10 results on '"Jimenez-Movilla, M."'
Search Results
2. Human sperm acrosome reaction is mediated by carbohydrate residues contained in the recombinant human ZP3
- Author
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Izquierdo, Mj, Jimenez-Movilla, M., Ramirez, Ma, Gutierrez-Adan, A., Girela, Jl, Gomez-Torres, Mj, Mondejar, I., Joaquin De Juan, Aviles, M., and Ballesta, J.
3. Editorial: Fertilization in the spotlight: Dynamics and mechanisms of sperm-egg interaction.
- Author
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Bianchi E, Jimenez-Movilla M, and Krauchunas AR
- Published
- 2022
- Full Text
- View/download PDF
4. Cytoplasmic cleavage of DPPA3 is required for intracellular trafficking and cleavage-stage development in mice.
- Author
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Shin SW, Vogt EJ, Jimenez-Movilla M, Baibakov B, and Dean J
- Subjects
- Amino Acid Motifs, Animals, Blastocyst metabolism, Cell Nucleus genetics, Cell Nucleus metabolism, Chromosomal Proteins, Non-Histone, Cytoplasm genetics, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Dioxygenases, Embryonic Development, Female, Gene Expression Regulation, Developmental, Lysosomal Membrane Proteins genetics, Lysosomal Membrane Proteins metabolism, Male, Mice genetics, Mice metabolism, Mice, Knockout, Pregnancy, Proteasome Endopeptidase Complex genetics, Proteasome Endopeptidase Complex metabolism, Protein Transport, Proteolysis, Proto-Oncogene Proteins genetics, Proto-Oncogene Proteins metabolism, Repressor Proteins chemistry, Repressor Proteins genetics, Zygote cytology, Zygote metabolism, Cytoplasm metabolism, Mice embryology, Repressor Proteins metabolism
- Abstract
Degradation of maternal proteins by the ubiquitin-proteasome system (UPS) accompanies the maternal-to-zygotic transition. DPPA3/Stella/PGC7, encoded by a maternal effect gene, is present in the nucleus and cytoplasm of zygotes and has been associated with protecting the female pronucleus from TET3-mediated demethylation. We now report that cytoplasmic DPPA3 is partially cleaved by the ubiquitin-proteasome system and an N-terminus fragment remains in the cytoplasm where it associates with early and re-cycling endosomes. If DPPA3 is absent or if cleavage is prevented, multiple vesicles coalesce/aggregate and markers of lysosomes are decreased. Fertilized eggs develop poorly into blastocysts, which results in significantly decreased fecundity of Dppa3
R60A transgenic mice. This phenocopies aspects of Lamp1/2 knockdowns and Dppa3KO embryos can be partially rescued in vitro by DPPA31-60 and to a lesser extent by LAMP1/2. Thus, the N-terminus of DPPA3 has a significant role in cytoplasmic vesicular trafficking in addition to its previously reported nuclear function.- Published
