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001-es BibID:BIBFORM102209
Első szerző:Demény Máté Ágoston (molekuláris biológus)
Cím:Structure of Transglutaminases: Unique Features Serve Diverse Functions / Máté Á. Demény, Ilma Korponay-Szabó, László Fésüs
Dátum:2016
Megjegyzések:Understanding the diverse functions and pathologies of transglutaminases requires detailed analysis and interpretation of their structures. This chapter is an attempt to describe in detail how these enzymes are folded into functional domains, what type of catalytic and scaffolding functions have been gained as the result of their evolution, how their regulation is achieved through unique Ca2+ and purine nucleotide binding sites, redox changes and specific proteolytic actions, and by influencing the equilibrium of open-close configurations. The importance of structural motifs in pathologies is underlined by the celiac epitopes of transglutaminase 2, responsible for autoimmune reactions.
ISBN:978-4-431-55823-1
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
könyvrészlet
Domain organization
Crystallography
Catalytic mechanism
Regulation; Ca2+
Purine nucleotides
Proteolysis
Redox
Open-close conformation
Substrates
Interactions
Celiac epitope
Megjelenés:Transglutaminases / Ed. Kiyotaka Hitomi, Soichi Kojima, Laszlo Fesus. - p. 1-41. -
További szerzők:Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Fésüs László (1947-) (orvos biokémikus)
Internet cím:Szerző által megadott URL
DOI
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001-es BibID:BIBFORM011938
Első szerző:Hodrea Judit (vegyész)
Cím:Transglutaminase 2 is expressed and active on the surface of human monocyte-derived dendritic cells and macrophages / Hodrea J., Demény M. A., Majai G., Sarang Z., Korponay-Szabo I., Fésüs L.
Dátum:2010
Megjegyzések:The multifunctional enzyme, transglutaminase 2 (TG2), can be found intracellularly, in the extracellular matrix and on the cell surface. Cell surface TG2 (csTG2) could not be detected by TG2-specific antibodies or autoantibodies on immunocompetent cells. A supposedly csTG2-specific antibody, 6B9, was recently shown to actually react with CD44. Though the importance of TG2-mediated deamidation of gluten in the pathogenesis of celiac disease has been well recognized, it is not known in which intestinal cells or cell compartment the deamidation occurs. Duodenal dendritic cells (DCs) can be directly involved in gluten-reactive T-cell activation. Here we use blood monocyte-derived dendritic cells (iDC) and macrophages (MPhi) as a model for intestinal antigen-presenting cells (APCs) and show that they contain large amounts of TG2. We found that TG100, a commercial TG2-specific monoclonal antibody can recognize TG2 on the surface of these cells, that is monocyte-derived APCs express surface-associated TG2. TG2 expression was found on the surface of individual tunica propria cells in frozen small bowel tissue sections from both normal and celiac subjects. We also demonstrate that the pool of TG2 on the surface of iDCs can be catalytically active, hence it might directly be involved in the deamidation of gliadin peptides. Bacterial lipopolysaccharide (LPS) increased the level of TG2 on the surface of maturing DCs, supporting the hypothesis that an unspecific inflammatory process in the gut may expose more transglutaminase activity.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Immunology Letters. - 13 : 1-2 (2010), p. 74-81. -
További szerzők:Demény Máté Ágoston (1976-) (molekuláris biológus) Majai Gyöngyike (1977-) (belgyógyász, immunológus) Sarang Zsolt (1976-) (mikrobiológus) Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Fésüs László (1947-) (orvos biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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