Osteopontin (OPN) is a multi-functional protein that is involved in various cellular processes such as cell adhesion, migration, and signaling. There is a single conserved thrombin cleavage site in OPN that, when cleaved, yields two fragments with different properties from full-length OPN. In cancer, OPN has tumor-promoting activity and plays a role in tumor growth and metastasis. High levels of OPN expression in cancer cells and tumor tissue are found in various types of cancer, including breast, lung, prostate, ovarian, colorectal, and pancreatic cancer, and are associated with poor prognosis and decreased survival rates. OPN promotes tumor progression and invasion by stimulating cell proliferation and angiogenesis and also facilitates the metastasis of cancer cells to other parts of the body by promoting cell adhesion and migration. Furthermore, OPN contributes to immune evasion by inhibiting the activity of immune cells. Thrombin cleavage of OPN initiates OPN's tumor-promoting activity, and thrombin cleavage fragments of OPN down-regulate the host immune anti-tumor response.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10340489 | PMC |
| http://dx.doi.org/10.3390/cancers15133480 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Dependence of clot structure and fibrinolysis on apixaban and clotting activator.
Res Pract Thromb Haemost
November 2024
Department of Biomedical Engineering, Rutgers University, Piscataway, New Jersey, USA.
Background: Anticoagulants prevent the formation of potentially fatal blood clots. Apixaban is a direct oral anticoagulant that inhibits factor (F)Xa, thereby impeding the conversion of prothrombin into thrombin and the formation of blood clots. Blood clots are held together by fibrin networks that must be broken down (fibrinolysis) to restore blood flow.
View Article and Find Full Text PDFEntropy-driven self-assembled enzyme-DNA nanomatrix cascade DNAzyme-CRISPR/cas system for multiplexed enhancement of self-powered sensing platform for protein detection.
Int J Biol Macromol
December 2024
Analysis and Test Center, Chinese Academy of Tropical Agricultural Sciences, Haikou 571101, China. Electronic address:
Clustered Regularly Interspaced Short Palindromic Repeats and CRISPR-associated Proteins (CRISPR/Cas) system can accurately identify and cleave target DNA sequences, while the effective combination of DNA nanomatrix and entropy-driven self-assembled enzymes can significantly enhance the sensitivity, stability, and diversified functionality of sensors through highly ordered molecular arrangement and spontaneous efficient assembly processes. Herein, a carbon-encapsulated MoS hollow nanorod (C-MoS) with excellent conductivity and multiple active sites is used to construct bioanode of biofuel cell by integrating it with an entropy-driven self-assembled enzyme-DNA nanomatrix cascade DNAzyme-CRISPR/Cas system. When thrombin binds aptamer, it exposes the trigger strand on the anode, initiating chain displacement.
View Article and Find Full Text PDFBack to basics: the coagulation pathway.
Blood Res
October 2024
Daisy Hill Hospital, 5 Hospital Road, Newry, BT35 8DR, UK.
The classic coagulation cascade model of intrinsic and extrinsic coagulation pathways, i.e. contact activation pathway and tissue factor pathway, has been widely modified.
View Article and Find Full Text PDFNovel Deep Sea Isoindole Alkaloid FGFC1 Exhibits Its Fibrinolytic Effects by Inhibiting Thrombin-Activatable Fibrinolysis Inhibitor.
Pharmaceuticals (Basel)
October 2024
Department of Marine Bio-Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China.
Background: The thrombin-activatable fibrinolysis inhibitor (TAFI) is an important regulator in the balance between blood clot formation (coagulation) and dissolution (fibrinolysis), which is mainly activated by thrombin bonded with thrombomodulin (TM).
Methods: In this study, the investigation focused on the unique target TAFI of fungi fibrinolytic compound 1 (FGFC1), a novel fibrinolytic compound sourced from the deep sea. In this sense, the regulation of TAFI by FGFC1, in comparison to established TAFI inhibitors such as DS-1040 and PCTI in hPPP, was investigated, which was validated through the molecular docking of FGFC1 to TAFI.
Factor XIII Activation Peptide Residues Play Important Roles in Stability, Activation, and Transglutaminase Activity.
Biochemistry
November 2024
Department of Chemistry, University of Louisville, Louisville, Kentucky 40292, United States.
Article Synopsis
- The study investigates the activation and stability of factor XIII subunit FXIII-A, focusing on its unique activation peptide (AP) and how specific mutations affect its function.
- Recombinant FXIII-A AP variants were created to analyze their role in thrombin activation and transglutaminase activity, using techniques like SDS-PAGE and mass spectrometry for assessment.
- Key findings highlight that certain mutations to the activation peptide impair FXIII-A stability and activation, indicating that specific amino acid interactions are essential for its functionality in the coagulation process.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!