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Results: 1 to 9 of 9

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Rif1 inhibits replication fork progression and controls DNA copy number in Drosophila.
Munden A, Rong Z, Sun A, Gangula R, Mallal S, Nordman JT
(2018) Elife 7:
MeSH Terms: Amino Acid Sequence, Animals, Carrier Proteins, DNA, DNA Replication, DNA-Binding Proteins, Drosophila Proteins, Drosophila melanogaster, Gene Dosage, Genome, Insect, Heat-Shock Response, Heterochromatin, Mutation, Protein Binding, Protein Domains, Reproducibility of Results, Salivary Glands
Show Abstract · Added March 3, 2020
Control of DNA copy number is essential to maintain genome stability and ensure proper cell and tissue function. In polyploid cells, the SNF2-domain-containing SUUR protein inhibits replication fork progression within specific regions of the genome to promote DNA underreplication. While dissecting the function of SUUR's SNF2 domain, we identified an interaction between SUUR and Rif1. Rif1 has many roles in DNA metabolism and regulates the replication timing program. We demonstrate that repression of DNA replication is dependent on Rif1. Rif1 localizes to active replication forks in a partially SUUR-dependent manner and directly regulates replication fork progression. Importantly, SUUR associates with replication forks in the absence of Rif1, indicating that Rif1 acts downstream of SUUR to inhibit fork progression. Our findings uncover an unrecognized function of the Rif1 protein as a regulator of replication fork progression.
© 2018, Munden et al.
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MeSH Terms
Mistargeting of a truncated Na-K-2Cl cotransporter in epithelial cells.
Koumangoye R, Omer S, Delpire E
(2018) Am J Physiol Cell Physiol 315: C258-C276
MeSH Terms: Animals, Cell Membrane, Cells, Cultured, Colon, Cytoplasm, Dogs, Epithelial Cells, Female, Madin Darby Canine Kidney Cells, Male, Mice, Oocytes, Salivary Glands, Sodium-Potassium-Chloride Symporters, Sodium-Potassium-Exchanging ATPase, Solute Carrier Family 12, Member 2, Xenopus laevis
Show Abstract · Added May 4, 2018
We recently reported the case of a young patient with multisystem failure carrying a de novo mutation in SLC12A2, the gene encoding the Na-K-2Cl cotransporter-1 (NKCC1). Heterologous expression studies in nonepithelial cells failed to demonstrate dominant-negative effects. In this study, we examined expression of the mutant cotransporter in epithelial cells. Using Madin-Darby canine kidney (MDCK) cells grown on glass coverslips, permeabilized support, and Matrigel, we show that the fluorescently tagged mutant cotransporter is expressed in cytoplasm and at the apical membrane and affects epithelium integrity. Expression of the mutant transporter at the apical membrane also results in the mislocalization of some of the wild-type transporter to the apical membrane. This mistargeting is specific to NKCC1 as the Na-K-ATPase remains localized on the basolateral membrane. To assess transporter localization in vivo, we created a mouse model using CRISPR/cas9 that reproduces the 11 bp deletion in exon 22 of Slc12a2. Although the mice do not display an overt phenotype, we show that the colon and salivary gland expresses wild-type NKCC1 abundantly at the apical pole, confirming the data obtained in cultured epithelial cells. Enough cotransporter must remain, however, on the basolateral membrane to participate in saliva secretion, as no significant decrease in saliva production was observed in the mutant mice.
1 Communities
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17 MeSH Terms
Members of the salivary gland surface protein (SGS) family are major immunogenic components of mosquito saliva.
