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  • 1
    Electronic Resource
    Electronic Resource
    The Pharmacokinetics, Distribution and Degradation of Human Recombinant Interleukin 1β in Normal Rats (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 34 (1991), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Based upon in vivo rat experiments it was recently suggested that interleukin I in the circulation may be implicated in the initial events of β-cell destruction leading to insulin-dependent diabetes mellitus (IDDM) in humans. The aim of the present study was to estimate half-lives of distribution and elimination phases (T1/2β) of human recombinant interleukin 1β(rIL-1β), and its tissue distribution and cellular localization by means of mono-labelled, biologically active 125I-rIL-1β. After intravenous (iv.) injection, 125I-rIL-1β was eliminated from the circulation with a T1/2α of 2.9 min and a T1/2β of 41.1 min. The central and peripheral volume of distribution was 20.7 and 19.1 ml/rat, respectively, and the metabolic clearance rate was 16.9 ml/min/kg. The kidney and liver showed the highest accumulation of tracer, and autoradiography demonstrated that 125I-rIL-1β was localized 10 the proximal tubules in the kidney and to the hepatocytes in the liver. Furthermore, grains were localized to the islets of Langerhans in the pancreas. Tracer-bound proteins corresponding to intact 125I-rIL-1β were found in the circulation after i.v., intraperitoneal (i,p.) and subcutaneous (s.c.) injections, as demonstrated by high performance size exclusion chromatography. trichloracetic acid precipitation and SDS PAGE until 5h after tracer injection. Pre-treatment with “cold” rIL-1β enhanced degradation of a subsequent injection of tracer. The route of administration was of importance for the biological effects of rIL-1β as demonstrated by a reduced food intake, increased rectal temperature and blood glucose after s.c. injection of rIL-1β compared with i.p. The present demonstration of intact rIL-1β in the circulation and the islets of Langerhans supports the hypothesis that systemic IL-1β may be involved in the initial 1β-cell destruction leading to IDDM in humans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1991.tb01583.x
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison of Biological and Immunological Activities of Human Monocyte-Derived Interleukin 1β and Human Recombinant Interleukin 1β (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 31 (1990), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Recombinant human interleukin 1β (rhIL-1β) and supernatants of Escherichia coli lipopolysaccharides-stimulated human monocyte (Mo) cultures, containing native human IL-lβ (nhIL-1β), demonstrate significant differences when tested in the mouse co-stimulatory thymocyte (lymphocyte activating factor [LAF]) assay. The aims of the present study were to investigate this characteristic difference between rhIL-1β and Mo culture supernatants (Mo supernatants), and to compare the biological and the immunological activity of preparations of rhlL-lβ and nhlL-1β during each step of an identical purification procedure. The biological activity of rhIL-1β/nhIL-lβ preparations was characterized by the use of the LAF assay and the rat islet insulin release assay. An IL-1β enzyme-linked immunosorbent assay (ELISA) was established in order to compare the biological and immunological responses of the IL-lβ preparations.We report that the significant difference between rhIL-lβ and supernatants of Mo cultures, which was only demonstrable in the LAF assay, is due to the presence of interleukin 6 (IL-6) in the Mo supernatants. We describe a simple cation exchange chromatography separating nhlL-lβ and lL-6 of Mo supernatants. The highly purified rhIL-β possessing the correct amino-terminal sequence and nhIL-lβ have identical biological and immunological activities demonstrating a specific biological activity (SBA) of 3x102 U/ng IL-lβ, Thus, we have no indications of secondary or tertiary structural differences between rhIL-1β and purified nhIL-lβ.In contrast, both in the LAF assay and in the rat islet insulin release assay the SBA of anaminoextended rhIL-lβ form, Met-Glu-Ala-Glu-rhIL-lβ, was only 1-2% of the SBA of rhIL-lβ, suggesting that structural changes were introduced into the molecule by the amino-terminal extension. In the present study we have demonstrated that systematic combined testing of IL-lβ preparations in two different biological assays and an immunological assay is useful for the characterization and comparison of the activity of recombinant and native IL-1β preparations purified by the use of exactly the same procedures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1990.tb02763.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation by anion-exchange of immunologically and enzymatically active human islet glutamic acid decarboxylase 65 overexpressed in Sf9 insect cells (1995)
    Springer
    Diabetologia 38 (1995), S. 14-23 
    Details
    ISSN: 1432-0428
    Keywords: Key words Baculovirus ; Sf9 cells ; recombinant ; human ; islet ; glutamic acid decarboxylase ; 65 kDa ; purification.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The enzyme l-glutamic acid decarboxylase is a major autoantigen of the beta cell. Autoantibodies against this enzyme are observed before the onset of insulin-dependent diabetes mellitus (IDDM) in man and may be of predictive value. There is evidence that this enzyme is involved in the development of autoimmune diabetes in animals. In order to facilitate the investigation of the role of l-glutamine acid decarboxylase in IDDM, we expressed the 65 kDa isoform of human islet l-glutamic acid decarboxylase in insect cells using a baculovirus-based vector. The material was expressed at high levels (up to 50 mg/l of cells). Partially purified metabolically labelled l-glutamic acid decarboxylase bound to immunoglobulins in the sera from 20 of 49 subjects with newly-diagnosed IDDM. The enzyme was isolated in high yields (up to 26 mg/l cell culture) with fully maintained enzymatic activity by either ion-exchange chromatography or immunoaffinity chromatography. Purified l-glutamic acid decarboxylase inhibited the binding of radioactive l-glutamic acid decarboxylase, prepared by in vitro translation of mRNA, to immunoglobulins in the sera of subjects with IDDM. Recombinant human islet l-glutamic acid decarboxylase, isolated from Sf9 cells, is a suitable material for the large scale investigation of the utility of this enzyme in the prediction and prevention of autoimmune diabetes. [Diabetologia (1995) 38: 14–23
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250050248
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation by anion-exchange of immunologically and enzymatically active human islet glutamic acid decarboxylase 65 overexpressed in Sf9 insect cells (1995)
    Springer
    Diabetologia 38 (1995), S. 14-23 
    Details
    ISSN: 1432-0428
    Keywords: Baculovirus ; Sf9 cells ; recombinant ; human ; islet ; glutamic acid decarboxylase ; 65 kDa ; purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The enzymel-glutamic acid decarboxylase is a major autoantigen of the beta cell. Autoantibodies against this enzyme are observed before the onset of insulin-dependent diabetes mellitus (IDDM) in man and may be of predictive value. There is evidence that this enzyme is involved in the development of autoimmune diabetes in animals. In order to facilitate the investigation of the role ofl-glutamine acid decarboxylase in IDDM, we expressed the 65 kDa isoform of human isletl-glutamic acid decarboxylase in insect cells using a baculovirus-based vector. The material was expressed at high levels (up to 50 mg/l of cells). Partially purified metabolically labelledl-glutamic acid decarboxylase bound to immunoglobulins in the sera from 20 of 49 subjects with newly-diagnosed IDDM. The enzyme was isolated in high yields (up to 26 mg/l cell culture) with fully maintained enzymatic activity by either ion-exchange chromatography or immunoaffinity chromatography. Purifiedl-glutamic acid decarboxylase inhibited the binding of radioactivel-glutamic acid decarboxylase, prepared by in vitro translation of mRNA, to immunoglobulins in the sera of subjects with IDDM. Recombinant human isletl-glutamic acid decarboxylase, isolated from Sf9 cells, is a suitable material for the large scale investigation of the utility of this enzyme in the prediction and prevention of autoimmune diabetes. [Diabetologia (1995) 38: 14–23
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02369348
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