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In vivo administration of Gamendazole and Lonidamine

ABSTRACT: rat testis time changes Experimental details are found at Tash et al, Gamendazole, an orally active indazole carboxylic acid male contraceptive agent, targets HSP-90, eEF1A, and stimulates IL-1 transcription in Sertoli cells, Biol. Reprod. (2007) under review Keywords: time course

ORGANISM(S): Rattus norvegicus Rattus rattus

PROVIDER: GSE8485 | GEO | 2008/01/24

SECONDARY ACCESSION(S): PRJNA101575

REPOSITORIES: GEO

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Transcription profiling of rat AFTER IN vivo administration OF Gamendazole AND Lonidamine

Project description:rat testis time changes; Experimental details are found at Tash et al, Gamendazole, an orally active indazole carboxylic acid male contraceptive agent, targets HSP-90, eEF1A, and stimulates IL-1 transcription in Sertoli cells, Biol. Reprod. (2007) under review Experiment Overall Design: Adult male rats administered single ip dose of 6mg/kg Gamendazole or 25 mg/kg lonidamine or vehicle control (buffered DMSO) - testes harvested at 0 4 12 and 24 hr - 3 chips used for each time point

2008-04-10 | E-GEOD-8485 | biostudies-arrayexpress

Adjudin-induced germ cell loss from adult rat testes

Project description:This is a study to explore the transcriptional changes after Adjudin treatment in adult rat testes at three time points (control, 8 hour and 4 day). Adjudin, [1-(2,4-dichlorobenzyl)-1H-indazole-3-carbohydrazide], is a potential male contraceptive that targets the Sertoli-germ cell interface and causes germ cell depletion from the seminiferous epithelium. Adjudin has been proved to be a useful model to study the mechanisms that regulate junction restructuring in the testis. Keywords: Sertoli-germ cell adhesion regulation using an Adjudin model

2006-07-07 | GSE5131 | GEO

Expression data from cultured mouse spermatogonia cryopreserved on the International Space Station (ISS) or on Earth

Project description:Spermatogonial stem cells (SSCs) undergo self-renewal division to maintain spermatogenesis. In this study, we used SSCs for long-term cryopreservation in space flight. We derived germline stem cell (GS) cultures from DBA/2 mouse testes by supplementing GDNF and FGF2 (Kanatsu-Shinohara et al., 2003, Biol. Reprod. 69, 216-616). GS cells were cryopreserved in the ISS for 6 months. Frozen GS cells were thawed upon return to Earth and their gene expression profiles were analysed.

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Germline transmission of cryopreserved mouse spermatogonial stem cells maintained on the International Space Station

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Expression data from adult liver of offspring derived from cultured spermatogonia (GS cells) cryopreserved for a 6 months on the International Space Station (ISS) or on Earth.

Project description:Spermatogonial stem cells (SSCs) undergo self-renewal division to maintain spermatogenesis. In this study, we used SSCs for long-term cryopreservation in space flight. We derived germline stem cell (GS) cultures from DBA/2 mouse testes (Kanatsu-Shinohara et al., 2003, Biol. Reprod. 69, 216-616). GS cells were cryopreserved in the ISS for 6 months. Frozen GS cells were thawed upon return to Earth and tranplanted into the seminifelous tubules of infertile W mice. Recipients were housed with wild-type C57BL/6 females, and livers of F1 offspring were analyzed for gene expression.

2025-08-15 | GSE280404 | GEO

Dedicated chaperone at the ribosome safeguards the proteostasis network during eEF1A biogenesis

Project description:Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we find that the universal cotranslational machinery adapts to accommodate the challenging biogenesis of abundantly expressed eukaryotic translation elongation factor 1A (eEF1A). During eEF1A synthesis, chaperone Chp1 is recruited to the ribosome with the help of the nascent polypeptide-associated complex (NAC), where it safeguards eEF1A biogenesis. Aberrant eEF1A production triggers instant proteolysis, widespread protein aggregation, activation of Hsf1 stress transcription and compromises cellular fitness. The expression of pathogenic eEF1A2 variants linked to epileptic-dyskinetic encephalopathy is protected by Chp1. Thus, eEF1A is a difficult to fold protein that necessitates dedicated folding factor Chp1 at the ribosomal tunnel exit to protect the eukaryotic cell from proteostasis collapse.

