Interleukin-6-interleukin-11 receptor chimeras reveal ionomycin-induced proteolysis beyond ADAM10.
FEBS Lett
; 595(24): 3072-3082, 2021 12.
Article
in En
| MEDLINE
| ID: mdl-34778975
ABSTRACT
Interleukin-6 (IL-6) and interleukin-11 (IL-11) are two important pleiotropic cytokines, both of which signal through a homodimer of the ß-receptor gp130. Specificity is gained through the unique, nonsignaling α-receptors IL-6R and IL-11R. Soluble variants of IL-6R and IL-11R also exist. Both membrane-bound receptors can be cleaved by the metalloprotease ADAM10. Here, we use ten different chimeric receptors consisting of different parts of IL-6R and IL-11R and analyze their susceptibility toward cleavage by ADAM10. As expected, all chimeras are substrates of ADAM10. However, we observed that cleavage of chimeric receptors containing the stalk region of the IL-11R could be blocked by the protease inhibitor GI (selective for ADAM10), but not by the protease inhibitor GW (selective for both ADAM10 and ADAM17), suggesting that another protease besides ADAM10 is involved in cleavage of these chimeras.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Recombinant Fusion Proteins
/
Ionomycin
/
Receptors, Interleukin-11
/
Proteolysis
/
ADAM10 Protein
Limits:
Humans
Language:
En
Journal:
FEBS Lett
Year:
2021
Document type:
Article
Affiliation country:
Germany