The cAMP Pathway Amplifies Early MyD88-Dependent and Type I Interferon-Independent LPS-Induced Interleukin-10 Expression in Mouse Macrophages

Autor: Orna Ernst, Yifat Glucksam-Galnoy, Muhammad Athamna, Iris Ben-Dror, Hadar Ben-Arosh, Galit Levy-Rimler, Iain D. C. Fraser, Tsaffrir Zor

Publikováno v: Mediators of Inflammation, Vol 2019 (2019)

Interleukin-10 (IL-10) is a key anti-inflammatory cytokine, secreted by macrophages and other immune cells to attenuate inflammation. Autocrine type I interferons (IFNs) largely mediate the delayed expression of IL-10 by LPS-stimulated macrophages. W

Externí odkaz: https://doaj.org/article/886b6554b65c4643a00abb21d2041f34

The cAMP Pathway Amplifies Early MyD88-Dependent and Type I Interferon-Independent LPS-Induced Interleukin-10 Expression in Mouse Macrophages

Autor: Galit Levy-Rimler, Muhammad Athamna, Yifat Glucksam-Galnoy, Orna Ernst, Hadar Ben-Arosh, Iain D. C. Fraser, Tsaffrir Zor, Iris Ben-Dror

Publikováno v: Mediators of Inflammation, Vol 2019 (2019)
Mediators of Inflammation

Interleukin-10 (IL-10) is a key anti-inflammatory cytokine, secreted by macrophages and other immune cells to attenuate inflammation. Autocrine type I interferons (IFNs) largely mediate the delayed expression of IL-10 by LPS-stimulated macrophages. W

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a89150bf03ca7de0edf70399f8ebfc48
https://doaj.org/article/886b6554b65c4643a00abb21d2041f34

Synergistic IL-10 induction by LPS and the ceramide-1-phosphate analog PCERA-1 is mediated by the cAMP and p38 MAP kinase pathways

Autor: Galit Levy-Rimler, Orna Ernst, Michael M. Meijler, Yifat Glucksam, Tsaffrir Zor, Dorit Avni, Meir Goldsmith

Publikováno v: Molecular Immunology. 46:1979-1987

Expression of the anti-inflammatory cytokine IL-10 can be induced either by TLR agonists such as lipopolysaccharide (LPS), or by various endogenous stimuli, in particular those acting via a cAMP-dependent signaling pathway. We have previously reporte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1f97d29fb51e6fb72c296139e8f8853
https://doi.org/10.1016/j.molimm.2009.03.009

Type I chaperonins: not all are created equal

Autor: Abdussalam Azem, Rachel E. Bell, Nir Ben-Tal, Galit Levy-Rimler

Publikováno v: FEBS Letters. 529:1-5

Type I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts. Since their discovery, the bacterial chaperonins have provided an excellent model system for inve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a82fd3b14f177d9824c9f6bf31440d3
https://doi.org/10.1016/s0014-5793(02)03178-2

Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin

Autor: Peter A. Lund, Amir Pri-Or, Peter Bross, Abdussalam Azem, Shahar Nisemblat, Avital Parnas, Tsaffrir Zor, Galit Levy-Rimler, Celeste Weiss

Publikováno v: Parnas, A, Nisemblat, S, Weiss, C, Levy-Rimler, G, Pri-Or, A, Zor, T, Lund, P A, Bross, P & Azem, A 2012, ' Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin ', P L o S One, vol. 7, no. 12, pp. e50318 . https://doi.org/10.1371/journal.pone.0050318
PLoS ONE
PLoS ONE, Vol 7, Iss 12, p e50318 (2012)

Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a75b303cc3db4f91e77b2f0e37ac10ca
https://pure.au.dk/portal/da/publications/identification-of-elements-that-dictate-the-specificity-of-mitochondrial-hsp60-for-its-cochaperonin(5fb9ecb4-b870-48ae-b192-d84e21469783).html