David M. Waisman

Dalhousie University

David Waisman is a Professor in the Department of Pathology at Dalhousie University and formerly held a Canada Research Chair in Cancer Research. Renowned for his pioneering work on the pathobiology of cancer, his research focuses on the mechanisms of tumor growth and metastasis, particularly in breast, pancreatic, and lung cancers. His most significant contributions include discovering how the protein S100A10 regulates plasmin production and drives tumor growth, invasion, and metastasis. This discovery has significantly advanced our understanding of cancer cell invasion and opened new possibilities for targeted therapies to inhibit cancer spread. His work also led to the discovery of the protein calreticulin (CRT). It redefined CRT as a key regulator of plasmin-mediated proteolysis in cancer. This finding has revolutionized our understanding of cancer progression. Dr. Waisman has been a faculty member at Dalhousie since 2006.

David M. Waisman

1books edited

3chapters authored

Latest work with IntechOpen by David M. Waisman

Fibrinolysis, the process of breaking down the fibrin network, was reported in 1925 by Fischer, who demonstrated that explants of virally induced chicken tumors rapidly caused lysis of plasma clots, whereas explants of normal tissue did not. This observation provided evidence for the importance of fibrinolysis in cancer. Then, in 1933, Tillett and Garner observed the liquefaction of a fibrin clot by the plasma of many patients who had recovered from acute hemolytic streptococcal infections. These investigators showed that broth cultures of hemolytic streptococci derived from patients could rapidly liquefy normal human fibrin clots. This suggested that fibrinolysis might play a key role in homeostasis, although its regulation mechanism was unknown. Fibrinolysis is now known to be regulated by four components, namely the plasminogen activators that function to convert plasminogen into plasmin to initiate fibrin degradation, such as tissue-type and urokinase-type plasminogen activators, the plasminogen activator inhibitors that block the plasminogen activators, the plasmin inhibitors such as alpha2-antiplasmin, and finally the enzymes that block plasminogen binding sites on fibrin or the endothelial cell surface, such as the thrombin activatable fibrinolysis inhibitor. Originally, fibrinolysis was thought to be only responsible for promoting vascular patency, the failure of which resulted in myocardial infarction and stroke. However, recent studies from multiple laboratories have identified the key role of fibrinolysis in a host of physiological and pathophysiological processes. Most recently, fibrinolysis has been suggested to play a role in forming the premetastatic niche, a hospitable site for future metastases in distal tissues, which is formed by secretions from the primary tumor before the departure of metastatic cancer cells. This book explores the multifaceted and intriguing role of fibrinolysis in several processes, including cancer, cardiovascular disease, neuroinflammation, and infection. The latest advances in fibrinolytic therapies are also discussed, which illustrates the complexity and depth of the field.

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