Cancer and the prothrombotic state

Lip, Gregory Y.H.; Chin, Bernard S P; Blann, Andrew D.

doi:10.1016/s1470-2045(01)00619-2

Cited by 338 publications

(267 citation statements)

References 57 publications

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“…As a consequence, cancer patients commonly have an elevated turnover of platelets in their circulation and increased risk of thrombotic occlusion of vessels. 146 In a recent study from the group of R.O. Hynes it was demonstrated that direct contact between tumor cells and platelets induces EMT (Fig.…”

Section: Platelet-derived Tgfb and Nf-kb Signaling Asmentioning

confidence: 99%

Reprogramming during epithelial to mesenchymal transition under the control of TGFβ

Tan¹,

Olsson

Moustakas

2014

Cell Adhesion & Migration

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Epithelial-mesenchymal transition (EMT) refers to plastic changes in epithelial tissue architecture. Breast cancer stromal cells provide secreted molecules, such as transforming growth factor b (TGFb), that promote EMT on tumor cells to facilitate breast cancer cell invasion, stemness and metastasis. TGFb signaling is considered to be abnormal in the context of cancer development; however, TGFb acting on breast cancer EMT resembles physiological signaling during embryonic development, when EMT generates or patterns new tissues. Interestingly, while EMT promotes metastatic fate, successful metastatic colonization seems to require the inverse process of mesenchymal-epithelial transition (MET). EMT and MET are interconnected in a timedependent and tissue context-dependent manner and are coordinated by TGFb, other extracellular proteins, intracellular signaling cascades, non-coding RNAs and chromatin-based molecular alterations. Research on breast cancer EMT/MET aims at delivering biomolecules that can be used diagnostically in cancer pathology and possibly provide ideas for how to improve breast cancer therapy.

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Section: Platelet-derived Tgfb and Nf-kb Signaling Asmentioning

confidence: 99%

Reprogramming during epithelial to mesenchymal transition under the control of TGFβ

Tan¹,

Olsson

Moustakas

2014

Cell Adhesion & Migration

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“…nattokinase [7] and lumbrokinase [8] which can directly degrade the fibrin of blood clots, thereby dissolving the thrombi rapidly and completely [9]. However, these enzymes are expensive and patients may suffer from undesirable side effects such as gastrointestinal bleeding, allergic reaction, and resistance to repercussion [10,11]. Therefore, antithrombotic, anticoagulant and thrombolytic reagents from various sources have been investigated [12].…”

Section: Introductionmentioning

confidence: 99%

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

et al. 2016

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a b s t r a c tPlant serine proteases have been widely used in food science and technology as well as in medicine. In this sense, several plant serine proteases have been proposed as potential anti-coagulants and antiplatelet agents. Previously, we have reported the purification and identification of a plant serine protease from Solanum tuberosum leaves. This potato enzyme, named as StSBTc-3, has a molecular weight of 72 kDa and it was characterized as a subtilisin like protease. In this work we determine and characterize the biochemical and medicinal properties of StSBTc-3. Results obtained show that, like the reported to other plant serine proteases, StSBTc-3 is able to degrade all chains of human fibrinogen and to produces fibrin clot lysis in a dose dependent manner. The enzyme efficiently hydrolyzes b subunit followed by partially hydrolyzed a and g subunits of human fibrinogen. Assays performed to determine StSBTc-3 substrate specificity using oxidized insulin b-chain as substrate, show seven cleavage sites: Asn3-Gln4; Cys7-Gly8; Glu13-Ala14; Leu15-Tyr16; Tyr16-Leu17; Arg22-Gly23 and Phe25-Tyr26, all of them were previously reported for other serine proteases with fibrinogenolytic activity. The maximum StSBTc-3 fibrinogenolytic activity was determined at pH 8.0 and at 37 C. Additionally, we demonstrate that StSBTc-3 is able to inhibit platelet aggregation and is unable to exert cytotoxic activity on human erythrocytes in vitro at all concentrations assayed. These results suggest that StSBTc-3 could be evaluated as a new agent to be used in the treatment of thromboembolic disorders such as strokes, pulmonary embolism and deep vein thrombosis.

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“…In patients with cancer, each of the three components of Virchow's triad that predispose thrombus formation is altered and thereby induces a prothrombotic state [1]. This can explain the many venous thrombo-embolic (VTE) complications seen in patients with cancer.…”

Section: Discussionmentioning

confidence: 99%