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1.

001-es BibID:BIBFORM060640
Első szerző:Fésüs László (orvos biokémikus)
Cím:Activation of transglutaminase and production of protein-bound gamma-glutamylhistamine in stimulated mouse mast cells / Laszlo Fesus, Eva F. Szucs, Kim E. Barrett, Dean D. Metcalfe, J. E. Folk
Dátum:1985
Megjegyzések:The identification of transglutaminase in the growth-factor-dependent mouse mast cell line PT18 was accomplished through its characteristic catalytic properties (specificity, calcium dependency, and inhibition by iodoacetamide); and by both immunoprecipitation and Western blot analysis using affinity purified antibody. The enzymatic activity in these cells increased in association with the release of histamine from the cells induced by an IgE-dependent mechanism or by exposure to the ionophores A23187 or Br-x537A. The increase in transglutaminase activity was paralleled by a marked increase in the level of protein-bound gamma-glutamylhistamine, determined in radiolabeled form in mast cells that were either metabolically labeled with [3H]histidine or incubated with [3H]histamine before degranulation. The highest level of bound gamma-glutamylhistamine was found in the immunologically stimulated cells. Enzymatic activity and the gamma-glutamyl derivative were associated primarily with the cells, both before and after stimulation. Separation of gamma-glutamylhistamine in a proteolytic digest of these cells was carried out using a combination of ion exchange chromatography and high performance liquid chromatography. The gamma-glutamyl compound was identified and quantitated through the enzymatic production of histamine with the use of gamma-glutamylamine cyclotransferase, an enzyme specific for the disassembly of gamma-glutamylamines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biological Chemistry 260 : 25 (1985), p. 13771-13778. -
További szerzők:Szűcs Éva F. Barrett, Kim E. Metcalfe, Dean D. Folk, J. E.
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2.

001-es BibID:BIBFORM060641
Első szerző:Lee, K. N.
Cím:Development of selective inhibitors of transglutaminase : phenylthiourea derivatives / K. N. Lee, L. Fesus, S. T. Yancey, J. E. Girard, S. I. Chung
Dátum:1985
Megjegyzések:For the purpose of developing a transglutaminase inhibitor which could be effective in physiological and pharmacological studies, a series of phenylthiourea derivatives of alpha, omega-diaminoalkanes were designed, synthesized, and evaluated kinetically as inhibitors of transglutaminases. A homologous series of compounds of the structure phenylthiourea-(CH2)n-NH2, where n = 2, 3, 4, 5, and 6, were tested for the inhibition of both guinea pig liver transglutaminase-catalyzed amine incorporation into various glutamine-containing substrates and plasma transglutaminase (factor XIIIa)-catalyzed amine incorporation into fibrin and fibrin cross-linking. It was found that the inhibitory activity of the compounds increases with increasing number of methylene groups in the side chain up to a maximum of n = 5. A further increase in the length of the methylene side chain to n = 6 results in decreased activity. The Ki value (4.9 X 10(-5) M) of 1-(5-aminopentyl)-3-phenylthiourea (PPTU) (n = 5) for the inhibition of guinea pig transglutaminase-catalyzed amine incorporation into the B chain of oxidized insulin is in close agreement to its Km(app) value (7.1 X 10(-5) M) obtained using 14C-labeled PPTU. PPTU was also found to be a potent inhibitor of plasma transglutaminase-catalyzed fibrin cross-linking. The finding that the specificity of the alkylamines for inhibition is correlated with the length of their methyl side chains is compatible with those reported for aliphatic amines and monodansylcadaverine analogues (where dansyl is 5-dimethylaminonaphthalene-1-sulfonyl). The phenylthiourea derivatives, however, are far less toxic in mice than monodansylcadaverine as indicated by their LD50 values: PPTU, 400 +/- 25 mg/kg; and monodansylcadaverine, 160 +/- 20 mg/kg.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biological Chemistry 260 : 27 (1985), p. 14689-14694. -
További szerzők:Fésüs László (1947-) (orvos biokémikus) Yancey, S. T. Girard, James E. Chung, Soo Il
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM033276
035-os BibID:WOS:A1997XR22100042
Első szerző:Nemes Zoltán (molekuláris biológus, pszichiáter)
Cím:Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis / Zoltán Nemes, Róza Adány, Margit Balázs, Peter Boross, László Fésüs
Dátum:1997
Megjegyzések:A lysine derivative, 3-[N-alpha[N-epsilon-[2',4'-dinitrophenyl]-amino-n-hexanoyl-L-lysylamido]-propane-1-ol, a novel amine substrate of transglutaminases, was synthesized and delivered into intact HL-60 and U937 human leukemia cells to probe the function of the intracellular enzyme. The novel substrate compound was covalently incorporated into intracellular proteins in these cells expressing high levels of tissue transglutaminase and undergoing apoptosis following the induction of their differentiation with dimethyl sulfoxide and retinoic acid. Immunoaffinity purification and microsequencing of labeled proteins identified cytoplasmic actin as the main endogenous glutaminyl substrate in these cells. As shown by confocal image analysis, cells revealed distinct labeling of the microfilament meshwork structures by the novel compound as the result of the intracellular action of transglutaminase.
Tárgyszavak:Orvostudományok Egészségtudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:The Journal of biological chemistry. - 272 : 33 (1997), p. 20577-20583. -
További szerzők:Boross Péter (1972-) (biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Ádány Róza (1952-) (megelőző orvostan és népegészségtan szakorvos)
Internet cím:DOI
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4.

