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001-es BibID:	BIBFORM047042
035-os BibID:	PMID:15156565
Első szerző:	Tar Krisztina (biokémikus, molekuláris biológus)
Cím:	Phosphatase 2A is involved in endothelial cell microtubule remodeling and barrier regulation / Krisztina Tar, Anna A. Birukova, Csilla Csortos, Éva Bakó, Joe G. N. Garcia, Alexander D. Verin
Dátum:	2004
ISSN:	0730-2312
Megjegyzések:	We have recently shown that microtubule (MT) inhibitor, nocodazole (2-5 microM) significantly increases endothelial cells (EC) actomyosin contraction and permeability indicating the importance of MT in maintaining the EC barrier (Verin et al. [2001]: Cell Mol Physiol 281:L565-L574). Okadaic acid (OA, 2-5 nM), a powerful inhibitor of protein phosphatase 2A (PP2A), significantly potentiates the effect of submaximal concentrations of nocodazole (50-200 nM) on transendothelial electrical resistance (TER) suggesting the involvement of PP2A activity in the MT-mediated EC barrier regulation. Immunofluorescent staining of EC revealed that in control cells PP2A distributes in a pattern similar to MT. Consistent with these results, we demonstrated that significant amounts of PP2A were present in MT-enriched EC fractions indicating tight association of PP2A with MT in endothelium. Treatment of EC with OA leads to disappearance of MT-like PP2A staining suggesting dissociation of PP2A from the MT network. Next, we examined the effect of PP2A inhibition on phosphorylation status of MT-associated protein tau, which in its unphosphorylated form promotes MT assembly. OA caused significant increases in tau phosphorylation confirming that tau is a substrate for PP2A in endothelium. Immunofluorescent experiments demonstrated that the OA-induced increases in tau phosphorylation strongly correlated with translocation of phospho-tau to cell periphery and disassembly of peripheral MT. These results suggest the involvement of PP2A-mediated tau dephosphorylation in alteration of EC MT structure and highlight the potential importance of PP2A in the regulation of EC the MT cytoskeleton and barrier function.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Cellular Biochemistry. - 92 : 3 (2004), p. 534-546. -
További szerzők:	Birukova, Anna A. Csortos Csilla (1956-) (biokémikus) Bakó Éva (1958-) (biokémikus) Garcia, Joe G. N. Verin, Alexander
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001-es BibID:	BIBFORM003558
Első szerző:	Tar Krisztina (biokémikus, molekuláris biológus)
Cím:	Role of protein phosphatase 2A in the regulation of endothelial cell cytoskeleton structure / Krisztina Tar, Csilla Csortos, Istvan Czikora, Gabor Olah, Shwu-Fan Ma, Raj Wadgaonkar, Pal Gergely, Joe G. N. Garcia, Alexander D. Verin
Dátum:	2006
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban endothelium phosphatase 2A permeability microtubules microfilaments tau HSP27
Megjelenés:	Journal of Cellular Biochemistry. - 98 : 4 (2006), p. 931-953. -
További szerzők:	Csortos Csilla (1956-) (biokémikus) Czikora István (1979-) (vegyész, biokémikus) Oláh Gábor Ma, Shwu-Fan Wadgaonkar, Raj Gergely Pál (1947-) (biokémikus) Garcia, Joe G. N. Verin, Alexander
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001-es BibID:	BIBFORM047044
035-os BibID:	PMID:10906760
Első szerző:	Verin, Alexander
Cím:	Characterization of the protein phosphatase 1 catalytic subunit in endothelium : involvement in contractile responses / Alexander D. Verin, Csilla Csortos, Steve D. Durbin, Antonina Aydanyan, Peiyi Wang, Carolyn E. Patterson, Joe G. N. Garcia
Dátum:	2000
ISSN:	0730-2312
Megjegyzések:	We have previously demonstrated the direct involvement of a type 1 Ser/Thr phosphatase (PPase 1) in endothelial cell (EC) barrier regulation [Am. J. Physiol. 269:L99-L108, 1995]. To further extend this observation, we microinjected either the Ser/Thr PPase inhibitor, calyculin, or the PPase 1 inhibitory protein, I-2 into bovine pulmonary artery EC and demonstrated both an increase in F-actin stress fibers and a shift from a regular polygonal shape to a spindle shape with gaps apparent at the cell borders. Northern blot analysis with specific cDNA probes revealed the presence of three major PPase 1 catalytic subunit (CS1) isoforms (alpha, delta, and gamma) in human and bovine EC. To characterize the myosin-associated EC CS1 isoform, myosin-enriched bovine EC fraction was screened with anti-CS1alpha and anti-CS1delta antibodies The anti-CS1delta antiserum, but not anti-CS1alpha antiserum cross reacts with the CS1 isoform present in myosin-enriched fraction and CS1delta was found in stable association with EC myosin/myosin light chain kinase (MLCK) complex in MLCK immunoprecipitates under nondenaturing conditions. Consistent with these data, overexpression of CS1delta-GFP construct in bovine endothelium followed by immunoprecipitation of CS1 with anti-GFP antibody revealed the stable association of CS1delta with actomyosin complex. Finally, screening of a human EC oligo(dT)-primed cDNA library with a probe encoding a rat CS1delta cDNA segment yielding several positive clones that encoded the entire CS1delta open reading frame and partially noncoding regions. Sequence analysis determined a high homology ( approximately 99%) with human CS1delta derived from a teratocarcinoma cell line. Together, these data suggest that CS1delta is the major of PPase 1 isoform specifically associated with EC actomyosin complex and which participates in EC barrier regulation.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Cellular Biochemistry. - 79 : 1 (2000), p. 113-125. -
További szerzők:	Csortos Csilla (1956-) (biokémikus) Durbin, Steve D. Aydanyan, Antonina Wang, Peiyi Patterson, Carolyn E. Garcia, Joe G. N.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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