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001-es BibID:	BIBFORM046972
035-os BibID:	PMID:7626120
Első szerző:	Rosfjord, Edward
Cím:	Phosphorylation and DNA binding of the octamer binding transcription factor Oct-3 / Edward Rosfjord, Beáta Scholtz, Robert Lewis, Angie Rizzino
Dátum:	1995
ISSN:	0006-291X
Megjegyzések:	Phosphorylation influences DNA binding and transactivator capabilities of multiple transcription factors. In this study, we demonstrate that the POU-domain transcription factor, Oct-3, can be phosphorylated in vivo. In addition, we show that in COS-1 cells Oct-3 is phosphorylated exclusively on serine residues. Lastly, we provide evidence that phosphorylation is not required for Oct-3 binding to DNA and treatment of Oct-3 with calf intestinal alkaline phosphatase does not influence its ability to bind DNA.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochemical and Biophysical Research Communications. - 212 : 3 (1995), p. 847-853. -
További szerzők:	Scholtz Beáta (1967-) (biokémikus, molekuláris biológus) Lewis, Robert Rizzino, Angie
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM046590
035-os BibID:	PMID:8606002
Első szerző:	Scholtz Beáta (biokémikus, molekuláris biológus)
Cím:	Appearance of nuclear protease activity after embryonal carcinoma cells undergo differentiation / Beáta Scholtz, Kimberly Lamb, Edward Rosfjord, Michelle Kingsley, Angie Rizzino
Dátum:	1996
ISSN:	0012-1606
Megjegyzések:	Eppley Institute for Research in Cancer and Allied Diseases (Omaha, NE) Proteolytic systems are involved via multiple mechanisms in the regulation of gene expression, including tightly controlled metabolism of transcription factors. In this study, we demonstrate that differentiation of mouse embryonal carcinoma cells to parietal endoderm-like cells is accompanied by the appearance of nuclear protease activity. Interestingly, this nuclear-associated protease activity is not observed in the visceral endoderm-like cell line, PSA-5E, or in the differentiated cells derived from both mouse embryonic stem cells and the human embryonal carcinoma cell line NT2/D1. We also determined that this differentiation-associated nuclear protease activity causes proteolysis of a wide range of different transcription factors, including ATF-1, Sp1, NF-YA and B, and octamer-binding proteins Oct-1 and Oct-3. Based on the effects of specific inhibitors, the nuclear protease(s) can be classified as a cysteine protease; however, lack of inhibition by calpastatin and EGTA distinguishes this protease activity from the calpain family of proteases. Given the properties of the differentiation-associated nuclear protease(s), we discuss the possibility that this protease(s) plays a role in the metabolism of transcription factors during the differentiation of specific embryonic cells.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Developmental Biology. - 173 : 2 (1996), p. 420-427. -
További szerzők:	Lamb, Kimberly Rosfjord, Edward Kingsley-Kallesen, Michelle Rizzino, Angie
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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