001-es BibID:BIBFORM008378
Első szerző:Nemes Zoltán (molekuláris biológus, pszichiáter)
Cím:Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies / Nemes, Z., Petrovski, G., Aerts, M., Sergeant, K., Devreese, B., Fésüs, L.
Dátum:2009
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Journal of Biological Chemistry. - 284 : 40 (2009), p. 27252-27264. -
További szerzők:Petrovski, Goran (1975-) (orvos) Aerts, Maarten Sergeant, Kjell Devreese, Bart Fésüs László (1947-) (orvos biokémikus)
Internet cím:elektronikus változat
DOI
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5.

001-es BibID:BIBFORM060606
Első szerző:Nemes Zoltán (patológus)
Cím:Cholesterol 3-Sulfate Interferes with Cornified Envelope Assembly by Diverting Transglutaminase 1 Activity from the Formation of Cross-links and Esters to the Hydrolysis of Glutamine / Zoltán Nemes, Máté Demény, Lyuben N. Marekov, László Fésüs, Peter M. Steinert
Dátum:2000
ISSN:0021-9258 1083-351X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Biological Chemistry. - 275 : 4 (2000), p. 2636-2646. -
További szerzők:Demény Máté Ágoston (1976-) (molekuláris biológus) Marekov, Lyuben N. Fésüs László (1947-) (orvos biokémikus) Steinert, Peter M.
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DOI
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6.

001-es BibID:BIBFORM060625
Első szerző:Tarcsa Edit
Cím:An involucrin-like protein in hepatocytes serves as a substrate for tissue transglutaminase during apoptosis / Edit Tarcsa, Noemi Kedei, Vilmos Thomazy, Laszlo Fésüs
Dátum:1992
Megjegyzések:Cornified envelopes and apoptotic bodies are transglutaminase-cross-linked end-products of physiological cell death pathways. The two structures have similar amino acid composition. Involucrin has been considered as a cornified envelope precursor protein expressed specifically in terminally differentiating keratinocytes and squamous epithelia. We report the presence in hepatocytes of an involucrin-like protein which could be purified from dog liver with procedures characteristic to involucrins. When compared to purified dog esophagus involucrin, the liver protein also reacts with anti-involucrin antibodies, has the same relative molecular mass, possesses similar amino acid composition, and shows almost identical peptide mapping pattern. The involucrin-like protein is detectable by immunohistochemistry in normal and apoptotic hepatocytes, is a substrate of tissue transglutaminase, and is incorporated into cross-linked apoptotic bodies. These results suggest that there are overlapping molecular components in the two characteristic forms (cornification and apoptosis) of naturally occurring cell death.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biological Chemistry 267 : 36 (1992), p. 25648-25651. -
További szerzők:Kedei Noémi Thomázy Vilmos Fésüs László (1947-) (orvos biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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