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Journal articles on the topic 'N-WASP'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 January 2023

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1

Liu, Chaohong, Shruti Sharma, Heather Miller, et al. "Pivotal roles of both Wiskott-Aldrich syndrome protein (WASP) and N-WASP in the activation and attenuation of the B cell receptor (P1093) (42.1)." Journal of Immunology 188, no. 1_Supplement (2012): 42.1. http://dx.doi.org/10.4049/jimmunol.188.supp.42.1.

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Abstract Lymphocytes express both Wiskott-Aldrich syndrome protein (WASP) and N-WASP. WASP deficiency, the cause of WAS, generates more severe defects in T-cells than B cells, suggesting a strong compensatory role of N-WASP in B cells. Using knockout mouse models, this study shows that WASP knockout (WKO) reduces B cell spreading, B cell receptor (BCR) aggregation, tyrosine phosphorylation, Btk phosphorylation and F-actin accumulation at the B cell surface induced by membrane-associated antigen, and WASP/N-WASP double knockout nearly abolished these activities. However, in B cells with N-WASP

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Adamo, Shelley A. "Feeding suppression in the tobacco hornworm, Manduca sexta: costs and benefits to the parasitic wasp Cotesia congregata." Canadian Journal of Zoology 76, no. 9 (1998): 1634–40. http://dx.doi.org/10.1139/z98-105.

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While the larvae of the parasitic wasp Cotesia congregata developed inside the tobacco hornworm, Manduca sexta, the host's behaviour was similar to that of unparasitized M. sexta. However, once the wasps had exited the host to spin their cocoons, M. sexta stopped feeding. Unparasitized M. sexta ate C. congregata cocoons, which suggests that cessation of feeding by parasitized M. sexta prevented them from consuming the wasps' cocoons. However, suppression of host feeding might be expected to lead to increased host mortality. Host mortality decreased wasp survival. Few cocoons (18%, n = 43) atta

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Clemente, Mateus Aparecido, Karine Munck Vieira, Núbia Ribeiro Campos, Kleber Del-Claro, and Fábio Prezoto. "Social wasp guild (Hymenoptera: Vespidae) visiting flowers in two of the phytophysiognomic formations: Riparian Forest and campos rupestres." Sociobiology 64, no. 2 (2017): 217. http://dx.doi.org/10.13102/sociobiology.v64i2.1364.

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Social wasps are part of the floral visitor guild. In this study we investigated the distribution of flower-visiting wasp species in two phytophysiognomies in the State Park of Ibitipoca, Minas Gerais, Brazil. We inspected flowering plants with visiting wasps along a 1 km transect in riparian forest and another 1 km transect in campos rupestres over the course of one year, for a total sampling effort of 240 hours. We found a total of 103 individuals with 15 species distributed among 7 genera, the most common belonging to the Erythroxylaceae (n = 10) and Asteraceae (n = 10) families. Asteraceae

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Martinez-Quiles, Narcisa, Hsin-Yi Henry Ho, Marc W. Kirschner, Narayanaswamy Ramesh, and Raif S. Geha. "Erk/Src Phosphorylation of Cortactin Acts as a Switch On-Switch Off Mechanism That Controls Its Ability To Activate N-WASP." Molecular and Cellular Biology 24, no. 12 (2004): 5269–80. http://dx.doi.org/10.1128/mcb.24.12.5269-5280.2004.

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ABSTRACT The Arp2/3 complex can be independently activated to initiate actin polymerization by the VCA domain of WASP family members and by the acidic N-terminal and F-actin-binding repeat region of cortactin, which possesses a C-terminal SH3 domain. Cortactin is a target for phosphorylation by Src tyrosine kinases and by serine/threonine kinases that include Erk. Here we demonstrate that cortactin binds N-WASP and WASP via its SH3 domain, induces in vitro N-WASP-mediated actin polymerization, and colocalizes with N-WASP and WASP at sites of active actin polymerization. Erk phosphorylation and

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Park, Haein, та Dianne Cox. "Cdc42 Regulates FcγReceptor-mediated Phagocytosis through the Activation and Phosphorylation of Wiskott-Aldrich Syndrome Protein (WASP) and Neural-WASP". Molecular Biology of the Cell 20, № 21 (2009): 4500–4508. http://dx.doi.org/10.1091/mbc.e09-03-0230.

