119 research outputs found
A szegényháztól a produktív szociálpolitikáig
Recenzió: Nyilas Mihály(szerk). Szociálpolitika-történeti szöveggyűjtemény, ELTE-TáTK Szociális Munka és Szociálpolitikai Tanszék – Hilscher Rezső Szociálpolitikai Egyesület, Budapest 2008. A Szociális Szakképzés Könyvtára – Társadalomtörténeti Olvasókönyvek, 476 p
Szociálpolitika a 20. századi Magyarországon
Tomka Béla: Szociálpolitika a 20. századi Magyarországon európai perspektívában, Századvég Kiadó, Budapest 2003
Gyermekvédelem Szabolcs és Szatmár vármegyében, 1867–1950 között
Recenzió: Gaál Ibolya: A közigazgatás feladatkörébe utalt gyermekvédelem Szabolcs és Szatmár vármegyében 1867–1950. Nyíregyháza 2007. Szabolcs-Szatmár-Bereg Megyei Múzeumok Igazgatóságának kiadványai, 59. sz. 298 o
Lmo Mutants Reveal a Novel Role for Circadian Pacemaker Neurons in Cocaine-Induced Behaviors
Drosophila has been developed recently as a model system to investigate the molecular and neural mechanisms underlying responses to drugs of abuse. Genetic screens for mutants with altered drug-induced behaviors thus provide an unbiased approach to define novel molecules involved in the process. We identified mutations in the Drosophila LIM-only (LMO) gene, encoding a regulator of LIM-homeodomain proteins, in a genetic screen for mutants with altered cocaine sensitivity. Reduced Lmo function increases behavioral responses to cocaine, while Lmo overexpression causes the opposite effect, reduced cocaine responsiveness. Expression of Lmo in the principal Drosophila circadian pacemaker cells, the PDF-expressing ventral lateral neurons (LN(v)s), is sufficient to confer normal cocaine sensitivity. Consistent with a role for Lmo in LN(v) function, Lmo mutants also show defects in circadian rhythms of behavior. However, the role for LN(v)s in modulating cocaine responses is separable from their role as pacemaker neurons: ablation or functional silencing of the LN(v)s reduces cocaine sensitivity, while loss of the principal circadian neurotransmitter PDF has no effect. Together, these results reveal a novel role for Lmo in modulating acute cocaine sensitivity and circadian locomotor rhythmicity, and add to growing evidence that these behaviors are regulated by shared molecular mechanisms. The finding that the degree of cocaine responsiveness is controlled by the Drosophila pacemaker neurons provides a neuroanatomical basis for this overlap. We propose that Lmo controls the responsiveness of LN(v)s to cocaine, which in turn regulate the flies' behavioral sensitivity to the drug
Juno and CD9 protein network organization in oolemma of mouse oocyte
Juno and CD9 protein, expressed in oolemma, are known to be essential for sperm-oocyte binding and fusion. Although evidence exists that these two proteins cooperate, their interaction has not yet been demonstrated. Here in, we present Juno and CD9 mutual localization over the surface of mouse metaphase II oocytes captured using the 3D STED super-resolution technique. The precise localization of examined proteins was identified in different compartments of oolemma such as the microvillar membrane, planar membrane between individual microvilli, and the membrane of microvilli-free region. Observed variance in localization of Juno and CD9 was confirmed by analysis of transmission and scanning electron microscopy images, which showed a significant difference in the presence of proteins between selected membrane compartments. Colocalization analysis of super-resolution images based on Pearson’s correlation coefficient supported evidence of Juno and CD9 mutual position in the oolemma, which was identified by proximity ligation assay. Importantly, the interaction between Juno and CD9 was detected by co-immunoprecipitation and mass spectrometry in HEK293T/17 transfected cell line. For better understanding of experimental data, mouse Juno and CD9 3D structure were prepared by comparative homology modelling and several protein-protein flexible sidechain dockings were performed using the ClusPro server. The dynamic state of the proteins was studied in real-time at atomic level by molecular dynamics (MD) simulation. Docking and MD simulation predicted Juno-CD9 interactions and stability also suggesting an interactive mechanism. Using the multiscale approach, we detected close proximity of Juno and CD9 within microvillar oolemma however, not in the planar membrane or microvilli-free region. Our findings show yet unidentified Juno and CD9 interaction within the mouse oolemma protein network prior to sperm attachment. These results suggest that a Juno and CD9 interactive network could assist in primary Juno binding to sperm Izumo1 as a prerequisite to subsequent gamete membrane fusion
Functional characterization and phenotyping of RAB2A and Lactadherin/MFGE8 as boar sperm zona pellucida binding proteins
Mammalian fertilization begins with the species-specific binding of spermatozoa to the oocyte’s zona pellucida (ZP), a process mediated by multiple surface proteins forming a functional receptor complex. Among them, the Ras oncogene family protein RAB2A and lactadherin/MFGE8 (p47/SED1) were previously identified as ZP-binding candidates in pig; however, their functional roles in sperm-oocyte interactions remained unconfirmed. This study aimed to evaluate their involvement in sperm-ZP binding by using antibody-blocking and competitive binding assays with porcine oocytes. In parallel, we validated the specificity and functional relevance of two in-house raised monoclonal antibodies, 5C5 and 1H9, targeting RAB2A and lactadherin/MFGE8, respectively, and further characterized these proteins in boar spermatozoa. Immunofluorescence detection indicated that both RAB2A and lactadherin/MFGE8 became accessible on the sperm surface upon capacitation. Their surface localization at this stage supports their potential involvement in the primary sperm-ZP interactions preceding acrosomal exocytosis. Moreover, the sperm-specific 5C5 antibody detected reduced RAB2A levels in ejaculates from men with abnormal sperm parameters. This highlights the potential of RAB2A as a biomarker of sperm quality and acrosomal integrity, with promising translational relevance from animal models to humans. In vitro sperm-zona binding assays revealed that while in-house raised antibody treatments showed no significant inhibition, follow-up experiments using a commercial anti-RAB2A antibody demonstrated a significant reduction in sperm binding to the ZP of the oocyte. Both recombinant RAB2A (rc-RAB2A) and recombinant lactadherin (rc-lactadherin) significantly reduced sperm-ZP binding, highlighting their functional relevance. Our results support the role of RAB2A and lactadherin/MFGE8 in sperm-oocyte binding and highlight the utility of monoclonal antibodies 5C5 and 1H9 for sperm phenotyping. Future work should focus on identifying molecular interaction partners and signaling mechanisms that mediate the initiation of acrosomal exocytosis at fertilization
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