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SPP1-ITGα5/β1 Accelerates Calcification of Nucleus Pulposus Cells by Inhibiting Mitophagy via Ubiquitin-Dependent PINK1/PARKIN Pathway Blockade.
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Department of Orthopedic, Qilu Hospital of Shandong University, Jinan, Shandong, 250012, China.
Low back pain (LBP) caused by nucleus pulposus degeneration and calcification leads to great economic and social burden worldwide. Unexpectedly, no previous studies have demonstrated the association and the underlying mechanism between nucleus pulposus tissue degeneration and calcification formation. Secreted Phosphoprotein 1 (SPP1) exerts crucial functions in bone matrix mineralization and calcium deposition.
View Article and Find Full Text PDFThe novel ECM protein SNED1 mediates cell adhesion via the RGD-binding integrins α5β1 and αvβ3.
J Cell Sci
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Department of Physiology and Biophysics, University of Illinois Chicago, Illinois, 60612, USA.
The extracellular matrix (ECM) is a complex meshwork comprising over 100 proteins. It serves as an adhesive substrate for cells and, hence, plays critical roles in health and disease. We have recently identified a novel ECM protein, SNED1, and have found that it is required for neural crest cell migration and craniofacial morphogenesis during development and in breast cancer, where it is necessary for the metastatic dissemination of tumor cells.
View Article and Find Full Text PDFO-GlcNAcylation stabilized WTAP promotes GBM malignant progression in an N6-methyladenosine-dependent manner.
Neuro Oncol
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Department of Neurosurgery, Qilu Hospital of Shandong University, Cheeloo College of Medicine and Institute of Brain and Brain-Inspired Science, Shandong University, Jinan 250012, Shandong, China.
Background: Interactions between mesenchymal glioblastoma stem cells (MES GSCs) and myeloid-derived macrophages (MDMs) shape the tumor-immunosuppressive microenvironment (TIME), promoting the progression of glioblastoma (GBM). N6-methyladenosine (m6A) plays important roles in the tumor progression. However, the mechanism of m6A in shaping the TIME of GBM remains elusive.
View Article and Find Full Text PDFA Novel P-III Metalloproteinase from Venom Degrades Extracellular Matrix Proteins, Inhibits Platelet Aggregation, and Disrupts Endothelial Cell Adhesion via α5β1 Integrin Receptors to Arginine-Glycine-Aspartic Acid (RGD)-Containing Molecules.
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Laboratório de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paraná, UFPR, Curitiba 81531-980, Brazil.
Article Synopsis
- Viperid snake venoms contain metalloproteinases like barnettlysin-III (Bar-III), which cause bleeding and disrupt blood clotting and tissue integrity in victims.
- Bar-III, a specific type of metalloproteinase, has been characterized in terms of its properties, including its activity being enhanced by calcium and inhibited by zinc, and its ability to degrade important blood and tissue proteins.
- The study also highlights Bar-III’s effects on platelets and endothelial cells, suggesting that it affects platelet aggregation and cell adhesion, providing insights that could lead to new treatments for snakebite envenomation.
In the heart, cell-matrix and cell-cell adhesions reorganize in response to increased cardiac demand and growth to promote cardiomyocyte maturation. Vinculin, a mechanosensitive adaptor protein, links filamentous actin to cell-matrix and cell-cell adhesions and is thus positioned to regulate adhesion reorganization. However, how the two adhesion systems are coordinated in the heart, and the role of vinculin in this process is poorly understood.
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