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Cdc42 is a key regulator of the actin cytoskeleton and activator of Wiskott-Aldrich syndrome protein (WASP). Although several studies have separately demonstrated the requirement for both Cdc42 and WASP in Fcγreceptor (FcγR)-mediated phagocytosis, their precise roles in the signal cascade leading to engulfment are still unclear. Reduction of endogenous Cdc42 expression by using RNA-mediated interference (short hairpin RNA [shRNA]) severely impaired the phagocytic capacity of RAW/LR5 macrophages, due to defects in phagocytic cup formation, actin assembly, and pseudopod extension. Addition of wi

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6

Liu, Guang-hua, Jian Chen, Zhi-gang Ji, and Li Zhou. "Expression of Neural Wiskott-Aldrich Syndrome Protein in Clear Cell Renal Cell Carcinoma and Its Correlation with Clinicopathological Features." Urologia Internationalis 95, no. 1 (2014): 79–85. http://dx.doi.org/10.1159/000365595.

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Introduction: Neural Wiskott-Aldrich syndrome protein (N-WASP) expression is associated with tumor cell invasion and migration. However, its expression status in clear cell renal cell carcinoma (CCRCC) remains unclear. We examined the level of N-WASP in CCRCC and its association with clinicopathological features characteristic. Materials and Methods: 73 CCRCC patients who underwent radical nephrectomy or partial nephrectomy were enrolled. Immunohistochemical staining for N-WASP was performed on tissue microarrays constructed from tumor and para-tumor tissue obtained from these patients. The di

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7

Shcherbina, Anna, Hiroaki Miki, Dianne M. Kenney, Fred S. Rosen, Tadaomi Takenawa, and Eileen Remold-O'Donnell. "WASP and N-WASP in human platelets differ in sensitivity to protease calpain." Blood 98, no. 10 (2001): 2988–91. http://dx.doi.org/10.1182/blood.v98.10.2988.

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Abstract Mutations of Wiskott-Aldrich syndrome protein (WASP) underlie the severe thrombocytopenia and immunodeficiency of the Wiskott-Aldrich syndrome. WASP, a specific blood cell protein, and its close homologue, the broadly distributed N-WASP, function in dynamic actin polymerization processes. Here it is demonstrated that N-WASP is expressed along with WASP, albeit at low levels, in human blood cells. The presence of approximately 160 nmol/L rapidly acting N-WASP molecules may explain the normal capacity of WASP-negative patient platelets for early agonist-induced aggregation and filopodia

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8

Volpi, Stefano, Elettra Santori, Katrina Abernethy, et al. "N-WASP is required for B-cell–mediated autoimmunity in Wiskott-Aldrich syndrome." Blood 127, no. 2 (2016): 216–20. http://dx.doi.org/10.1182/blood-2015-05-643817.

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Key Points Mice lacking both WASP and N-WASP in B lymphocytes have impaired response to T-cell-dependent antigens and defective B-cell activation. Deletion of N-WASP in B cells attenuates autoimmunity in WASP-deficient mice.

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9

Rohatgi, Rajat, Hsin-yi Henry Ho, and Marc W. Kirschner. "Mechanism of N-Wasp Activation by Cdc42 and Phosphatidylinositol 4,5-Bisphosphate." Journal of Cell Biology 150, no. 6 (2000): 1299–310. http://dx.doi.org/10.1083/jcb.150.6.1299.

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Neuronal Wiskott-Aldrich Syndrome protein (N-WASP) transmits signals from Cdc42 to the nucleation of actin filaments by Arp2/3 complex. Although full-length N-WASP is a weak activator of Arp2/3 complex, its activity can be enhanced by upstream regulators such as Cdc42 and PI(4,5)P2. We dissected this activation reaction and found that the previously described physical interaction between the NH2-terminal domain and the COOH-terminal effector domain of N-WASP is a regulatory interaction because it can inhibit the actin nucleation activity of the effector domain by occluding the Arp2/3 binding s

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10

Zhang, Wenwu, Yidi Wu, Liping Du, Dale D. Tang, and Susan J. Gunst. "Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle." American Journal of Physiology-Cell Physiology 288, no. 5 (2005): C1145—C1160. http://dx.doi.org/10.1152/ajpcell.00387.2004.

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Contractile stimulation has been shown to initiate actin polymerization in smooth muscle tissues, and this actin polymerization is required for active tension development. We evaluated whether neuronal Wiskott-Aldrich syndrome protein (N-WASp)-mediated activation of the actin-related proteins 2 and 3 (Arp2/3) complex regulates actin polymerization and tension development initiated by muscarinic stimulation in canine tracheal smooth muscle tissues. In vitro, the COOH-terminal CA domain of N-WASp acts as an inhibitor of N-WASp-mediated actin polymerization; whereas the COOH-terminal VCA domain o

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Takenawa, T., and H. Miki. "WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement." Journal of Cell Science 114, no. 10 (2001): 1801–9. http://dx.doi.org/10.1242/jcs.114.10.1801.