King JG, Vernick KD, Hillyer JF
(2011) J Biol Chem 286: 40824-34
MeSH Terms: Animals, Anopheles, Computational Biology, Drosophila Proteins, Female, Gene Expression Regulation, Glue Proteins, Drosophila, Humans, Immunologic Factors, Proteolysis, Saliva, Salivary Glands, Time Factors
Show Abstract · Added February 5, 2016
Mosquitoes transmit Plasmodium and certain arboviruses during blood feeding, when they are injected along with saliva. Mosquito saliva interferes with the host's hemostasis and inflammation response and influences the transmission success of some pathogens. One family of mosquito salivary gland proteins, named SGS, is composed of large bacterial-type proteins that in Aedes aegypti were implicated as receptors for Plasmodium on the basal salivary gland surface. Here, we characterize the biology of two SGSs in the malaria mosquito, Anopheles gambiae, and demonstrate their involvement in blood feeding. Western blots and RT-PCR showed that Sgs4 and Sgs5 are produced exclusively in female salivary glands, that expression increases with age and after blood feeding, and that protein levels fluctuate in a circadian manner. Immunohistochemistry showed that SGSs are present in the acinar cells of the distal lateral lobes and in the salivary ducts of the proximal lobes. SDS-PAGE, Western blots, bite blots, and immunization via mosquito bites showed that SGSs are highly immunogenic and form major components of mosquito saliva. Last, Western and bioinformatic analyses suggest that SGSs are secreted via a non-classical pathway that involves cleavage into a 300-kDa soluble fragment and a smaller membrane-bound fragment. Combined, these data strongly suggest that SGSs play an important role in blood feeding. Together with their role in malaria transmission, we propose that SGSs could be used as markers of human exposure to mosquito bites and in the development of disease control strategies.
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13 MeSH Terms
Efficiency of salivary gland invasion by malaria sporozoites is controlled by rapid sporozoite destruction in the mosquito haemocoel.
Hillyer JF, Barreau C, Vernick KD
(2007) Int J Parasitol 37: 673-81
MeSH Terms: Aedes, Animals, Anopheles, Female, Host-Parasite Interactions, Phagocytosis, Plasmodium berghei, Plasmodium gallinaceum, Salivary Glands, Sporozoites
Show Abstract · Added February 5, 2016
For successful transmission to the vertebrate host, malaria sporozoites must migrate from the mosquito midgut to the salivary glands. Here, using purified sporozoites inoculated into the mosquito haemocoel, we show that salivary gland invasion is inefficient and that sporozoites have a narrow window of opportunity for salivary gland invasion. Only 19% of sporozoites invade the salivary glands, all invasion occurs within 8h at a rate of approximately 200 sporozoites per hour, and sporozoites that fail to invade within this time rapidly die and are degraded. Then, using natural release of sporozoites from oocysts, we show that haemolymph flow through the dorsal vessel facilitates proper invasion. Most mosquitoes had low steady-state numbers of circulating sporozoites, which is remarkable given the thousands of sporozoites released per oocyst, and suggests that sporozoite degradation is a rapid immune process most efficient in regions of high haemolymph flow. Only 2% of Anopheles gambiae haemocytes phagocytized Plasmodium berghei sporozoites, a rate insufficient to explain the extent of sporozoite clearance. Greater than 95% of haemocytes phagocytized Escherichia coli or latex particles, indicating that their failure to sequester large numbers of sporozoites is not due to an inability to engage in phagocytosis. These results reveal the operation of an efficient sporozoite-killing and degradation machinery within the mosquito haemocoel, which drastically limits the numbers of infective sporozoites in the mosquito salivary glands.
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10 MeSH Terms
Blocked acinar development, E-cadherin reduction, and intraepithelial neoplasia upon ablation of p120-catenin in the mouse salivary gland.
Davis MA, Reynolds AB
(2006) Dev Cell 10: 21-31
MeSH Terms: Age Factors, Animals, Animals, Newborn, Apoptosis, Cadherins, Carcinoma in Situ, Catenins, Cell Adhesion Molecules, Cell Differentiation, Cell Proliferation, Desmoglein 1, Embryo, Mammalian, Epithelial Cells, Gene Expression Regulation, Developmental, Immunohistochemistry, Membrane Glycoproteins, Mice, Mice, Knockout, Molecular Biology, Phosphoproteins, RNA, Messenger, Reverse Transcriptase Polymerase Chain Reaction, Salivary Glands, Skin, Sodium-Potassium-Exchanging ATPase, Trans-Activators, beta Catenin
Show Abstract · Added August 13, 2010
p120 catenin is thought to be a key regulator of E-cadherin function and stability, but its role(s) in vivo is poorly understood. To examine these directly, we generated a conditional p120 knockout mouse and targeted p120 ablation to the embryonic salivary gland. Surprisingly, acinar differentiation is completely blocked, resulting in a gland composed entirely of ducts. Moreover, p120 ablation causes E-cadherin deficiency in vivo and severe defects in adhesion, cell polarity, and epithelial morphology. These changes closely phenocopy high-grade intraepithelial neoplasia, a condition that, in humans, typically progresses to invasive cancer. Tumor-like protrusions appear immediately after p120 ablation at e14 and expand into the lumen until shortly after birth, at which time the animals die with completely occluded glands. The data reveal an unexpected role for p120 in salivary acinar development and show that p120 ablation by itself induces effects consistent with a role in tumor progression.
