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001-es BibID:BIBFORM063538
Első szerző:Birukov, Konstantin G.
Cím:Molecular and biochemical characterization of alternatively spliced variants of human endothelial cell MLCK / K. G. Birukov, Cs. Csortos, S. Dudek, V. Lazar, A. D. Verin, J. G. N. Garcia
Dátum:1999
ISSN:1073-449X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:American Journal of Respiratory and Critical Care Medicine 159 : 3 (1999), p. 1. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Dudek, Steven Lázár Viktória (1981-) (molekuláris biológus) Verin, Alexander Garcia, Joe G. N.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

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.
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3.

001-es BibID:BIBFORM063539
Első szerző:Csortos Csilla (biokémikus)
Cím:Molecular and biochemical characterization of protein phosphatase 1 (PP1) in endothelium / Cs. Csortos, A. D. Verin, S. D. Durbin, C. E. Patterson, J. G. N. Garcia
Dátum:1998
ISSN:1073-449X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:American Journal of Respiratory and Critical Care Medicine 157 : 3 (1998), p. 1. -
További szerzők:Verin, Alexander Durbin, Steve D. Patterson, Carolyn E. Garcia, Joe G. N.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM047046
035-os BibID:PMID:21341016
Első szerző:Csortos Csilla (biokémikus)
Cím:Screening cDNA Libraries Using Partial Probes to Isolate Full-Length cDNAs from Vascular Cells / Csilla Csortos, Virginie Lazar, Joe G. N. Garcia
Dátum:1999
Megjegyzések:The purpose of screening cDNA libraries is to isolate a particular cDNA clone encoding a mRNA and by implication, a protein, of interest. The screening is based on identification of the desired clone among a large number of recombinant clones within the library selected (1,2). As an example of both the utility and power of library screening, we will relate our own library screening efforts utilized to isolate the nonmuscle high molecular weight myosin light chain kinase isoform from a human umbilical vein endothelial cell cDNA library (3). This unique nonmuscle myosin light chain kinase isoform phosphorylates myosin light chains, thereby playing an essential role in agonist-mediated endothelial cell contraction, paracellular gap formation and increased vascular permeability. We are hopeful that this step-by-step approach will help the reader to understand the discussed methods.
ISBN:978-0-89603-731-1
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Methods in Molecular Medicine. - 30 (1999), p. 59-72. -
További szerzők:Lazar, Virginie Garcia, Joe G. N.
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5.

001-es BibID:BIBFORM047045
035-os BibID:PMID:10362724
Első szerző:Garcia, Joe G. N.
Cím:Regulation of endothelial cell myosin light chain kinase by Rho, cortactin, and p60(src) / Joe G. N. Garcia, Alexander D. Verin, Kane Schaphorst, Rafat Siddiqui, Carolyn E. Patterson, Csilla Csortos, Viswanathan Natarajan
Dátum:1999
ISSN:1040-0605
Megjegyzések:Inflammatory diseases of the lung are characterized by increases in vascular permeability and enhanced leukocyte infiltration, reflecting compromise of the endothelial cell (EC) barrier. We examined potential molecular mechanisms that underlie these alterations and assessed the effects of diperoxovanadate (DPV), a potent tyrosine kinase activator and phosphatase inhibitor, on EC contractile events. Confocal immunofluorescent microscopy confirmed dramatic increases in stress-fiber formation and colocalization of EC myosin light chain (MLC) kinase (MLCK) with the actin cytoskeleton, findings consistent with activation of the endothelial contractile apparatus. DPV produced significant time-dependent increases in MLC phosphorylation that were significantly attenuated but not abolished by EC MLCK inhibition with KT-5926. Pretreatment with the Rho GTPase-inhibitory C3 exotoxin completely abolished DPV-induced MLC phosphorylation, consistent with Rho-mediated MLC phosphatase inhibition and novel regulation of EC MLCK activity. Immunoprecipitation of EC MLCK after DPV challenge revealed dramatic time-dependent tyrosine phosphorylation of the kinase in association with increased MLCK activity and a stable association of MLCK with the p85 actin-binding protein cortactin and p60(src). Translocation of immunoreactive cortactin from the cytosol to the cytoskeleton was noted after DPV in concert with cortactin tyrosine phosphorylation. These studies indicate that DPV activates the endothelial contractile apparatus in a Rho GTPase-dependent fashion and suggests that p60(src)-induced tyrosine phosphorylation of MLCK and cortactin may be important features of contractile complex assembly.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:American Journal of Physiology. Lung Cellular and Molecular Physiology. - 276 : 6 Pt 1 (1999), p. L989-L998. -
További szerzők:Verin, Alexander Schaphorst, Kane Siddiqui, Rafat Patterson, Carolyn E. Csortos Csilla (1956-) (biokémikus) Natarajan, Viswanathan
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6.

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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7.

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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8.

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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