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Plasminogen receptor with a C-terminal lysine (PLGRKT) is an integral transmembrane protein that exposes a lysine at its C-terminus, enabling cell-surface binding and activation of plasminogen by plasminogen activators such as urokinase and tissue-type plasminogen activator. It is highly expressed on monocytes, macrophages, and some lymphocytes, and is upregulated during cell differentiation and inflammatory responses. PLGRKT plays a key role in regulating macrophage migration and recruitment, promotes matrix metalloproteinase activation, and participates in wound healing, tissue remodeling, cancer invasion/proliferation, and possibly metabolic regulation. While no drugs currently target PLGRKT directly, its cell-surface localization and critical role in plasminogen activation make it a promising therapeutic target, especially in inflammation and cancer.
Drugs or antibodies blocking PLGRKT prevent plasminogen binding and activation at the cell surface, thereby inhibiting downstream plasmin-dependent processes like cell migration, invasion, and cytokine release. Antagonists may reduce inflammation or metastasis by limiting macrophage recruitment and/or matrix degradation. Inhibitors of plasminogen activation (e.g., EACA) act by blocking lysine-binding sites (which include the C-terminal lysine on PLGRKT).
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