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Reorganization of cortical actin filaments plays critical roles in cell movement and pattern formation. Recently, the WASP and WAVE family proteins WASP and N-WASP, and WAVE1, WAVE2 and WAVE3 have been shown to regulate cortical actin filament reorganization in response to extracellular stimuli. These proteins each have a verprolin-homology (V) domain, cofilin-homology (C) domain and an acidic (A) region at the C-terminus, through which they activate the Arp2/3 complex, leading to rapid actin polymerization. N-WASP is usually present as an inactive form in which the VCA region is masked. Coope

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Somavilla, Alexandre, Paulo C. S. Barroso, Marcos Aragão, Sidnei Mateus, and Rodolpho S. T. Menezes. "An integrative taxonomic and phylogenetic approach reveals a new Neotropical swarm-founding social wasp, Pseudopolybia cryptica sp. n. (Vespidae: Polistinae: Epiponini)." Arthropod Systematics & Phylogeny 79 (April 16, 2021): 25–35. http://dx.doi.org/10.3897/asp.79.e64304.

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Phenotypic characters are traditionally the main information for species discrimination in taxonomic studies of invertebrates. However, the presence of inter- and intraspecific polymorphism makes it difficult to identify species in many groups such as Neotropical social wasps. Herein, we examined different sources of biological information such as adult morphology, male genitalia, nest architecture, and genetic data applying an integrative taxonomic approach to study pinned museum specimens belonging to the social wasp genus Pseudopolybia de Saussure, 1863. Based on multiple independent lines

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Khanduja, Nimisha, and Jeffrey R. Kuhn. "Processive acceleration of actin barbed-end assembly by N-WASP." Molecular Biology of the Cell 25, no. 1 (2014): 55–65. http://dx.doi.org/10.1091/mbc.e12-11-0781.

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Neuronal Wiskott–Aldrich syndrome protein (N-WASP)–activated actin polymerization drives extension of invadopodia and podosomes into the basement layer. In addition to activating Arp2/3, N-WASP binds actin-filament barbed ends, and both N-WASP and barbed ends are tightly clustered in these invasive structures. We use nanofibers coated with N-WASP WWCA domains as model cell surfaces and single-actin-filament imaging to determine how clustered N-WASP affects Arp2/3-independent barbed-end assembly. Individual barbed ends captured by WWCA domains grow at or below their diffusion-limited assembly r

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Katanov, Christina, Nurit Novak, Anya Vainshtein, Ofra Golani, Jeffery L. Dupree, and Elior Peles. "N-Wasp Regulates Oligodendrocyte Myelination." Journal of Neuroscience 40, no. 32 (2020): 6103–11. http://dx.doi.org/10.1523/jneurosci.0912-20.2020.

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15

Bickenson, Antony F. "N-WASP supports junctional integrity." Nature Reviews Molecular Cell Biology 12, no. 9 (2011): 548–49. http://dx.doi.org/10.1038/nrm3172.

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Mizutani, Kiyohito, Shiro Suetsugu, and Tadaomi Takenawa. "FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-dependent microspike formation." Biochemical and Biophysical Research Communications 313, no. 3 (2004): 468–74. http://dx.doi.org/10.1016/j.bbrc.2003.11.139.

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Harlander, Ronald S., Michael Way, Qun Ren, Dale Howe, Scott S. Grieshaber, and Robert A. Heinzen. "Effects of Ectopically Expressed Neuronal Wiskott-Aldrich Syndrome Protein Domains on Rickettsia rickettsii Actin-Based Motility." Infection and Immunity 71, no. 3 (2003): 1551–56. http://dx.doi.org/10.1128/iai.71.3.1551-1556.2003.

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ABSTRACT Neuronal Wiskott-Aldrich syndrome protein (N-WASP) and the actin-related protein 2/3 (Arp2/3) complex have emerged as critical host proteins that regulate pathogen actin-based motility. Actin tail formation and motility in Listeria monocytogenes require the Arp2/3 complex but bypasses N-WASP signaling. Motility of Shigella flexneri and vaccinia virus requires both N-WASP and the Arp2/3 complex. Functional roles for these cytoskeletal regulatory proteins in actin-based motility of Rickettsia rickettsii have not been established. In this study, functional domains of N-WASP tagged with g

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Guerriero, Christopher J., and Ora A. Weisz. "N-WASP inhibitor wiskostatin nonselectively perturbs membrane transport by decreasing cellular ATP levels." American Journal of Physiology-Cell Physiology 292, no. 4 (2007): C1562—C1566. http://dx.doi.org/10.1152/ajpcell.00426.2006.

