Találati lista | Tudóstér

001-es BibID:	BIBFORM058126
Első szerző:	Brodie, Chaya
Cím:	PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters / Chaya Brodie, Rivka Steinhart, Gila Kazimirsky, Hadara Rubinfeld, Tehila Hyman, Jolene N. Ayres, Gang Min Hur, Attila Toth, Dazhi Yang, Susan H. Garfield, James C. Stone, Peter M. Blumberg
Dátum:	2004
ISSN:	0026-895X
Megjegyzések:	RasGRP is a family of guanine nucleotide exchange factors that activate small GTPases and contain a C1 domain similar to the one present in protein kinase C (PKC). In this study, we examined the interaction of RasGRP3 and PKC in response to the phorbol ester PMA. In Chinese hamster ovary or LN-229 cells heterologously expressing RasGRP3, phorbol 12-myristate 13-acetate (PMA) induced translocation of RasGRP3 to the perinuclear region and a decrease in the electrophoretic mobility of RasGRP3. The mobility shift was associated with phosphorylation of RasGRP3 on serine residues and seemed to be PKCdelta-dependent because it was blocked by the PKCdelta inhibitor rottlerin as well as by a PKCdelta kinase-dead mutant. Using coimmunoprecipitation, we found that PMA induced the physical association of RasGRP3 with PKCdelta and, using in situ methods, we showed colocalization of PKCdelta and RasGRP3 in the perinuclear region. PKCdelta phosphorylated RasGRP3 in vitro. Previous studies suggest that ectopic expression of RasGRP3 increases activation of Erk1/2. We found that overexpression of either PKCdelta or RasGRP3 increased the activation of Erk1/2 by PMA. In contrast, coexpression of PKCdelta and RasGRP3 yielded a level of phosphorylation of Erk1/2 similar to that of control vector cells. Our results suggest that PKCdelta may act as an upstream kinase associating with and phosphorylating RasGRP3 in response to PMA. The interaction between RasGRP3 and PKCdelta points to the existence of complex cross-talk between various members of the phorbol ester receptors which can have important impact on major signal transduction pathways and cellular processes induced by phorbol esters or DAG
Tárgyszavak:	Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Molecular Pharmacology. - 66 : 1 (2004), p. 76-84. -
További szerzők:	Steinhart, Rivka Kazimirsky, Gila Rubinfeld, Hadara Hyman, Tehila Ayres, Jolene N. Min Hur, Gang Tóth Attila (1971-) (biológus) Yang, Dazhi Garfield, Susan H. Stone, James C. Blumberg, Peter M.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM058130
Első szerző:	Kedei Noémi
Cím:	Characterization of the interaction of ingenol 3-angelate with protein kinase C / Noemi Kedei, Daniel J. Lundberg, Attila Toth, Peter Welburn, Susan H. Garfield, Peter M. Blumberg
Dátum:	2004
ISSN:	0008-5472
Megjegyzések:	Ingenol 3-angelate (I3A) is one of the active ingredients in Euphorbia peplus, which has been used in traditional medicine. Here, we report the initial characterization of I3A as a protein kinase C (PKC) ligand. I3A bound to PKC-alpha in the presence of phosphatidylserine with high affinity; however, under these assay conditions, little PKC isoform selectivity was observed. PKC isoforms did show different sensitivity and selectivity for down-regulation by I3A and phorbol 12-myristate 13-acetate (PMA) in WEHI-231, HOP-92, and Colo-205 cells. In all of the three cell types, I3A inhibited cell proliferation with somewhat lower potency than did PMA. In intact CHO-K1 cells, I3A was able to translocate different green fluorescent protein-tagged PKC isoforms, visualized by confocal microscopy, with equal or higher potency than PMA. PKC-delta in particular showed a different pattern of translocation in response to I3A and PMA. I3A induced a higher level of secretion of the inflammatory cytokine interleukin 6 compared with PMA in the WEHI-231 cells and displayed a marked biphasic dose-response curve for the induction. I3A was unable to cause the same extent of association of the C1b domain of PKC-delta with lipids, compared with PMA or the physiological regulator diacylglycerol, and was able to partially block the association induced by these agents, measured by surface plasmon resonance. The in vitro kinase activity of PKC-alpha induced by I3A was lower than that induced by PMA. The novel pattern of behavior of I3A makes it of great interest for further evaluation.
Tárgyszavak:	Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Cancer Research. - 64 : 9 (2004), p. 3243-3255. -
További szerzők:	Lundberg, Daniel J. Tóth Attila (1971-) (biológus) Welburn, Peter Garfield, Susan H. Blumberg, Peter M.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM020697
Első szerző:	Lázár József
Cím:	Kinetics of Penetration Influence the Apparent Potency of Vanilloids on TRPV1 / Jozsef Lazar, Derek C. Braun, Attila Tóth, Yun Wang, Larry V. Pearce, Vladimir A. Pavlyukovets, Peter M. Blumberg, Susan H. Garfield, Stephen Wincovitch, Hyun-Kyung Choi, and Jeewoo Lee
Dátum:	2006
ISSN:	0026-895X
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Molecular Pharmacology. - 69 : 4 (2006), p. 1166-1173. -
További szerzők:	Braun, Derek C. Tóth Attila (1971-) (biológus) Wang, Yun Pearce, Larry V. Pavlyukovets, Vladimir A. Blumberg, Peter M. Garfield, Susan H. Wincovitch, Stephen Choi, Hyun-Kyung Lee, Jeewoo
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: