Anticytokine Therapy in Autoimmune Diseases.

Nishimoto, Norihiro; Kishimoto, Tadamitsu; Yoshizaki, Kazuyuki

doi:10.2169/internalmedicine.38.178

Cited by 17 publications

(13 citation statements)

References 28 publications

(16 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, with the rise of biotherapies, IL-6R antibodies have turned into the center of interest to block B-cell activity in autoimmune diseases (34). A variety of anti-IL-6R antibodies have already been applied for the treatment of autoimmune diseases (35) such as rheumatoid arthritis, systemic onset juvenile idiopathic arthritis (JIA) adult Still's disease, Castleman's disease, and Crohn's disease (35).…”

Section: Discussionmentioning

confidence: 99%

Epidermal loss of JunB leads to a SLE phenotype due to hyper IL-6 signaling

Pflegerl

Vesely

Hantusch

et al. 2009

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

Self Cite

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Epidermal loss of JunB leads to a SLE phenotype due to hyper IL-6 signaling

Pflegerl

Vesely

Hantusch

et al. 2009

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…Abnormal IL-6 production is associated with a variety of diseases (2) such as rheumatoid arthritis (3), AIDS (4,5), osteoporosis (6,7), psoriasis (8), multiple myeloma (9, 10) and Kaposi's sarcoma (11). Thus the interactions between IL-6 and its associated receptors, the transmembrane glycoproteins IL-6R and gp130 (12), present an attractive target for therapeutic antagonists (13). IL-6 signaling is known to proceed via initial binding of IL-6 to the IL-6R to form a binary 1:1 complex.…”

mentioning

confidence: 99%

Characterization of an Antagonist Interleukin-6 Dimer by Stable Isotope Labeling, Cross-linking, and Mass Spectrometry

Taverner

Hall

O’Hair

et al. 2002

Journal of Biological Chemistry

110

101

View full text Add to dashboard Cite

The homodimeric form of a recombinant cytokine interleukin-6 (IL-6 D ) is known to antagonize IL-6 signaling. In this study, spatially proximal residues between IL-6 chains in IL-6 D were identified using a method for specific recognition of intermolecular cross-linked peptides. Our strategy involved mixing 1:1 15 N-labeled and unlabeled ( 14 N) protein to form a mixture of isotopically labeled and unlabeled homodimers, which was chemically cross-linked. This cross-linked IL-6 D was subjected to proteolysis by trypsin and the generated peptides were analyzed by electrospray ionization time-of-flight mass spectrometry (

show abstract

“…Although in some situations they play a part in pathogenesis, e.g., in autoimmune and allergic diseases (5,6), some cytokines are used as therapeutic agents to treat diseases (7)(8)(9). However, it seems unlikely that all the properties of a given cytokine determined from in vitro studies are important, or at any rate equally important, in vivo.…”

mentioning

confidence: 99%