- 2017
- Full Text
- View/download PDF
5. ZP2 peptide beads select human sperm in vitro, decoy mouse sperm in vivo, and provide reversible contraception.
- Author
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Avella MA, Baibakov BA, Jimenez-Movilla M, Sadusky AB, and Dean J
- Subjects
- Acrosome physiology, Animals, Female, Fertilization physiology, Fertilization in Vitro, Humans, Male, Mice, Ovum chemistry, Zona Pellucida chemistry, Contraception methods, Peptides chemistry, Spermatozoa physiology
- Abstract
Gamete recognition in the female reproductive tract occurs at the surface of the zona pellucida surrounding ovulated eggs. The acellular zona matrix is composed of three (mouse) or four (human) proteins (ZP1 to ZP4), and the amino terminus of ZP2 is the primary sperm-binding ligand. Mouse and human sperm bind, respectively, to recombinant moZP2(35-149) and huZP2(39-154) peptides attached to agarose beads. Mouse ZP2 peptide beads markedly inhibited fertilization of ovulated mouse eggs inseminated in vitro and incubated overnight. Similarly, human ZP2 peptide beads prevented sperm binding and penetration of transgenic ZP2(Rescue) zonae pellucidae, in which human ZP2 replaced mouse ZP2. When mouse ZP2 peptide beads were transcervically deposited into the uterus, there was no change in mating behavior and copulatory plugs were present, but bound sperm did not progress into the oviduct and female mice were infertile. On average, contraception lasted >10 estrus cycles but was reversible with no detectable pathology in the reproductive tract. Despite the long-term contraceptive effect, initial sperm binding to the peptide beads was reversible in vitro. We exploited this observation to select human sperm that were better able to penetrate the zonae of human ZP2(Rescue) eggs, and the approach holds promise for identifying superior sperm for human assisted reproductive technologies (ART). We conclude that the amino-terminal ZP2 peptide supports sperm binding, which is initially reversible but, with time, becomes irreversible. Short-term, reversible binding may be useful in selecting sperm for ART, and long-term binding decoys sperm and results in effective contraception in mice., (Copyright © 2016, American Association for the Advancement of Science.)
- Published
- 2016
- Full Text
- View/download PDF
6. Figla-Cre transgenic mice expressing myristoylated EGFP in germ cells provide a model for investigating perinatal oocyte dynamics.
- Author
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Lin RS, Jimenez-Movilla M, and Dean J
- Subjects
- Animals, Female, Gene Order, Gene Targeting, Genetic Vectors genetics, Male, Mice, Mice, Transgenic, Ovary metabolism, Spermatogonia metabolism, Gene Expression, Germ Cells metabolism, Green Fluorescent Proteins genetics, Oocytes metabolism
- Abstract
FIGLA (Factor in the germline, alpha) is a bHLH transcription factor expressed abundantly in female and less so in male germ cells. Mice lacking FIGLA do not form primordial follicles in the ovary and females are sterile, but there is no obvious phenotype in males. Using the Figla promoter to express Cre recombinase, we have established mEGFP/mTomato reporter mice with green germ cells and red somatic tissue. These mice were crossed into the Figla null background to accelerate perinatal oocyte loss. Live imaging of cultured newborn ovaries provides evidence that few oocytes egress and the vast majority disappear within the confines of the ovary. Although a cohort of mobile, phagocytic cells was observed, macrophage depletion in Csf1(op/op) mice did not affect oocyte loss. Investigations with TUNEL assays and caspase inhibitors suggest that apoptosis plays a role in the perinatal loss of oocyte in female mice. These results establish the utility of Figla-EGFP/Cre; mTomato/mEGFP in investigating germ cell dynamics in prepubertal mice.
- Published
- 2014
- Full Text
- View/download PDF
7. Disruption of Ttll5/stamp gene (tubulin tyrosine ligase-like protein 5/SRC-1 and TIF2-associated modulatory protein gene) in male mice causes sperm malformation and infertility.