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Wiskott-Aldrich syndrome protein (WASP) and WAVE stimulate actin-related protein (Arp)2/3-mediated actin polymerization, leading to diverse downstream effects, including the formation and remodeling of cell surface protrusions, modulation of cell migration, and intracytoplasmic propulsion of organelles and pathogens. Selective inhibitors of individual Arp2/3 activators would enable more exact dissection of WASP- and WAVE-dependent cellular pathways and are potential therapeutic targets for viral pathogenesis. Wiskostatin is a recently described chemical inhibitor that selectively inhibits neur

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SUETSUGU, Shiro, Tohru TEZUKA, Toshifumi MORIMURA, et al. "Regulation of actin cytoskeleton by mDab1 through N-WASP and ubiquitination of mDab1." Biochemical Journal 384, no. 1 (2004): 1–8. http://dx.doi.org/10.1042/bj20041103.

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Migration of cells is critical to development of the central nervous system. Reelin, which was identified from the reeler mutant mice having a defect in the multilamellar structure of the brain, is thought to be a key signalling molecule that functions as a cue for determination of cell position. mDab1 (mouse Disabled homologue 1) functions downstream of Reelin. However, the mechanism by which mDab1 regulates cell migration during brain development is unknown. In the present paper, we show that mDab1 associates with N-WASP (neuronal Wiskott–Aldrich syndrome protein) in vitro and in brains of e

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Legg, John A., Guillaume Bompard, John Dawson, et al. "N-WASP Involvement in Dorsal Ruffle Formation in Mouse Embryonic Fibroblasts." Molecular Biology of the Cell 18, no. 2 (2007): 678–87. http://dx.doi.org/10.1091/mbc.e06-06-0569.

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The Wiskott–Aldrich syndrome protein (WASP) family activates the Arp2/3 complex leading to the formation of new actin filaments. Here, we study the involvement of Scar1, Scar2, N-WASP, and Arp2/3 complex in dorsal ruffle formation in mouse embryonic fibroblasts (MEFs). Using platelet-derived growth factor to stimulate circular dorsal ruffle assembly in primary E13 and immortalized E9 Scar1+/+and Scar1 null MEFs, we establish that Scar1 loss does not impair the formation of dorsal ruffles. Reduction of Scar2 protein levels via small interfering RNA (siRNA) also did not affect dorsal ruffle prod

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Okrut, Julia, Sumit Prakash, Qiong Wu, Mark J. S. Kelly, and Jack Taunton. "Allosteric N-WASP activation by an inter-SH3 domain linker in Nck." Proceedings of the National Academy of Sciences 112, no. 47 (2015): E6436—E6445. http://dx.doi.org/10.1073/pnas.1510876112.

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Actin filament networks assemble on cellular membranes in response to signals that locally activate neural Wiskott–Aldrich-syndrome protein (N-WASP) and the Arp2/3 complex. An inactive conformation of N-WASP is stabilized by intramolecular contacts between the GTPase binding domain (GBD) and the C helix of the verprolin-homology, connector-helix, acidic motif (VCA) segment. Multiple SH3 domain-containing adapter proteins can bind and possibly activate N-WASP, but it remains unclear how such binding events relieve autoinhibition to unmask the VCA segment and activate the Arp2/3 complex. Here, w

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Yu, Xinzi, Tobias Zech, Laura McDonald, et al. "N-WASP coordinates the delivery and F-actin–mediated capture of MT1-MMP at invasive pseudopods." Journal of Cell Biology 199, no. 3 (2012): 527–44. http://dx.doi.org/10.1083/jcb.201203025.

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Metastasizing tumor cells use matrix metalloproteases, such as the transmembrane collagenase MT1-MMP, together with actin-based protrusions, to break through extracellular matrix barriers and migrate in dense matrix. Here we show that the actin nucleation–promoting protein N-WASP (Neural Wiskott-Aldrich syndrome protein) is up-regulated in breast cancer, and has a pivotal role in mediating the assembly of elongated pseudopodia that are instrumental in matrix degradation. Although a role for N-WASP in invadopodia was known, we now show how N-WASP regulates invasive protrusion in 3D matrices. In

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Suetsugu, Shiro, Hiroaki Miki, Hideki Yamaguchi, Takeshi Obinata, and Tadaomi Takenawa. "Enhancement of branching efficiency by the actin filament-binding activity of N-WASP/WAVE2." Journal of Cell Science 114, no. 24 (2001): 4533–42. http://dx.doi.org/10.1242/jcs.114.24.4533.