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The dual methyltransferase METTL13 targets N-terminus and Lys55 of eEF1A and regulates codon-specific translation rates

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The novel lysine specific methyltransferase METTL21B affects mRNA translation through inducible and dynamic methylation of Lys-165 in human eukaryotic elongation factor 1 alpha (eEF1A)

Project description:Lysine methylation is abundant on histone proteins, representing a dynamic regulator of chromatin state and gene activity, but is also frequent on many nonhistone proteins, including eukaryotic elongation factor 1 alpha (eEF1A). However, the functional significance of eEF1Amethylation remains obscure and it has remained unclear whether eEF1A methylation is dynamic and subject to active regulation. We here demonstrate, using a wide range of in vitro and in vivo approaches, that the previously uncharacterized human methyltransferase METTL21B specifically targets Lys-165 in eEF1A in an aminoacyl-tRNA- and GTP-dependent manner. Interestingly, METTL21B mediated eEF1A methylation showed strong variation across different tissues and cell lines, and was induced by altering growth conditions or by treatment with certain ER-stress-inducing drugs, concomitant with an increase in METTL21B gene expression. Moreover, genetic ablation of METTL21B function in mammalian cells caused substantial alterations in mRNA translation, as measured by ribosome profiling. A non-canonical function for eEF1A in organization of the cellular cytoskeleton has been reported, and interestingly, METTL21B accumulated in centrosomes, in addition to the expected cytosolic localization. In summary, the present study identifies METTL21B as the enzyme responsible for methylation of eEF1A on Lys-165 and shows that this modification is dynamic, inducible and likely of regulatory importance.

2017-01-05 | GSE93133 | GEO

Expression data from Saccharomyces cerevisiae with eEF1A overexpression

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The structural scaffold of the TPLATE complex deforms the membrane during plant endocytosis

Project description:Eukaryotic cells maintain homeostasis of their outer membrane by controlled internalization of lipid and protein constituents by endocytosis (Kaksonen & Roux, Nat Rev Mol Cell Biol. 2018). Endocytosis is evolutionary conserved and utilizes similar structural folds. How these structural folds are combined into proteins and protein complexes however differs between eukaryotic kingdoms (Kraus, Pleskot & Van Damme, Ann review 2024). The TPLATE complex in plants is an evolutionary ancient protein module that combines several endocytic folds into a single octameric protein complex (Gadeyne et al., Cell 2014, Hirst et al., eLife 2014, More et al., Curr Biol. 2020). Its molecular architecture, lipid-nucleated condensate formation, and its requirement for clathrin cage curvature revealed its function in endocytosis initiation in plants (Yperman & Wang et al., Sci Adv. 2021, Dragwidge et al., Nat Cell Biol. 2024, Johnson et al., PNAS 2021). Mechanistic understanding of how this complex drives membrane deformation during plant endocytosis is, however, lacking. Here, we used an integrative structural approach to obtain a precise molecular structure of the TPLATE complex. In addition, our approach also allowed visualizing the structural flexibility that hallmarks this enigmatic complex. We prove that the intrinsic structural flexibility is required for its functionality and membrane recruitment. We map different lipid-binding preferences onto specific domains located at the curved face of the complex. Finally, we show that the crescent shape of the structured part of the complex is sufficient for membrane curvature generation. Our mechanistic insight answers the longstanding question of how plants can execute endocytosis without cytoskeletal-based force generation.

2025-11-06 | PXD056680 | Pride

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