Publications by authors named "T D Kovalenko"
Extensive neovascularization is a hallmark of glioblastoma (GBM). In addition to supplying oxygen and nutrients, vascular endothelial cells provide trophic support to GBM cells via paracrine signaling. Here we report that Endocan (ESM1), an endothelial-secreted proteoglycan, confers enhanced proliferative, migratory, and angiogenic properties to GBM cells and regulates their spatial identity.
View Article and Find Full Text PDFBackground: Breeding programs for nutrient-efficient tea plant varieties could be advanced by the combination of genotyping and phenotyping technologies. This study was aimed to search functional SNPs in key genes related to the nitrogen-assimilation in the collection of tea plant (L.) Kuntze.
View Article and Find Full Text PDFArticle Synopsis
- - Cowden syndrome, caused by mutations in the PTEN gene, increases the risk of various tumors due to disrupted cell cycle regulation, leading to unchecked cell growth throughout a person's life.
- - A clinical case presented discusses a 7-year-old patient with typical features of Cowden syndrome, including macrocephaly and skin manifestations like trichilemmomas and keratosis, alongside benign and malignant tumors.
- - Common malignancies associated with Cowden syndrome are breast, thyroid, colorectal, renal cell, and endometrial cancers, with thyroid cancer often developing early in childhood, necessitating regular screenings for affected individuals.
Prothrombinase complex, composed of coagulation factors Xa (FXa) and Va (FVa) is a major enzyme of the blood coagulation network that produces thrombin via activation of its inactive precursor prothrombin (FII) on the surface of phospholipid membranes. However, pathways and mechanisms of prothrombinase formation and substrate delivery are still discussed. Here we designed a novel mathematical model that considered different potential pathways of FXa or FII binding (from the membrane or from solution) and analyzed the kinetics of thrombin formation in the presence of a wide range of reactants concentrations.
View Article and Find Full Text PDFBackground: Factor X activation by the phospholipid-bound intrinsic tenase complex is a critical membrane-dependent reaction of blood coagulation. Its regulation mechanisms are unclear, and a number of questions regarding diffusional limitation, pathways of assembly and substrate delivery remain open.
Methods: We develop and analyze here a detailed mechanism-driven computer model of intrinsic tenase on phospholipid surfaces.