Plasminogen and Plasmin can Bind to Human T Cells and Generate Truncated CCL21 that Increases Dendritic Cell Chemotactic Responses
Posted by Adam Awdish on
Human Alpha 2 Antiplasmin Purified Lyophilized from Innovative Research was used in the following study:
Evert J. Loef, Hilary M. Sheppard, Nigel P. Birch, Rod Dunbar
Journal of Biological Chemistry
June 9, 2022
Plasmin, a broad-spectrum protease that is highly regulated, is formed from plasminogen. This normally occurs in the blood, as plasminogen is found in high concentrations in circulation where it’s converted to plasmin by plasminogen activators. There are also high levels of α2-antiplasmin in circulation, which is a rapid inhibitor of plasmin activity.
Researchers in this study showed in earlier work that T cells could activate plasmin, however, they don’t express plasminogen on their own. In this study, the researchers found that T cells express plasminogen receptors and then bind to plasminogen on their cell surface. Following this, they carry the plasminogen to tissues where the T cells were activated, subsequently activating the plasminogen, and converting it to plasmin.
The researchers wanted to understand what the consequences of plasmin generation outside of circulation were, so they investigated its effect on chemokine ligand 21 (CCL21). They found that plasmin bound by T cells cleaves CCL21 and increases the chemotactic response of monocyte-dendritic cells toward increased CCL21 concentrations.
By carrying plasminogen to peripheral tissues and activating it and generating plasmin outside of circulation, this system can avoid the plasmin inhibitor α2-antiplasmin, creating a powerful proteolytic system of plasmin activation. The researchers suggest that this system may strongly modulate chemokine responses in peripheral tissues.
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