- Author
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Lee GS, He Y, Dougherty EJ, Jimenez-Movilla M, Avella M, Grullon S, Sharlin DS, Guo C, Blackford JA Jr, Awasthi S, Zhang Z, Armstrong SP, London EC, Chen W, Dean J, and Simons SS Jr
- Subjects
- Animals, Carrier Proteins genetics, Gene Expression Regulation genetics, Infertility, Male genetics, Infertility, Male pathology, Male, Mice, Mice, Mutant Strains, Nuclear Receptor Coactivator 1 genetics, Nuclear Receptor Coactivator 1 metabolism, Nuclear Receptor Coactivator 2 genetics, Nuclear Receptor Coactivator 2 metabolism, Protein Processing, Post-Translational genetics, Spermatozoa pathology, Testis pathology, Tubulin genetics, Tubulin metabolism, Carrier Proteins metabolism, Gene Deletion, Infertility, Male metabolism, Sperm Motility, Spermatozoa metabolism, Testis metabolism
- Abstract
TTLL5/STAMP (tubulin tyrosine ligase-like family member 5) has multiple activities in cells. TTLL5 is one of 13 TTLLs, has polyglutamylation activity, augments the activity of p160 coactivators (SRC-1 and TIF2) in glucocorticoid receptor-regulated gene induction and repression, and displays steroid-independent growth activity with several cell types. To examine TTLL5/STAMP functions in whole animals, mice were prepared with an internal deletion that eliminated several activities of the Stamp gene. This mutation causes both reduced levels of STAMP mRNA and C-terminal truncation of STAMP protein. Homozygous targeted mutant (Stamp(tm/tm)) mice appear normal except for marked decreases in male fertility associated with defects in progressive sperm motility. Abnormal axonemal structures with loss of tubulin doublets occur in most Stamp(tm/tm) sperm tails in conjunction with substantial reduction in α-tubulin polyglutamylation, which closely correlates with the reduction in mutant STAMP mRNA. The axonemes in other structures appear unaffected. There is no obvious change in the organs for sperm development of WT versus Stamp(tm/tm) males despite the levels of WT STAMP mRNA in testes being 20-fold higher than in any other organ examined. This defect in male fertility is unrelated to other Ttll genes or 24 genes previously identified as important for sperm function. Thus, STAMP appears to participate in a unique, tissue-selective TTLL-mediated pathway for α-tubulin polyglutamylation that is required for sperm maturation and motility and may be relevant for male fertility.
- Published
- 2013
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8. ZP2 and ZP3 cytoplasmic tails prevent premature interactions and ensure incorporation into the zona pellucida.
- Author
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Jimenez-Movilla M and Dean J
- Subjects
- Animals, CHO Cells, Cell Membrane chemistry, Cell Membrane genetics, Cell Membrane metabolism, Cricetinae, Cricetulus, Egg Proteins chemistry, Egg Proteins genetics, Female, Membrane Glycoproteins chemistry, Membrane Glycoproteins genetics, Mice, Oocytes chemistry, Oocytes metabolism, Protein Binding, Protein Structure, Tertiary, Protein Transport, Receptors, Cell Surface chemistry, Receptors, Cell Surface genetics, Zona Pellucida chemistry, Zona Pellucida Glycoproteins, Egg Proteins metabolism, Membrane Glycoproteins metabolism, Receptors, Cell Surface metabolism, Zona Pellucida metabolism
- Abstract
The zona pellucida contains three proteins (ZP1, ZP2, ZP3), the precursors of which possess signal peptides, 'zona' domains and short (9-15 residue) cytoplasmic tails downstream of a transmembrane domain. The ectodomains of ZP2 and ZP3 are sufficient to form the insoluble zona matrix and yet each protein traffics through oocytes without oligomerization. ZP2 and ZP3 were fluorescently tagged and molecular interactions were assayed by fluorescent complementation in CHO cells and growing oocytes. ZP2 and ZP3 traffic independently, but colocalize at the plasma membrane. However, protein-protein interactions were observed only after release and incorporation of ZP2 and ZP3 into the extracellular matrix surrounding mouse oocytes. In the absence of their hydrophilic cytoplasmic tails, ZP2 and ZP3 interacted within the cell and did not participate in the zona pellucida. A heterologous GPI-anchored 'zona' domain protein fused with the cytoplasmic tails was integrated into the zona matrix. We conclude that the cytoplasmic tails are sufficient and necessary to prevent intracellular oligomerization while ensuring incorporation of processed ZP2 and ZP3 into the zona pellucida.
- Published
- 2011
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- View/download PDF
9. FIGLA, a basic helix-loop-helix transcription factor, balances sexually dimorphic gene expression in postnatal oocytes.
