Human recombinant interleukin-1β isolated from Escherichia coli by simple osmotic shock

Joseph-Liauzun, Evelyne; Leplatois, Pascal; Legoux, Richard; Guerveno, V.; Marchese, E.; Ferrara, Pascual

doi:10.1016/0378-1119(90)90293-z

Cited by 22 publications

(9 citation statements)

References 16 publications

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“…sIL-lR is also released from the human B-cell Burkitt lymphoma cell line Raji, which expresses only type II IL-iR (16,17 of site-specific IL-1l3 mutants have been described (18). Wildtype and mutant IL-1l3 proteins were obtained by osmotic shock (19). Purity of the recombinant proteins was assessed to be 90-95% by SDS/PAGE and Coomassie blue staining.…”

mentioning

confidence: 99%

Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist.

Symons

Young

Duff

1995

Proc. Natl. Acad. Sci. U.S.A.

199

130

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The human IL-1 gene family comprises IL-la, IL-1f3, and IL-1 receptor antagonist (IL-lra). All three share limited amino acid identity and bind to the same receptors on different cell types (1). In the case of IL-ia and IL-11, ligand-receptor interaction activates signaling pathways involved in both immune and inflammatory responses. Binding of IL-lra to the IL-1 receptor (IL-lR) does not trigger signal transduction, and the actions of IL-la and IL-113 are blocked by this unique antagonist protein (2).Both IL-ia and IL-1,B are initially synthesized as precursor proteins of 31 kDa and are processed to 17-kDa mature polypeptides upon release. However, release does not seem to be dependent on processing, as significant amounts of IL-1 precursor can be found in the extracellular medium (3). The

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mentioning

confidence: 99%

Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist.

Symons

Young

Duff

1995

Proc. Natl. Acad. Sci. U.S.A.

199

130

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“…Some eukaryotic proteins, such as interleukin-lp, can be recovered by simple osmotic shock (Joseph-Liauzun et al, 1990); others, however, are unable to enter the export pathway. For these proteins, additional steps must be taken to obtain their secretion.…”

Section: Introductionmentioning

confidence: 99%

Targeting of interleukin-2 to the periplasm of Escherichia coli

Halfmann¹,

Brailly²,

Bernadac³

et al. 1993

Journal of General Microbiology

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A synthetic gene coding for interleukin-2 (IL-2) was used to produce large amounts of recombinant IL-2 (met-IL-2) in Escherichia coli. Met-IL-2 was found to accumulate in the cytoplasm in an insoluble, aggregated form. Inclusion bodies located at the pole caps of cells were detected using immunogold labelling. Constructs were designed to fuse the IL-2 gene to DNA fragments encoding signal peptides for an outer-membrane protein (OmpA) or for a periplasmic protein (PhoA) of E. coli. No significant maturation was observed with these fusion proteins which were found in an insoluble form in the cytoplasm. The influence of charge disposition at the N-terminus of the mature portion of the protein was investigated by replacing positively charged amino acids with glutamic acid. None of the introduced substitutions had any effect. Various factors that might affect expression, secretion and folding were examined in an attempt to obtain secretion. By fusing IL-2 to the precursor maltose-binding protein (preMBP) a large fraction of the preMBP-IL-2 protein was correctly processed and transported to the periplasmic space. IL-2 derived from MBP-IL-2 after FXa cleavage possessed similar specific activity to recombinant IL-2 produced in Chinese Hamster ovary cells.

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“…Plasmid pET3a (Novagen, Inc., Madison, WI) was used as the T7 expression plasmid (21). A NdeI-BamHI fragment corresponding to the synthetic human IL-1␤ gene was inserted between the NdeI and BamHI sites of pET3a to produce the expression plasmid.…”

Section: Materials-humanmentioning

confidence: 99%

Lectin-like Characteristics of Recombinant Human Interleukin-1β Recognizing Glycans of the Glycosylphosphatidylinositol Anchor

Fukushima

Hara-Kuge

Ohkura

et al. 1997

Journal of Biological Chemistry

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We found that 35 S-labeled recombinant human interleukin-1␤ (rhIL-1␤) binds phosphatidylinositol-specific phospholipase C-treated human placental alkaline phosphatase, phosphatidylinositol-specific phospholipase C-treated trypanosome surface variant glycoproteins, and urinary uromodulin immobilized on plates or immobilized on CNBr-activated Sepharose 4B. The interaction between rhIL-1␤ and these glycoproteins was lectin-like, since it was inhibited in the presence of specific saccharides, i.e. mannose 6-phosphate or synthetic Ac-NH⅐CH 2 ⅐CH 2 ⅐PO 4 ؊ 36Man␣13(؎2Man␣13؎6Man␣13)-propyl at about 1 M. On the other hand, a wide variety of compounds including biantennary sugar chains derived from these glycoproteins as well as ethanolamine phosphate, inositol phosphate, mannose 6-sulfate, mannose 1-phosphate, glucose 6-phosphate, and mannitol 6-phosphate did not show any inhibitory effect at concentrations up to 1 mM. These results indicate that rhIL-1␤ interacts with these glycoproteins via the mannose 6-phosphate diester of glycans on the glycosylphosphatidylinositol (GPI) anchor. Furthermore, when monolayers of polarized Madin-Darby canine kidney cells on polycarbonate filter membranes were incubated with 35 S-rhIL-1␤ in either the apical or basolateral chamber, 35S-interleukin-1␤ was found to bind specifically to the apical membranes with a K a value of 4.6 ؋ 10 7 M ؊1, and the specific interaction was inhibited by 1 M mannose 6-phosphate. Since the mannose 6-phosphate diester moiety exists only in the GPI glycans on plasma membranes, it was evident that interleukin-1␤ can directly interact with the mannose 6-phosphate diester component of the intact glycan of GPI anchors on plasma membranes.Until now, over 50 types of cytokines have been reported that mediate the regulatory network established between lymphoid cells, hematopoietic cells, and endothelial cells that control their differentiation and proliferation (1). In this cytokine network, a single cytokine can act as both a positive signal and a negative one, depending on the type of target cells. In contrast, in some instances multiple cytokines act on a single cell and show the same biological effects. The response of target cells to a given cytokine is determined by the expression of the cytokine receptor and/or the nature of the link between the receptor and the signal transduction pathways of the target cells. We have been interested in the lectin-like character of cytokines in relation to their role as signal transducers or effectors. On the basis of their lectin-like character, various cytokines have been categorized into several groups. Growth factors such as granulocyte-macrophage colony-stimulating factor (2), heparinbinding growth factor (3), basic fibroblast growth factor (4, 5), and midkine (6) bind to heparan sulfate, whereas tumor necrosis factor-␣ (TNF-␣) 1 (7), lymphotoxin (8), interleukin-1␣ and -1␤ (7, 9), interleukin-2 (10), and interleukin-3 (11) recognize N,NЈ-diacetylchitobiose and/or some oligomannosyl residues, although the precise car...

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Human recombinant interleukin-1β isolated from Escherichia coli by simple osmotic shock

Cited by 22 publications

References 16 publications

Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist.

Soluble type II interleukin 1 (IL-1) receptor binds and blocks processing of IL-1 beta precursor and loses affinity for IL-1 receptor antagonist.

Targeting of interleukin-2 to the periplasm of Escherichia coli

Lectin-like Characteristics of Recombinant Human Interleukin-1β Recognizing Glycans of the Glycosylphosphatidylinositol Anchor

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