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The actin-related protein (Arp) 2/3 complex is an essential regulator of de novo actin filament formation. Arp2/3 nucleates the polymerization of actin and creates branched actin filaments when activated by Arp2/3-complex activating domain (VCA) of Wiskott-Aldrich syndrome proteins (WASP family proteins). We found that the branching of actin filaments on pre-existing ADP filaments mediated by the Arp2/3 complex is twice as efficient when Arp2/3 was activated by wild-type neural WASP (N-WASP) or WASP-family verprolin-homologous protein (WAVE) 2 than when activated by the VCA domain alone. By co

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Fukuoka, Maiko, Shiro Suetsugu, Hiroaki Miki, Kiyoko Fukami, Takeshi Endo, and Tadaomi Takenawa. "A Novel Neural Wiskott-Aldrich Syndrome Protein (N-Wasp) Binding Protein, Wish, Induces Arp2/3 Complex Activation Independent of Cdc42." Journal of Cell Biology 152, no. 3 (2001): 471–82. http://dx.doi.org/10.1083/jcb.152.3.471.

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We identified a novel adaptor protein that contains a Src homology (SH)3 domain, SH3 binding proline-rich sequences, and a leucine zipper-like motif and termed this protein WASP interacting SH3 protein (WISH). WISH is expressed predominantly in neural tissues and testis. It bound Ash/Grb2 through its proline-rich regions and neural Wiskott-Aldrich syndrome protein (N-WASP) through its SH3 domain. WISH strongly enhanced N-WASP–induced Arp2/3 complex activation independent of Cdc42 in vitro, resulting in rapid actin polymerization. Furthermore, coexpression of WISH and N-WASP induced marked form

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Chung, Yat Joong, Amrita Salvi, Pazhanichamy Kalailingam, et al. "N-WASP Attenuates Cell Proliferation and Migration through ERK2-Dependent Enhanced Expression of TXNIP." Biology 11, no. 4 (2022): 582. http://dx.doi.org/10.3390/biology11040582.

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Neural Wiskott–Aldrich Syndrome Protein (N-WASP) regulates actin cytoskeleton remodeling. It has been known that reduced N-WASP expression in breast and colorectal cancers is associated with poor prognosis. Here, we found reduced N-WASP expression in squamous cell carcinoma (SCC) patient samples. The SCC cell line HSC-5 with reduced N-WASP expression was used to generate HSC-5CN (control) and HSC-5NW (N-WASP overexpression) cells. HSC-5NW cells had reduced cell proliferation and migration compared to HSC-5CN cells. HSC-5NW cells had increased phospho-ERK2 (extracellular signal-regulated kinase

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Garber, John J., Fuminao Takeshima, Inés M. Antón, et al. "Enteropathogenic Escherichia coli and Vaccinia Virus Do Not Require the Family of WASP-Interacting Proteins for Pathogen-Induced Actin Assembly." Infection and Immunity 80, no. 12 (2012): 4071–77. http://dx.doi.org/10.1128/iai.06148-11.

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ABSTRACTThe human pathogens enteropathogenicEscherichia coli(EPEC) and vaccinia virus trigger actin assembly in host cells by activating the host adaptor Nck and the actin nucleation promoter neural Wiskott-Aldrich syndrome protein (N-WASP). EPEC translocates effector molecules into host cells via type III secretion, and the interaction between the translocated intimin receptor (Tir) and the bacterial membrane protein intimin stimulates Nck and N-WASP recruitment, leading to the formation of actin pedestals beneath adherent bacteria. Vaccinia virus also recruits Nck and N-WASP to generate acti

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Novak, Nurit, Vered Bar, Helena Sabanay, et al. "N-WASP is required for membrane wrapping and myelination by Schwann cells." Journal of Cell Biology 192, no. 2 (2011): 243–50. http://dx.doi.org/10.1083/jcb.201010013.

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During peripheral nerve myelination, Schwann cells sort larger axons, ensheath them, and eventually wrap their membrane to form the myelin sheath. These processes involve extensive changes in cell shape, but the exact mechanisms involved are still unknown. Neural Wiskott–Aldrich syndrome protein (N-WASP) integrates various extracellular signals to control actin dynamics and cytoskeletal reorganization through activation of the Arp2/3 complex. By generating mice lacking N-WASP in myelinating Schwann cells, we show that N-WASP is crucial for myelination. In N-WASP–deficient nerves, Schwann cells

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Torniainen, Jyrki, and Atte Komonen. "Different trophic positions among social vespid species revealed by stable isotopes." Royal Society Open Science 8, no. 5 (2021): 210472. http://dx.doi.org/10.1098/rsos.210472.

