National Repository of Grey Literature 7 records found  Search took 0.00 seconds. 
Definition of the expression pattern of DASH system in transformed glial cells, the coupled expression of fibroblast activation protein and dipeptidyl peptidase-IV.
Balážiová, Eva ; Šedo, Aleksi (advisor) ; Borovanský, Jan (referee) ; Mareš, Vladislav (referee)
Dipeptidyl peptidase-IV (DPP-IV) is a multifunctional transmembrane glycoprotein removing X-Pro dipeptide from the amino-terminus of the peptide chain. This evolutionary conserved sequence protects a number of biologically active peptides against the unspecific proteolytic cleavage. DPP-IV belongs into the group of "Dipeptidyl peptidase-IV Activity and/or Structure Homologues" (DASH), which, except the canonical DPP-IV, comprises fibroblast activation protein-α/seprase (FAP), and several other molecules. However several of DASH molecules are the enzymes, they execute at least some of their biological functions by non-proteolytic protein-protein interactions. DASH molecules, their substrates and binding partners are parts of "DASH system" which is affected in several pathological process including a cancer. Specifically DPP-IV and its closest structural relative FAP are among others expected to be involved in the development and progression of malignant glioma. In this study we showed the expression and colocalization of DPP-IV and FAP in glioma cells in vitro and in human high grade gliomas. In addition to the DPP-IV/FAP double positive transformed glial cells, we also identified a subpopulation of FAP positive mesenchymal cells located in the perivascular compartment. Moreover we described the...
Dipeptidyl peptidase-IV and Fibroblast activation protein in gliomagenesis.
Trylčová, Jana ; Šedo, Aleksi (advisor) ; Mandys, Václav (referee) ; Mareš, Vladislav (referee)
"Dipeptidyl peptidase-IV Activity and/or Structure Homologues"(DASH) represent a newly defined group of multifunctional molecules, typically bearing dipeptidyl peptidase-IV- like hydrolytic activity. Dipeptidyl peptidase-IV (DPP-IV) cleaves out X-Pro dipeptides from the N-terminus of peptides. Other molecules carrying similar enzyme activity, such as Fibroblast activation protein (FAP), DPP-II, DPP8 and DPP9 or even DPP-IV structure-like but hydrolytically inactive molecules (DPP6 and DPP10) also belong to this group. Recent knowledge suggest a substantial role of DASH in cancer pathogenesis. The aim of this study is a preparation of a biological model and its use for understanding the mechanisms of interaction(s) between transformed glial cells and stroma in the processes of origin and development of tumors derived from neuroectoderm. Stable transfected human glioblastoma cell lines with inducible gene expression of DPP-IV, Fibroblast activation protein and their enzymatically inactive mutated forms, were prepared within the project. Prepared cell lines are used as a tool for studying not only the "autocrine" importance of DPP-IV and FAP for the expressing cells in in-vitro, but also for their potential "paracrine" effect(s) within the tumor microenvironment after homotopic implantation into the...
Definition of the expression pattern of DASH system in transformed glial cells, the coupled expression of fibroblast activation protein and dipeptidyl peptidase-IV.
Balážiová, Eva ; Šedo, Aleksi (advisor) ; Borovanský, Jan (referee) ; Mareš, Vladislav (referee)
Dipeptidyl peptidase-IV (DPP-IV) is a multifunctional transmembrane glycoprotein removing X-Pro dipeptide from the amino-terminus of the peptide chain. This evolutionary conserved sequence protects a number of biologically active peptides against the unspecific proteolytic cleavage. DPP-IV belongs into the group of "Dipeptidyl peptidase-IV Activity and/or Structure Homologues" (DASH), which, except the canonical DPP-IV, comprises fibroblast activation protein-α/seprase (FAP), and several other molecules. However several of DASH molecules are the enzymes, they execute at least some of their biological functions by non-proteolytic protein-protein interactions. DASH molecules, their substrates and binding partners are parts of "DASH system" which is affected in several pathological process including a cancer. Specifically DPP-IV and its closest structural relative FAP are among others expected to be involved in the development and progression of malignant glioma. In this study we showed the expression and colocalization of DPP-IV and FAP in glioma cells in vitro and in human high grade gliomas. In addition to the DPP-IV/FAP double positive transformed glial cells, we also identified a subpopulation of FAP positive mesenchymal cells located in the perivascular compartment. Moreover we described the...
Benefits and problems of the use of alternative multimedia (AMM) for teaching biology of students at the Faculty of Pedagogy
Mareš, Vladislav ; Hajer, J.
The paper reviews authors´ experience with the use of alternative multimedia (AMM) in teaching biology at the Faculty of Pedagogy, University of J.E. Purkinje in Usti nad Labem, Czech Republic. They include computer simulations, videtotapes , tissue cultures, protozoa and some invertebrates. Besides protection of animals, AMM enable us to demonstrate not available laboratory instruments, rare animals species in their habitats, etc. Some computer programs force students to a more active study of some topics of cell biology and physiology. The limitations in the use of AMM are discussed.
Ultrastructure of nuclear RNP particles extruded into cytoplasm in apoptotic cells
Krajčí, D. ; Mareš, Vladislav ; Lisá, Věra
In C6 glioma cells undergoing cisplatin induced apoptosis,structures resembling degraded nucleoli were frequently observedin the perinuclear cytoplasm. In some cells, these originallynuclear structures mooved through deep invaginations of the nuclearenvelope, while in the other cells breakdown of small nuclearlobules is the source of this cytoplasmic component.

See also: similar author names
1 Mareš, Viktor
2 Mareš, Vlastimil
4 Mareš, Václav
4 Mareš, Vít
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