Related Experiment Video
Updated: May 10, 2026

Intravital Imaging of Neutrophil Priming Using IL-1β Promoter-driven DsRed Reporter Mice
Published on: June 22, 2016
IL-1Ra and its delivery strategies: inserting the association in perspective
Muhammad Sajid Hamid Akash1, Kanwal Rehman, Shuqing Chen
1Institute of Pharmacology, Toxicology and Biochemical Pharmaceutics College of Pharmaceutical Sciences, Zhejiang University, Hangzhou, China, sajidakash@gmail.com.
Abstract:
Interleukin-1 receptor antagonist (IL-1Ra) is a naturally occurring anti-inflammatory antagonist of interleukin-1 family of pro-inflammatory cytokines. The broad spectrum anti-inflammatory effects of IL-1Ra have been investigated against various auto-immune diseases such as diabetes mellitus, rheumatoid arthritis. Despite of its outstanding broad spectrum anti-inflammatory effects, IL-1Ra has short biological half-life (4-6 h) and to cope with this problem, up till now, many delivery strategies have been applied either to extend the half-life and/or prolong the steady-state sustained release of IL-1Ra from its target site. Here in our present paper, we have provided an overview of all approaches attempted to prolong the duration of therapeutic effects of IL-1Ra either by fusing IL-1Ra using fusion protein technology to extend the half-life and/or development of new dosage forms using various biodegradable polymers to prolong its steady-state sustained release at the site of administration. These approaches have been characterized by their intended impact on either in vitro release characteristics and/or pharmacokinetic and pharmacodynamic parameters of IL-1Ra. We have also compared these delivery strategies with each other on the basis of bioactivity of IL-1Ra after fusion with fusion protein partner and/or encapsulation with biodegradable polymer.
Related Concept Videos
T Cell Types and Functions
Th1 cells stimulate dendritic cells to express necessary co-stimulatory molecules on their surfaces for...
Activation of Integrins
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
The JAK-STAT Signaling Pathway
Intracellular Signaling Affects Focal Adhesions
Some...
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
NF-κB-dependent Signaling Pathway
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...

