Psoriasis |
(1) p38 MAPK is phosphorylated in lesional psoriatic epidermis |
[20–23] |
(2) Phosphorylated p38 is widely detectable in the keratinocyte nuclei indicative of the kinase strong participation in active gene expression |
[21] |
(3) Among the p38 MAPK isoforms, p38alpha, p38beta, and p38delta are detectable in lesional psoriatic skin |
[20] |
(4) p38-activated kinases MK-2 and MSK-1 are also phosphorylated in psoriatic lesional skin and regulate the production of proinflammatory cytokines such as TNF-α
|
[23–25] |
(5) Dual-specificity phosphatase 1 (DUSP1) is an important negative regulator of p38 MAPK activity DUSP1 mRNA expression is downregulated in psoriatic skin lesions compared with paired samples of nonlesional psoriatic skin |
[26] |
(6) p38-MAPK induced Ser727 phosphorylation of STAT-1 and STAT-3 is detected in psoriatic skin |
[27, 28] |
(7) p38-MAPK-dependent expression of cathelicidin antimicrobial peptide, human β-defensin-2, human β-defensin-3, S100A7, and S100A8 |
[29, 30] |
|
Psoriatic arthritis |
(1) Phosphorylated p38 MAPK is detectable in both lining and sublining synovial area |
[31] |
(2) P38 positive cells are also detected in inflammatory infiltrates, in perivascular zones, and in the endothelium |
[31] |
(3) IL-36α is upregulated in PsA and RA synovia and leads to IL-6 and IL-8 production by synovial fibroblasts through p38/NFkB activation |
[32] |