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001-es BibID:	BIBFORM047043
035-os BibID:	PMID:11113114
Első szerző:	Birukov, Konstantin G.
Cím:	Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src) / Konstantin G. Birukov, Csilla Csortos, Lisa Marzilli, Steven Dudek, Shwu-Fan Ma, Anne R. Bresnick, Alexander D. Verin, Robert J. Cotter, Joe G. N. Garcia
Dátum:	2001
ISSN:	0021-9258 1083-351X
Megjegyzések:	The Ca(2+)/calmodulin-dependent endothelial cell myosin light chain kinase (MLCK) triggers actomyosin contraction essential for vascular barrier regulation and leukocyte diapedesis. Two high molecular weight MLCK splice variants, EC MLCK-1 and EC MLCK-2 (210-214 kDa), in human endothelium are identical except for a deleted single exon in MLCK-2 encoding a 69-amino acid stretch (amino acids 436-505) that contains potentially important consensus sites for phosphorylation by p60(Src) kinase (Lazar, V., and Garcia, J. G. (1999) Genomics 57, 256-267). We have now found that both recombinant EC MLCK splice variants exhibit comparable enzymatic activities but a 2-fold reduction of V(max), and a 2-fold increase in K(0.5 CaM) when compared with the SM MLCK isoform, whereas K(m) was similar in the three isoforms. However, only EC MLCK-1 is readily phosphorylated by purified p60(Src) in vitro, resulting in a 2- to 3-fold increase in EC MLCK-1 enzymatic activity (compared with EC MLCK-2 and SM MLCK). This increased activity of phospho-MLCK-1 was observed over a broad range of submaximal [Ca(2+)] levels with comparable EC(50) [Ca(2+)] for both phosphorylated and unphosphorylated EC MLCK-1. The sites of tyrosine phosphorylation catalyzed by p60(Src) are Tyr(464) and Tyr(471) within the 69-residue stretch deleted in the MLCK-2 splice variant. These results demonstrate for the first time that p60(Src)-mediated tyrosine phosphorylation represents an important mechanism for splice variant-specific regulation of nonmuscle MLCK and vascular cell function.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Biological Chemistry. - 276 : 11 (2001), p. 8567-8573. -
További szerzők:	Csortos Csilla (1956-) (biokémikus) Marzilli, Lisa Dudek, Steven Ma, Shwu-Fan Bresnick, Anne R. Verin, Alexander Cotter, Robert J. Garcia, Joe G. N.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM047047
035-os BibID:	PMID:8576224
Első szerző:	Csortos Csilla (biokémikus)
Cím:	High complexity in the expression of the B' subunit of protein phosphatase 2A0. Evidence for the existence of at least seven novel isoforms / Csilla Csortos, Stanislaw Zolnierowicz, Éva Bakó, Stephen D. Durbin, Anna A. DePaoli-Roach
Dátum:	1996
ISSN:	0021-9258 1083-351X
Megjegyzések:	Association of the catalytic subunit (C2) with a variety of regulatory subunits is believed to modulate the activity and specificity of protein phosphatase 2A (PP2A). In this study we report the cloning and expression of a new family of B-subunit, the B', associated with the PP2A0 form. Polymerase chain reactions and cDNA library screening have identified at least seven cDNA isotypes, designated alpha, beta 1, beta 2, beta 3, beta 4, gamma, and delta. The different beta subtypes appear to be generated by alternative splicing. The deduced amino acid sequences of the alpha, beta 2, beta 3, beta 4 and gamma isoforms predict molecular weights of 57,600, 56,500, 60,900, 52,500, and 68,000, respectively. The proteins are 60-80% identical and differ mostly at their termini. Two of the isoforms, B' beta 3 and B' gamma, contain a bipartite nuclear localization signal in their COOH terminus. No homology was found with other B- or B- related subunits. Northern analyses indicate a tissue-specific expression of the isoforms. Expression of B' alpha protein in Escherichia coli generated a polypeptide of approximately 53 kDa, similar to the size of the B' subunit present in the purified PP2A0. The recombinant protein was recognized by antibody raised against native B' and interacted with the dimeric PP2A (A.C2) to generate a trimeric phosphatase. The deduced amino acid sequences of the B' isoforms show significant homology to mammalian, fungal, and plant nucleotide sequences of unknown function present in the data bases. Notably, a high degree of homology (55-66%) was found with a yeast gene, RTS1, encoding a multicopy suppressor of a rox3 mutant. Our data indicate that at least seven B' subunit isoforms may participate in the generation of a large number of PP2A0 holoenzymes that may be spatially and/or functionally targeted to different cellular processes.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Biological Chemistry. - 271 : 5 (1996), p. 2578-2588. -
További szerzők:	Zolnierowicz, Stanislaw Bakó Éva (1958-) (biokémikus) Durbin, Steve D. DePaoli-Roach, Anna A.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM082777
035-os BibID:	(WoS)000505005800030 (Scopus)85077296143
Első szerző:	Thalwieser Zsófia (biológus)
Cím:	Protein phosphatase 2A-mediated flotillin-1 dephosphorylation up-regulates endothelial cell migration and angiogenesis regulation / Zsófia Thalwieser, Nikolett Király, Márton Fonódi, Csilla Csortos, Anita Boratkó
Dátum:	2019
ISSN:	0021-9258 1083-351X
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of Biological Chemistry. - 294 : 52 (2019), p. 20196-20206. -
További szerzők:	Király Nikolett (1992-) (molekuláris biológus, biokémikus) Fonódi Márton (1995-) (molekuláris biológus) Csortos Csilla (1956-) (biokémikus) Boratkó Anita (1985-) (biokémikus, molekuláris biológus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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