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001-es BibID:	BIBFORM020155
Első szerző:	Calpe, Silvia
Cím:	Identification and characterization of two related murine genes, Eat2a and Eat2b, encoding single SH2-domain adapters / Silvia Calpe, Erika Erdős, Gongxian Liao, Ninghai Wang, Svend Rietdijk, Maria Simarro, Beata Scholtz, Jill Mooney, Chang Hoon Lee, Min Sun Shin, Éva Rajnavölgyi, John Schatzle, Herbert C. Morse III, Cox Terhorst, Arpad Lanyi
Dátum:	2006
ISSN:	0093-7711
Megjegyzések:	Human EAT-2 (SH2D1B) and SLAM-associated protein (SAP) (SH2D1A) are single SH2-domain adapters, which bind to specific tyrosine residues in the cytoplasmic tail of six signaling lymphocytic activation molecule (SLAM) (SLAMF1)-related receptors. Here we report that, unlike in humans, the mouse and rat Eat2 genes are duplicated with an identical genomic organization. The coding regions of the mouse Eat2a and Eat2b genes share 91% identity at the nucleotide level and 84% at the protein level; similarly, segments of introns are highly conserved. Whereas expression of mouse Eat2a mRNA was detected in multiple tissues, Eat2b was only detectable in mouse natural killer cells, CD8(+) stop T cells, and ovaries, suggesting a very restricted tissue expression of the latter. Both the EAT-2A and EAT-2B coimmunoprecipitated with mouse SLAM in transfected cells and augmented tyrosine phosphorylation of the cytoplasmic tail of SLAM. Both EAT-2A and EAT-2B bind to the Src-like kinases Fyn, Hck, Lyn, Lck, and Fgr, as determined by a yeast two-hybrid assay. However, unlike SAP, the EAT-2 proteins bind to their kinase domains and not to the SH3 domain of these kinases. Taken together, the data suggest that both EAT-2A and EAT-2B are adapters that recruit Src kinases to SLAM family receptors using a mechanism that is distinct from that of SAP.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban adapter proteins EAT-2 SLAM Src kinases
Megjelenés:	Immunogenetics 58 : 1 (2006), p. 15-25. -
További szerzők:	Erdős Erika Liao, Gongxian Wang, Ninghai Rietdijk, Svend Simarro, Maria Scholtz Beáta (1967-) (biokémikus, molekuláris biológus) Mooney, Jill Lee, Chang Hoon Shin, Min Sun Rajnavölgyi Éva (1950-) (immunológus) Schatzle, John Morse, Herbert C. III Terhorst, Cox Lányi Árpád (1962-) (biológus, immunológus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM019938
Első szerző:	Réthi Bence (biológus, immunológus)
Cím:	SLAM/SLAM interactions inhibit CD40-induced production of inflammatory cytokines in monocyte-derived dendritic cells / Bence Réthi, Péter Gogolák, Istvan Szatmari, Ágota Veres, Erika Erdős, Laszlo Nagy, Éva Rajnavölgyi, Cox Terhorst, Árpád Lányi
Dátum:	2006
ISSN:	0006-4971
Megjegyzések:	Signaling lymphocyte activation molecule (SLAM, CD150, or SLAMF1) is a self-ligand receptor on the surface of activated T- and B-lymphocytes, macrophages, and dendritic cells (DCs). Here we examine the effect of SLAM/SLAM interactions on CD40L-induced CD40 signaling pathways in human DCs. CD40L-expressing L929 cells induced DCs to produce interleukin-6 (IL-6), tumor necrosis factor-alpha (TNF-alpha), and IL-12, which was strongly inhibited by coexpression of SLAM on the surface of the L929 cells. Similarly, transfection of DCs with SLAM strongly reduced CD40L-induced IL-12 production. Furthermore, the negative effect of SLAM/SLAM interactions on CD40L-induced DC activation was also detected in the presence of lipopolysaccharide (LPS). LPS-Induced IL-12 secretion, however, was not inhibited by SLAM engagement. CD40L-activated DCs affected by exposure to SLAM/SLAM engagement were impaired in their ability to induce differentiation of naive T lymphocytes into interferon-gamma (IFN-gamma)-producing T-helper 1 (Th1) effector cells. These inhibitory effects were not the result of a general unresponsiveness of DCs to CD40L, as SLAM/SLAM interactions did not prevent CD40L-induced up-regulation of CD83, CD86, or human leukocyte antigen (HLA)-DQ on the surface of DCs. Taken together, the results indicate that SLAM/SLAM interactions inhibit CD40-induced signal transduction in monocyte-derived dendritic cells, an effect that was not detectable in earlier studies using anti-SLAM monoclonal antibodies.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban linked lymphoproliferative-disease lymphocytic activation molecule controls T-cell measles virus differential expression immune-responses encoding gene CD150 SLAM in-vitro SAP
Megjelenés:	Blood. - 107 : 7 (2006), p. 2821-2829. -
További szerzők:	Gogolák Péter (1968-) (biológus, immunológus) Szatmári István (1971-) (biológus) Veres Ágota (laboráns) Erdős Erika Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Rajnavölgyi Éva (1950-) (immunológus) Terhorst, Cox Lányi Árpád (1962-) (biológus, immunológus)
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