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The social vespid wasps are common insect predators and several species behave in unison in the same biotopes. It is commonly accepted that social wasps are mainly opportunistic generalist predators without differences in prey selection and hence they compete for the same food resources. Trophic positions of six vespid wasp species and their potential prey from four sites in Finland and one in the UK were evaluated using carbon and nitrogen stable isotopes (δ 13 C and δ 15 N). The difference in isotope values indicated different trophic positions among species. In general, Dolichovespula spp.

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Souza, Marcos Magalhães de, Ângela Gomes Brunismann, and Mateus Aparecido Clemente. "Social wasp richness and species distributions among ecosystem types in Minas Gerais, Brazil." Sociobiology 64, no. 4 (2017): 456. http://dx.doi.org/10.13102/sociobiology.v64i4.1839.

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The state of Minas Gerais has high biodiversity, characterized by strong ecosystem heterogeneity that favors high richness of social wasps. There are currently 109 species known to occur in the state, however, there is lack of information concerning the distribution of these social insects among different ecosystems. The objective of this study was to evaluate social wasp species richness and distributions by ecosystem, thereby generating data for use in discerning relevant and priority environments for vespid conservation in Minas Gerais. We evaluated articles, theses, and dissertations publi

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Detoni, Mateus Fajardo de Freitas Salviato, Bruno Correa Barbosa, Tatiane Tagliatti Maciel, Samuel Júlio Lima Dos Santos, and Fabio Prezoto. "Long- and short-term changes in social wasp community structure in an urban area." Sociobiology 65, no. 2 (2018): 305. http://dx.doi.org/10.13102/sociobiology.v65i2.2597.

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The success of social wasps in anthropic environments is related to their ability to nest both in vegetation and human constructions, and, as humans modify their own environments, wasps community structure may shift as well. Our aim was to assess the diversity of social wasps and their interactions with nesting substrates seasonally in an urban squares area in Southeastern Brazil, 15 years after the first diversity study in this area. We actively searched for nests in the rainy season between 2014 and 2015 and in the dry season of 2015. Although social wasp species richness did not change sinc

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Ghimire, M., B. Pahari, N. Paudel, G. Das, SK Sharma, and G. Das. "Hymenoptera stings: a study of clinical profile, complication and outcome from a teaching hospital of central Nepal." Journal of College of Medical Sciences-Nepal 9, no. 3 (2014): 17–24. http://dx.doi.org/10.3126/jcmsn.v9i3.10210.

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Background Hymenoptera sting is a common health hazard in the tropics. Wasp and Bee stings can produce symptoms ranging from local allergic reactions to serious complications including anaphylaxis and multiple organ dysfunction syndromes.Objective To evaluate the clinical profile, management and early outcome of patients with gallbladder cancer.Methods We prospectively analyzed all the consecutive patients with Hymenopterid sting (Wasp and Bee stings), who were admitted in Nephrology Unit in college of Medical Sciences Teaching hospital over a period of two year; from June 2010 to May 2012. Da

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Cosme, Daiana Carla, Cynthia Maria de Lyra Neves, César Auguste Badji, Patrícia Vieira Ribeiro, Adriane Vieira Souza, and José Gomes Silva Filho. "Solitary wasp diversity (Hymenoptera: Aculeata) in different cultivation environments." Diversitas Journal 4, no. 3 (2019): 1156–70. http://dx.doi.org/10.17648/diversitas-journal-v4i3.839.

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ABSTRACT: Wasps contribute to environmental quality and ecosystem services, and play a key role in the functioning of many environments. The present study identified the diversity of species of solitary wasps that occupied trap-nests in farming environments. as well as the architecture of the nests found. The study focused on three areas of agroecosystem, where 30 blocks of trap-nests, with four diameters (5 mm, 7 mm, 9 mm, and 11 mm), were installed. A total of 56 nests were occupied by solitary wasps, with the most frequent species being Trypoxylon sp.1 (N=100, 54.9%), Pachodynerus cf. brevi

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Westerberg, Lisa S., Carin Dahlberg, Marisa Baptista, et al. "Wiskott-Aldrich syndrome protein (WASP) and N-WASP are critical for peripheral B-cell development and function." Blood 119, no. 17 (2012): 3966–74. http://dx.doi.org/10.1182/blood-2010-09-308197.

