IL-17A通过p38MAPK通路抑制巨噬细胞ABCA1蛋白的降解

Objective: To investigate the underlying mechanisms and intracellular signaling of up-regulating adenosine triphosphate binding cassette transporter A1 (ABCA1) by interleukin-17A (IL-17) in macrophages. Methods: Mouse RAW264.7 cells were treated with 20ng/mL of IL-17A. The protein expressions of ABCA1 and p-p38MAPK were detected using Western blot. The ubiquitination level of ABCA1 was detected using Co-immunoprecipitation. Results: IL-17A increased the expression of ABCA1 at the protein level, but not at the mRNA level. IL-17A reduced the degradation of ABCA1 protein. IL-17A attenuated binding of ABCA1 to ubiquitin. SB203580, p38MAPK inhibitor, reversed the decrease of ubiquitination and increased expression of ABCA1 protein induced by IL-17A in macrophages. Conclusion: IL-17A increases the expression of ABCA1 protein by inhibiting its degradation through p38MAPK pathway in macrophages.