2 Communities
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27 MeSH Terms
Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments.
Kiseleva E, Allen TD, Rutherford S, Bucci M, Wente SR, Goldberg MW
(2004) J Struct Biol 145: 272-88
MeSH Terms: Animals, Cell Nucleus, Chironomidae, Cytoplasm, Immunohistochemistry, Microscopy, Electron, Scanning, Models, Biological, Mutation, Nuclear Pore, Nuclear Pore Complex Proteins, Protein Conformation, Ribosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Salivary Glands, Schizosaccharomyces, Temperature, Xenopus
Show Abstract · Added March 21, 2014
The nuclear pore complex (NPC) controls transport of macromolecules across the nuclear envelope. It is large and complex but appears to consist of only approximately 30 different proteins despite its mass of > 60MDa. Vertebrate NPC structure has been analyzed by several methods giving a comprehensive architectural model. Despite our knowledge of yeast nucleoporins, structural data is more limited and suggests the basic organization is similar to vertebrates, but may lack some peripheral and other components. Using field emission scanning electron microscopy to probe NPC structure we found that the yeast, like higher eukaryotic, NPCs contain similar peripheral components. We can detect cytoplasmic rings and evidence of nucleoplasmic rings in yeasts. A filamentous basket is present on the nucleoplasmic face and evidence for cytoplasmic filaments is shown. We observed a central structure, possibly the transporter, that which may be linked to the cytoplasmic ring by internal filaments. Immuno-gold labeling suggested that Nup159p may be attached to the cytoplasmic ring, whereas Nup116p may be associated, partly, with the cytoplasmic filaments. Analysis of a Nup57p mutant suggested a role in maintaining the stability of cytoplasmic components of the NPC. We conclude that peripheral NPC components appear similar in yeasts compared to higher organisms and present a revised model for yeast NPC structural composition.
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18 MeSH Terms
Roles of interferon-gamma and interleukin-4 in murine lupus.
Peng SL, Moslehi J, Craft J
(1997) J Clin Invest 99: 1936-46
MeSH Terms: Animals, Autoantibodies, Female, Immunoglobulin Isotypes, Interferon-gamma, Interleukin-4, Kidney, Liver, Lupus Erythematosus, Systemic, Male, Mice, Mice, Inbred C57BL, Mice, Inbred DBA, Mice, Inbred MRL lpr, Mice, Knockout, Mutation, Salivary Glands
Show Abstract · Added March 4, 2015
The systemic autoimmune syndrome of MRL/Mp-lpr/lpr (MRL/lpr) mice consists of severe pan-isotype hypergammaglobulinemia, autoantibody production, lymphadenopathy, and immune complex-associated end-organ disease. Its pathogenesis has been largely attributed to helper alphabeta T cells that may require critical cytokines to propagate pathogenic autoantibody production. To investigate the roles of prototypical Th1 and Th2 cytokines in the pathogenesis of murine lupus, IFN-gamma -/- and IL-4 -/- lupus-prone mice were generated by backcrossing cytokine knockout animals against MRL/lpr breeders. IFN-gamma -/- animals produced significantly reduced titers of IgG2a and IgG2b serum immunoglobulins as well as autoantibodies, but maintained comparable levels of IgG1 and IgE in comparison to cytokine-intact controls; in contrast, IL-4 -/- animals produced significantly less IgG1 and IgE serum immunoglobulins, but maintained comparable levels of IgG2a and IgG2b as well as autoantibodies in comparison to controls. Both IFN-gamma -/- and IL-4 -/- mice, however, developed significantly reduced lymphadenopathy and end-organ disease. These results suggest that IFN-gamma and IL-4 play opposing but dispensable roles in the development of lupus-associated hypergammaglobulinemia and autoantibody production; however, they both play prominent roles in the pathogenesis of murine lupus-associated tissue injury, as well as in lpr-induced lymphadenopathy.