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Abstract The Wiskott-Aldrich syndrome protein (WASP) is a key cytoskeletal regulator of hematopoietic cells. Although WASP-knockout (WKO) mice have aberrant B-cell cytoskeletal responses, B-cell development is relatively normal. We hypothesized that N-WASP, a ubiquitously expressed homolog of WASP, may serve some redundant functions with WASP in B cells. In the present study, we generated mice lacking WASP and N-WASP in B cells (conditional double knockout [cDKO] B cells) and show that cDKO mice had decreased numbers of follicular and marginal zone B cells in the spleen. Receptor-induced activ

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Shintaku, Tatsushi, Kyle A. Glass, Matthew P. Hirakawa, et al. "Human Endothelial Cells Internalize Candida parapsilosis via N-WASP-Mediated Endocytosis." Infection and Immunity 81, no. 8 (2013): 2777–87. http://dx.doi.org/10.1128/iai.00535-13.

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ABSTRACTCandida parapsilosisis a frequent cause of disseminated candidiasis and is associated with significant morbidity and mortality. Although important in pathogenesis, interactions of this organism with endothelial cells have received less attention than those ofCandida albicans. Internalization ofC. parapsilosisby monolayers of human endothelial cells was examined in anin vitroassay and compared to that ofC. albicans. Both live and heat-killed yeast were efficiently internalized, with heat-killed yeast subsequently being detected in an acidic subcompartment. Internalization was marked by

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Falet, Hervé, Karin M. Hoffmeister, Ralph Neujahr, and John H. Hartwig. "Normal Arp2/3 complex activation in platelets lacking WASp." Blood 100, no. 6 (2002): 2113–22. http://dx.doi.org/10.1182/blood.v100.6.2113.

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Abstract Arp2/3 complex is believed to induce de novo nucleation of actin filaments at the edge of motile cells downstream of WASp family proteins. In this study, the signaling pathways leading to Arp2/3 complex activation, actin assembly, and shape change were investigated in platelets isolated from patients with Wiskott-Aldrich Syndrome (WAS), that is, who lack WASp, and in WASp-deficient mouse platelets. WASp-deficient human and mouse platelets elaborate filopodia, spread lamellae, and assemble actin, identical to control WASp-expressing platelets. Human platelets contain 2 μM Arp2/3 comple

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Falet, Hervé, Karin M. Hoffmeister, Ralph Neujahr, and John H. Hartwig. "Normal Arp2/3 complex activation in platelets lacking WASp." Blood 100, no. 6 (2002): 2113–22. http://dx.doi.org/10.1182/blood.v100.6.2113.h81802002113_2113_2122.

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Arp2/3 complex is believed to induce de novo nucleation of actin filaments at the edge of motile cells downstream of WASp family proteins. In this study, the signaling pathways leading to Arp2/3 complex activation, actin assembly, and shape change were investigated in platelets isolated from patients with Wiskott-Aldrich Syndrome (WAS), that is, who lack WASp, and in WASp-deficient mouse platelets. WASp-deficient human and mouse platelets elaborate filopodia, spread lamellae, and assemble actin, identical to control WASp-expressing platelets. Human platelets contain 2 μM Arp2/3 complex, or 860

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Suzuki, Toshihiko, Hitomi Mimuro, Hiroaki Miki, et al. "Rho Family Gtpase Cdc42 Is Essential for the Actin-Based Motility of Shigella in Mammalian Cells." Journal of Experimental Medicine 191, no. 11 (1999): 1905–20. http://dx.doi.org/10.1084/jem.191.11.1905.

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Shigella, the causative agent of bacillary dysentery, is capable of directing its movement within host cells by exploiting actin dynamics. The VirG protein expressed at one pole of the bacterium can recruit neural Wiskott-Aldrich syndrome protein (N-WASP), a downstream effector of Cdc42. Here, we show that Cdc42 is required for the actin-based motility of Shigella. Microinjection of a dominant active mutant Cdc42, but not Rac1 or RhoA, into Swiss 3T3 cells accelerated Shigella motility. In add-back experiments in Xenopus egg extracts, addition of a guanine nucleotide dissociation inhibitor for

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Farache, Fernando Henrique Antoniolli, Cecilia Bernardo Pereira, Cristiana Koschnitzke, et al. "The unknown followers: Discovery of a new species of Sycobia Walker (Hymenoptera: Epichrysomallinae) associated with Ficus benjamina L. (Moraceae) in the Neotropical region." Journal of Hymenoptera Research 67 (December 31, 2018): 85–102. http://dx.doi.org/10.3897/jhr.67.29733.

