Pneumocystosis in a patient with rheumatoid arthritis on adalimumab therapy: a case-based review

Kounatidis, Dimitris C.; Papadimitropoulos, Vasileios; Avramidis, Konstantinos; Plenga, Evgenia; Tsiara, Ioanna; Avgoustou, Elena; Vallianou, Natalia; Vassilopoulos, Dimitrios

doi:10.1007/s00296-023-05483-3

Cited by 2 publications

(2 citation statements)

References 14 publications

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“…Recently, we have identified peptide fragments of the TNFR1 ligand, the Tag7 protein, which performs only one function: either the inhibition of the TNF interaction with the receptor, or the cytotoxic effect on cells in complexes with the Hsp70 protein [34]. It has been shown that anti-TNF antibodies that reduce TNF levels result in a decrease in the development of rheumatoid arthritis and sepsis [28].…”

Section: Discussionmentioning

confidence: 99%

“…One of them is the use of antibodies to either TNF of TNFR1 proteins. This approach is used in the treatment of several diseases, for example, rheumatoid arthritis, and has several advantages, such as high specificity and a sufficient lifetime of the active molecules in the blood of the patients, but also several drawbacks, such as high costs and autoimmune problems [28]. Another approach is the identification of active peptide fragments of regulatory proteins that model the functional action of full-sized proteins.…”

Section: Introductionmentioning

confidence: 99%

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The 12-Membered TNFR1 Peptide, as Well as the 16-Membered and 6-Membered TNF Peptides, Regulate TNFR1-Dependent Cytotoxic Activity of TNF

Yurkina,

Romanova,

Tvorogova

et al. 2024

IJMS

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Understanding the exact mechanisms of the activation of proinflammatory immune response receptors is very important for the targeted regulation of their functioning. In this work, we were able to identify the sites of the molecules in the proinflammatory cytokine TNF (tumor necrosis factor) and its TNFR1 (tumor necrosis factor receptor 1), which are necessary for the two-stage cytotoxic signal transduction required for tumor cell killing. A 12-membered TNFR1 peptide was identified and synthesized, interacting with the ligands of this receptor protein’s TNF and Tag7 and blocking their binding to the receptor. Two TNF cytokine peptides interacting with different sites of TNFR1 receptors were identified and synthesized. It has been demonstrated that the long 16-membered TNF peptide interferes with the binding of TNFR1 ligands to this receptor, and the short 6-membered peptide interacts with the receptor site necessary for the transmission of a cytotoxic signal into the cell after the ligands’ interaction with the binding site. This study may help in the development of therapeutic approaches to regulate the activity of the cytokine TNF.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%