Der humane lösliche Interleukin-6-Rezeptor: Reinigung aus Plasma, Charakterisierung und Nachweis der von einer alternativ gespleißten mRNA translatierten Form
Year: 2004
Type: dissertation
Abstract: The human soluble interleukin-6-receptor: Purification from plasma, characterization and identification of an isoform generated through alternative splicing Soluble receptors for cytokines are soluble forms of their membrane counterparts which bind their ligands with similiar affinities to those of the membrane bound receptors. Two different mechanisms have been found to be responsible for the formation of soluble cytokine receptors. Some soluble receptors are generated by limited proteolysis (shedding, proteolytic cleavage, PC). The second mechanism involves a translation from a differentially spliced mRNA lacking the transmembrane domain (differential mRNA splicing, DS). It has previously been shown that the soluble interleukin-6-receptor (sIL-6R) can be generated by both mechanisms (resulting PC-sIL-6R or DS-sIL-6R). The sIL-6R was purified from human plasma. In a single immunoaffinity purification step a 140000-fold enrichment with a yield of 95% was achieved. The biological activity of the purified soluble receptor was clearly demonstrated by its ability to induce the synthesis of the acute-phase protein alpha-1-antichymotrypsin. It was shown that the sIL-6R isolated from human plasma is recognized by an affinity-purified peptide antibody raised against an amino acid sequence unique for the alternatively spliced isoform.
Source: RWTH Publications (RWTH Aachen)
Authors: Christian Köhne, Peter C. Heinrich
Language: German
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2241042661