Covalent disulfide binding of human IL-1β to α2-macroglobulin: Inhibition by d-penicillamine

Teodorescu, Marius; McAfee, Mary; Skosey, John L.; J, Wallman; Shaw, Andrew; Hanly, W. Carey

doi:10.1016/0161-5890(91)90144-9

Cited by 12 publications

(9 citation statements)

References 16 publications

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“…In the present series of experiments, however, the reduction of KBP below the detection limit in AA was affected only minimally by either indomethacine or ibuprofen. With both drugs the most responsive protein [69] Abnormal glycosylation/post-translational processing/ covalent reaction Glycoforms of a 1 -antichymotrypsin [70] Glycoforms of orosomucoid [71] Galactosylation deficiency in IgG [72,73] Increased content of fucose in IgG [74] Oncofetal epitope (due to differential glycosylation) on fibronectin (from synovial fluid but not serum) [75] Covalent binding of proteoglycans to IgG and albumin from articular cartilage [76] Covalent disulfide binding of IL-1 b to a 2 -M, and its hinhibition by D-penicillamine [77] ( [97] Proteolytically modified insulin-like growth factorbinding proteins [98] was a 2 -M, but the interference on AA effects differed by a factor of three. It thus seems difficult to select predictive markers, and none had actually been singled out even from similar tests in humans.…”

Section: Discussionmentioning

confidence: 99%

Proteins of rat serum V: Adjuvant arthritis and its modulation by nonsteroidal anti-inflammatory drugs

Eberini¹,

Agnello²,

Miller³

et al. 2000

Electrophoresis

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The effect of adjuvant arthritis (AA) on the pattern of rat serum proteins includes the upregulation of haptoglobin, orosomucoid, alpha2-macroglobulin, serine protease inhibitor-3, thiostatin, alpha1-antitrypsin, C-reactive protein, and the downregulation of kallikrein-binding protein, alpha1-inhibitor III, apolipoprotein A-I, alpha2-HS-glycoprotein, albumin, apolipoprotein A-IV, transthyretin and transferrin. Minor changes (+/- 20%) are observed for Gc-globulin, ceruloplasmin, and alpha1-macroglobulin. AA thus grossly resembles the acute inflammatory response elicited by the injection of turpentine, although the changes in the levels of negative acute-phase proteins (APP) are smaller in acute inflammation. Indomethacine and ibuprofen inhibit the effects of arthritis on the synthesis of rat serum proteins in different ways: The former is, on average, three times as effective as the latter. Each drug interferes differently with different proteins. In animals without AA, both nonsteroidal anti-inflammatory drugs (NSAID) mimic the inflammatory pattern to a certain extent, with more effect on the negative than on the positive APPs. Overall, the shifts in serum protein levels parallel changes in inflammatory parameters such as joint swelling and serum interleukin-6 (IL-6) activity. Protein quantitation after two-dimensional electrophoresis (2-DE) reveals some effects of the drugs per se which escape detection by other routine tests.

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Section: Discussionmentioning

confidence: 99%

Proteins of rat serum V: Adjuvant arthritis and its modulation by nonsteroidal anti-inflammatory drugs

Eberini¹,

Agnello²,

Miller³

et al. 2000

Electrophoresis

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“…Differences in levels were found in studies that compared the major techniques, enzyme-linked immunosorbent assay (ELISA), radioimmunoassay (RIA), and bioassays (3,13). Among the factors that have been implicated as causing the differences are compounds known to bind to cytokines, such as serum albumin and ␣2-microglobulin (6,27,32,53), autoantibodies (11,23,31), and soluble receptors that inhibit cytokine activity, i.e., soluble tumor necrosis factor (TNF) receptor types I and II for TNF-␣ (sTNF-RI and sTNF-RII, respectively) (1,3,52).…”

