1 cycle consisting of 1 min at 94°C, 45 s at 50°C, and 1 min at 72°C; 25 cycles preceded by 2 min at 95°C and followed by 7 min at 72°C). Oligonucleotide primers correspond to amino acids 21 to 29 and 101 to 109 of the MuIFN-0 sequence (29). One-tenth of each amplified DNA was used for Southern blot analysis.…”

Section: Methodsmentioning

confidence: 99%

Action of Spontaneously Produced Beta Interferon in Differentiation of Embryonal Carcinoma Cells through an Autoinduction Mechanism

Belhumeur¹,

Lanoix²,

Blais³

et al. 1993

Molecular and Cellular Biology

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In the current study, we have addressed the role of interferons (IFNs) in controlling the differentiation of pluripotent P19 embryonal carcinoma (EC) cells. Blocking IFN activity in the culture medium of differentiating cells with antibodies leads to a strong decrease in the degree of differentiation. The antibodies are active for a relatively short time. During this time, IFN-beta mRNA can be detected in the differentiating cells, as can increases of IFN stimulation response element-binding activity and NF-KB. The timing of IFN action also coincides with the accumulation of cytoplasmic double-stranded RNA (dsRNA) and with a drop in dsRNA unwindase-modificase activity. A model for the involvement of autoinduction of IFN by intracellular dsRNA in the control of differentiation in this system is presented.

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Structure and expression of a cloned cDNA for mouse interferon-beta.

Cited by 150 publications

References 40 publications

Roles of the 29-138 disulfide bond of subtype A of human .alpha. interferon in its antiviral activity and conformational stability

Roles of the 29-138 disulfide bond of subtype A of human .alpha. interferon in its antiviral activity and conformational stability

Murine Erythropoietin Gene: Cloning, Expression, and Human Gene Homology

Action of Spontaneously Produced Beta Interferon in Differentiation of Embryonal Carcinoma Cells through an Autoinduction Mechanism

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