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17 MeSH Terms
An edgewise look at basal epithelial cells: three-dimensional views of the rat prostate, mammary gland and salivary gland.
Hayward SW, Brody JR, Cunha GR
(1996) Differentiation 60: 219-27
MeSH Terms: Actins, Animals, Basal Metabolism, Cell Size, Epithelial Cells, Female, Image Processing, Computer-Assisted, Immunohistochemistry, Keratins, Male, Mammary Glands, Animal, Pregnancy, Prostate, Rats, Rats, Sprague-Dawley, Salivary Glands
Show Abstract · Added December 10, 2013
Wholemount immunocytochemical staining was used to visualize basal and luminal epithelial-cell-specific cytokeratin and smooth muscle alpha-actin expression in the developing and adult rat prostate, in the pregnant rat mammary gland and adult rat salivary gland. The stained samples were examined using an Edge R400 3D microscope. Images were collected in both single-image and stereo-pair formats. Prostatic basal epithelial cells were found to have a cell body covering an area of 52-62 microns 2. The mean footprint size of basal cells was not significantly different between prostatic lobes. Basal epithelial cells were most dense in the anterior and most sparse in the ventral prostatic lobes. Basal epithelial cells had a large body with many processes, which spread around the duct and projected between luminal cells towards the lumen. These processes closely approached their counterparts from adjacent basal cells. In the developing prostate the differentiation of the basal cells from undifferentiated epithelial cords was observed at the region of ductal widening associated with canalization. Following castration prostatic basal epithelial cells became more closely packed, though the size of individual cells was not significantly changed. There was a two-to four-fold increase in basal cell density by 7 days after surgery. Most prostatic luminal cells were found to have hexagonal bases though some were pentagonal in shape. Luminal cells had a mean basal area of 50 microns 2. In the prostate immunocytochemical staining against smooth muscle alpha-actin revealed discrete bands of muscle surrounding individual prostatic ducts. In the mammary and salivary glands the epithelium was organized into an alveolar arrangement. In the salivary gland a single basal epithelial cell covered the top of each alveolus with processes arranged down the side of the structure. In the mammary gland several basal cells were draped over each alveolus. The mammary and salivary gland basal cells expressed smooth muscle alpha-actin, indicating their myoepithelial phenotype. The organization of the mammary and salivary gland basal cells placed them in an ideal position to squeeze the alveolar structures.
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16 MeSH Terms
In situ localization of DNA topoisomerase II, a major polypeptide component of the Drosophila nuclear matrix fraction.
Berrios M, Osheroff N, Fisher PA
(1985) Proc Natl Acad Sci U S A 82: 4142-6
MeSH Terms: Animals, Cell Nucleus, DNA Topoisomerases, Type I, Drosophila melanogaster, Fluorescent Antibody Technique, Immunosorbent Techniques, Mitosis, Molecular Weight, Salivary Glands
Show Abstract · Added March 5, 2014
DNA topoisomerase II has been immunochemically identified on protein blots as a major polypeptide component of the Drosophila nuclear matrix-pore complex-lamina fraction. Indirect immunofluorescence analyses of larval cryosections have confirmed the nuclear localization of topoisomerase II in situ. Although apparently excluded from the nucleolus, the topoisomerase protein is otherwise distributed throughout the interior of interphase nuclei. Similar immunocytochemical studies performed with permeabilized whole giant cells from third-instar larval salivary glands have shown topoisomerase II to be largely restricted to the polytene chromosomes. Upon nuclear disassembly during mitosis, the topoisomerase polypeptide appears to redistribute diffusely throughout the cell. Faint immunofluorescent staining of mitotic chromosomes is also observed.
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9 MeSH Terms