- Author
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Hu W, Gauthier L, Baibakov B, Jimenez-Movilla M, and Dean J
- Subjects
- Animals, Animals, Newborn, Basic Helix-Loop-Helix Transcription Factors deficiency, Basic Helix-Loop-Helix Transcription Factors genetics, Fatty Acids genetics, Fatty Acids physiology, Fatty Alcohols, Female, Gene Expression, Male, Mice, Mice, Knockout, Mice, Transgenic, Oogenesis genetics, Oogenesis physiology, Ovary metabolism, RNA, Messenger genetics, RNA, Messenger metabolism, Recombinant Proteins genetics, Recombinant Proteins metabolism, Sex Characteristics, Testis metabolism, Basic Helix-Loop-Helix Transcription Factors metabolism, Oocytes metabolism
- Abstract
Maintenance of sex-specific germ cells requires balanced activation and repression of genetic hierarchies to ensure gender-appropriate development in mammals. Figla (factor in the germ line, alpha) encodes a germ cell-specific basic helix-loop-helix transcription factor first identified as an activator of oocyte genes. In comparing the ovarian proteome of normal and Figla null newborn mice, 18 testis-specific or -enhanced proteins were identified that were more abundant in Figla null ovaries than in normal ovaries. Transgenic mice, ectopically expressing Figla in male germ cells, downregulated a subset of these genes and demonstrated age-related sterility associated with impaired meiosis and germ cell apoptosis. Testis-associated genes, including Tdrd1, Tdrd6, and Tdrd7, were suppressed in the transgenic males with a corresponding disruption of the sperm chromatoid body and mislocalization of MVH and MILI proteins, previously implicated in posttranscriptional processing of RNA. These data demonstrate that physiological expression of Figla plays a critical dual role in activation of oocyte-associated genes and repression of sperm-associated genes during normal postnatal oogenesis.
- Published
- 2010
- Full Text
- View/download PDF
10. Hamster zona pellucida is formed by four glycoproteins: ZP1, ZP2, ZP3, and ZP4.
- Author
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Izquierdo-Rico MJ, Jimenez-Movilla M, Llop E, Perez-Oliva AB, Ballesta J, Gutierrez-Gallego R, Jimenez-Cervantes C, and Aviles M
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Cricetinae, Egg Proteins classification, Egg Proteins genetics, Female, Humans, Membrane Glycoproteins classification, Membrane Glycoproteins genetics, Mice, Molecular Sequence Data, Open Reading Frames, Phylogeny, Protein Isoforms classification, Protein Isoforms genetics, Rats, Receptors, Cell Surface classification, Receptors, Cell Surface genetics, Sequence Alignment, Zona Pellucida Glycoproteins, Egg Proteins chemistry, Membrane Glycoproteins chemistry, Mesocricetus, Protein Isoforms chemistry, Receptors, Cell Surface chemistry, Zona Pellucida chemistry
- Abstract
The zona pellucida (ZP) is an extracellular glycoprotein matrix that surrounds all mammalian oocytes. Recent data have shown the presence of four glycoproteins (ZP1, ZP2, ZP3, and ZP4) in the ZP of human and rat rather than the three glycoproteins proposed in the mouse model. In the hamster (Mesocricetus auratus), it was previously described that ZP was composed of three different glycoproteins, called ZP1, ZP2, and ZP3, even though only ZP2 and ZP3 have been cloned thus far. The aim of the study was to determine whether hamster might also express four, rather than three, ZP proteins. The full-length cDNAs encoding hamster ZP glycoproteins 1 and 4 were isolated using rapid amplification cDNA ends (RACE). The cDNA of ZP1 contains an open reading frame of 1851 nucleotides encoding a polypeptide of 616 amino acid residues. The amino acid sequence of ZP1 revealed a high homology with other mammalian species like human (66%), rat (80%), and mouse (80%). The cDNA of ZP4 contains an open reading frame of 1632 nucleotides encoding a polypeptide of 543 amino acid residues. The deduced amino acid sequence of ZP4 revealed high overall homology with rat (82%) and human (78%). Subsequent mass spectrometric analysis of the hamster ZP allowed identification of peptides from all four glycoproteins. The data presented in this study provide evidence, for the first time, that the hamster ZP matrix is composed of four glycoproteins.
- Published
- 2009
- Full Text
- View/download PDF
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