Rat Interleukin-2 Immunoglobulin M Fusion Proteins Are Cytotoxic in Vitro for Cells Expressing the Il-2 Receptor and Can Abolish Cell-Mediated Immunity in Vivo

Wm, Bogers; Lang, François; Ke, Parker; B, Le Mauff; Anegón, I.; Jacques, Yannick; Jp, Soulillou

doi:10.1097/00007890-199410270-00013

Cited by 8 publications

(3 citation statements)

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“…Both IgG and IgM based IL-2 fusion proteins were able to suppress sheep red blood cell (SRBC)-induced DTH responses in rodents (8,14). An IL-15 mutant-IgG2a fusion was also capable of suppressing the DTH response, with MBSA as the immunogen, ostensibly through targeting the IL-15 receptor ␣ chain present on activated T cells (15).…”

Section: Discussionmentioning

confidence: 99%

Suppression of the Cell-Mediated Immune Response by a Fas-Immunoglobulin Fusion Protein

Shen

Young²,

Lipman³

2006

Transplantation

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Section: Discussionmentioning

confidence: 99%

Suppression of the Cell-Mediated Immune Response by a Fas-Immunoglobulin Fusion Protein

Shen

Young²,

Lipman³

2006

Transplantation

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“…However, adverse reactions associated with murine proteins limited long-term efficacy, as well as the development of human anti-murine antibodies are current limitations of this approach. An approach to inhibit immune functions more selectively became feasible with the application of genetically engineered fusion proteins in animal models of organ transplantation or chronic inflammation [17][18][19][20]. For this approach cytokines or extracellular domains of integral membrane proteins were used to replace the variable regions of immunoglobulins.…”

Section: Schlüsselwörter: Zytokinfusionsproteine -Entzündung -Chronismentioning

confidence: 99%

Modulation of gastrointestinal inflammation by chimeric proteins in experimental models

Stallmach

Wittig²,

Zeitz³

2000

Z Gastroenterol

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Conventional drug therapy in patients with chronic gastrointestinal inflammation is clinically effective in the majority of patients. However, in a relevant group of patients with highly active disease refractory to conventional drugs and for patients with severe side effects new therapeutic strategies are necessary. An advanced understanding of the immune mechanisms underlying chronic diseases resulted in the possibility to use chimeric proteins, in which the variable domains of an immunoglobulin are replaced by extracellular domains of cell surface molecules or cytokines for specific immunomodulation. The immunomodulating effects of chimeric proteins such as CTLA-4-IgG, interleukin-10-IgG, IL-2-IgG or tumour necrosis factor (TNF)-receptor IgG have been proven beneficial in a variety of in vitro and in vivo models of chronic gastrointestinal inflammation and autoimmune diseases. It thus seems likely that genetically engineered fusion proteins targeting specific elements of the immune response may become an essential element in new clinical treatment protocols.

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“…Through molecular engineering, proteins can be altered to enhance their bioactivities. Fusion proteins, designed to combine antibodies with cytokines (2,3,5,6,13,16,17,19), antibodies with cytokine receptors (1), or cytokines with toxins (8), are currently being evaluated in preclinical and clinical studies (18). The ch14.18-interleukin 2 (IL-2) and hu14.18-IL-2 proteins are two such engineered, antitumor antibodycytokine fusion proteins (3).…”

mentioning

confidence: 99%

Specific Enzyme-Linked Immunosorbent Assays for Quantitation of Antibody-Cytokine Fusion Proteins

Gan

Kendra²,

Ricci

et al. 1999

Clin Diagn Lab Immunol

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Preliminary testing has shown in vitro and in vivo that antitumor activity can be obtained with fusion proteins linking tumor-reactive monoclonal antibodies to cytokines, such as granulocyte-macrophage colony-stimulating factor or interleukin 2 (IL-2). Preclinical and clinical testing of these reagents requires their in vitro and in vivo quantitation and pharmacokinetic evaluation. We have focused on the detection of a fusion protein which links one human IL-2 molecule to the carboxy terminus of each heavy chain of the tumor-reactive human-mouse chimeric anti-GD2 antibody, ch14.18. We have developed enzyme-linked immunosorbent assays (ELISAs) to evaluate intact tumor-reactive fusion proteins. By these ELISAs we can reliably measure nanogram quantities of intact ch14.18-IL-2 fusion protein and distinguish the intact protein from its components (ch14.18 and IL-2) in buffer, mouse serum, and human serum with specificity and reproducibility. The measurement of intact ch14.18-IL-2 fusion protein is not confounded by free IL-2 or free ch14.18 when 100 ng or less of total immunoglobulin per ml is used during the assay procedure. Our results indicate that these ELISAs are suitable for preclinical and clinical testing and with slight modifications are applicable to the analysis of a variety of other fusion proteins.

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Rat Interleukin-2 Immunoglobulin M Fusion Proteins Are Cytotoxic in Vitro for Cells Expressing the Il-2 Receptor and Can Abolish Cell-Mediated Immunity in Vivo

Cited by 8 publications

References 0 publications

Suppression of the Cell-Mediated Immune Response by a Fas-Immunoglobulin Fusion Protein

Suppression of the Cell-Mediated Immune Response by a Fas-Immunoglobulin Fusion Protein

Modulation of gastrointestinal inflammation by chimeric proteins in experimental models

Specific Enzyme-Linked Immunosorbent Assays for Quantitation of Antibody-Cytokine Fusion Proteins

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