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confidence: 99%

Variables That Affect Assays for Plasma Cytokines and Soluble Activation Markers

Aziz

Nishanian

Mitsuyasu

et al. 1999

Clin Diagn Lab Immunol

131

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Cytokines and soluble immune activation markers that reflect cytokine activities in vivo are increasingly being measured in plasma, serum, and other body fluids. They provide useful diagnostic and prognostic information as well as insight into disease pathogenesis. Assays of neopterin, β2-microglobulin, soluble interleukin-2 receptor, and soluble tumor necrosis factor receptor type II as well as of the cytokines tumor necrosis factor alpha and gamma interferon (IFN-γ) were evaluated by using serum and plasma samples of human immunodeficiency virus (HIV)-positive and HIV-negative subjects. Many factors were found to influence the outcomes of these assays. Substantial differences in apparent levels of analytes were frequently found when enzyme-linked immunosorbent assay (ELISA) kits from different manufacturers were used. In some cases, differences were found in the standards provided by separate manufacturers. Furthermore, the analytic results from different lots of ELISA kits supplied by single manufacturers differed by as much as 50%. The need for uniformity in the standards for quantitative assays was clearly illustrated. International reference standards are available for cytokines but not for soluble cytokine receptors or soluble activation markers. Marker levels in serum or in plasma were similar except those for IFN-γ. Most of the analytes were stable under several storage conditions. Thus, batch testing of frozen stored samples is feasible. The findings indicate that for longitudinal studies, the levels of cytokines and immune activation markers in plasma or serum should be measured by using preverified reagents from one manufacturer. The quality of laboratory performance can have an impact on clinical relevance. Proficiency testing and external quality assurance programs can help to develop the needed consensus.

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“…Recently, a number of naturally occurring IL-1 inhibitors have been described [1,7,10,II,13,15,16]. One ofthese, uromodulin, is an 85,000 mol.…”

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confidence: 99%

“…Uromodulin binds IL-1, but only when IL-1 is adsorbed to plastic [9]. An 18,000-25,000 protein found in urine from febrile patients has been found to block the binding of IL-1 to its receptor [13,14], and 012macroglobulin may regulate IL-1 activity by formation of disulphide bonds with the cytokine [16]. In all cases, the inhibitors do not seem to discriminate between the two major lL-1 species.…”

mentioning

confidence: 99%

IgG Autoantibodies against Interleukin 1α in Sera of Normal Individuals

et al. 1989

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A pool of human sera from healthy blood donors was found to interfere competitively with the binding of 125I-labelled human recombinant interleukin 1 alpha (rIL-1 alpha) to the murine T-cell line EL4. The interference was reversible at the cellular level, and direct binding of the ligand to serum factors was therefore investigated. After preincubation of [125I]rIL-1 alpha with pooled serum, the 125I activity eluted in two peaks from a Sephadex G-75 column. The first was located in the void volume. The second eluted together with monomer rIL-1 alpha. An almost complete displacement of the high molecular weight 125I fraction was achieved with an excess of unlabelled rIL-1 alpha but not with rIL-1 beta. The serum factors binding to [125I]rIL-1 alpha were located in the molecular weight range 100,000-200,000, judged by fractionation on a Sephacryl S-400 column, and the factors were bound to immobilized protein A. Furthermore, [125I]rIL-1 alpha preincubated with serum co-precipitated with a specific rabbit anti-human IgG antibody. Screening of 29 sera from normal individuals showed similar effects in three cases. We conclude that approximately 10% of normal human sera contains detectable IgG autoantibodies to IL-1 alpha.

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Covalent disulfide binding of human IL-1β to α2-macroglobulin: Inhibition by d-penicillamine

Cited by 12 publications

References 16 publications

Proteins of rat serum V: Adjuvant arthritis and its modulation by nonsteroidal anti-inflammatory drugs

Proteins of rat serum V: Adjuvant arthritis and its modulation by nonsteroidal anti-inflammatory drugs

Variables That Affect Assays for Plasma Cytokines and Soluble Activation Markers

IgG Autoantibodies against Interleukin 1α in Sera of Normal Individuals

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