At Michigan State University, researchers in the Luyendyk Lab are uncovering a hidden layer of biology that could reshape how we understand — and treat — trauma, wound healing, and chronic disease. Their latest work reveals a surprising twist in the story of how blood clots form and function, and could lead to new therapies for conditions ranging from traumatic tissue injury to pathologic blood clots (known as thrombosis).
Blood clotting is a vital defense mechanism within the body. When blood vessels are injured, a protein known as fibrin forms a mesh that stops bleeding and begins the healing process. The structure of this mesh, the blood clot, is stabilized by an enzyme called Factor XIII.
“Factor XIII crosslinks fibrin together like bolting pieces of lumber together,” says Nana Kwame Kwabi Boateng, a PhD student in the Luyendyk Lab.
Luyendyk’s team discovered that another enzyme, tissue transglutaminase (TG2), plays a previously unknown role in reshaping fibrin’s structure during trauma. “We found that TG2 bolts fibrin together differently than Factor XIII does,” says Boateng. “It’s like a completely different blueprint in trauma clots.”