PTPN7 acts preferentially on tyrosine-phosphorylated MAPK1 (Mitogen-Activated Protein Kinase 1). This protein plays a crucial role in the regulation of T and B-lymphocyte development and signal transduction . The non-catalytic N-terminus of PTPN7 can interact with MAP kinases and suppress their activities, which is essential for the regulation of T cell antigen receptor (TCR) signaling .
PTPN7 is preferentially expressed in a variety of hematopoietic cells and is an early response gene in lymphokine-stimulated cells . The expression of PTPN7 is regulated by various stimuli, including lipopolysaccharide (LPS), which acts as an endotoxin and elicits strong immune responses in animals . Stimulation of RAW 264.7 cells with LPS leads to a transient decrease in the levels of PTPN7 mRNA and protein .
PTPN7 has been shown to act as a negative regulator of pro-inflammatory TNF-α (Tumor Necrosis Factor-alpha) production in macrophages . Overexpression of PTPN7 inhibits LPS-stimulated production of TNF-α, while knock-down of PTPN7 increases TNF-α production . This indicates that PTPN7 plays a critical role in modulating the inflammatory response in macrophages by negatively regulating the extracellular signal-regulated kinase 1/2 (ERK1/2) and p38 pathways .
Given its role in regulating immune responses and cell signaling, PTPN7 is of significant interest in the context of diseases such as juvenile myelomonocytic leukemia . Understanding the function and regulation of PTPN7 can provide insights into potential therapeutic targets for treating immune-related disorders and certain types of cancer.