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Biotic invasion in mutualistic communities is of particular interest due to the possible establishment of new relationships with native species. Ficus species are widely cultivated as ornamental plants, and they host specific communities of chalcid wasps that are strictly associated with the fig inflorescences. Some introduced fig species are capable of establishing new relationships with the local fig wasps, and fig wasp species may also be concomitantly introduced with their host plants. Ficusbenjamina L. is widely cultivated across the world, but the associated fig wasps are not reported ou

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GUPTA, ANKITA, CORNELIS VAN ACHTERBERG, CHANDISH R. BALLAL, et al. "Two new species of Rhogadopsis Brèthes (Braconidae: Opiinae) as solitary parasitoids of Merochlorops species complex (Diptera: Chloropidae) from India." Zootaxa 4550, no. 2 (2019): 268. http://dx.doi.org/10.11646/zootaxa.4550.2.7.

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During surveys for the potential biocontrol agents Merochlorops species complex (Diptera: Chloropidae), to control the invasive weed Hedychium gardnerianum Sheppard ex Ker Gawl. (Zingiberaceae), two new species of Rhogadopsis Brèthes (Braconidae: Opiinae) viz., R. gratia Gupta & van Achterberg, sp. n. and R. macrusa Gupta & van Achterberg, sp. n. were reared as solitary larval-pupal parasitoids of Merochlorops in the stems of H. gardnerianum. Interestingly, both wasp species have very different ovipositor lengths, in addition to other characters for species delimitation. Perhaps parasi

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Egile, Coumaran, Thomas P. Loisel, Valérie Laurent, et al. "Activation of the Cdc42 Effector N-Wasp by the Shigella flexneri Icsa Protein Promotes Actin Nucleation by Arp2/3 Complex and Bacterial Actin-Based Motility." Journal of Cell Biology 146, no. 6 (1999): 1319–32. http://dx.doi.org/10.1083/jcb.146.6.1319.

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To propel itself in infected cells, the pathogen Shigella flexneri subverts the Cdc42-controlled machinery responsible for actin assembly during filopodia formation. Using a combination of bacterial motility assays in platelet extracts with Escherichia coli expressing the Shigella IcsA protein and in vitro analysis of reconstituted systems from purified proteins, we show here that the bacterial protein IcsA binds N-WASP and activates it in a Cdc42-like fashion. Dramatic stimulation of actin assembly is linked to the formation of a ternary IcsA–N-WASP–Arp2/3 complex, which nucleates actin polym

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Sarmiento, Corina, Weigang Wang, Athanassios Dovas, et al. "WASP family members and formin proteins coordinate regulation of cell protrusions in carcinoma cells." Journal of Cell Biology 180, no. 6 (2008): 1245–60. http://dx.doi.org/10.1083/jcb.200708123.

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We examined the role of the actin nucleation promoters neural Wiskott-Aldrich syndrome protein (N-WASP) and WAVE2 in cell protrusion in response to epidermal growth factor (EGF), a key regulator in carcinoma cell invasion. We found that WAVE2 knockdown (KD) suppresses lamellipod formation and increases filopod formation, whereas N-WASP KD has no effect. However, simultaneous KD of both proteins results in the formation of large jagged protrusions with lamellar properties and increased filopod formation. This suggests that another actin nucleation activity is at work in carcinoma cells in respo

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Dragoi, Ana-Maria, Arthur M. Talman, and Hervé Agaisse. "Bruton's Tyrosine Kinase Regulates Shigella flexneri Dissemination in HT-29 Intestinal Cells." Infection and Immunity 81, no. 2 (2012): 598–607. http://dx.doi.org/10.1128/iai.00853-12.

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ABSTRACTShigella flexneriis a Gram-negative intracellular pathogen that infects the intestinal epithelium and utilizes actin-based motility to spread from cell to cell.S. flexneriactin-based motility has been characterized in various cell lines, but studies in intestinal cells are limited. Here we characterizedS. flexneriactin-based motility in HT-29 intestinal cells. In agreement with studies conducted in various cell lines, we showed thatS. flexnerirelies on neural Wiskott-Aldrich Syndrome protein (N-WASP) in HT-29 cells. We tested the potential role of various tyrosine kinases involved in N

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Luna, Ana, Olga B. Matas, José Angel Martı́nez-Menárguez, et al. "Regulation of Protein Transport from the Golgi Complex to the Endoplasmic Reticulum by CDC42 and N-WASP." Molecular Biology of the Cell 13, no. 3 (2002): 866–79. http://dx.doi.org/10.1091/mbc.01-12-0579.

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Actin is involved in the organization of the Golgi complex and Golgi-to-ER protein transport in mammalian cells. Little, however, is known about the regulation of the Golgi-associated actin cytoskeleton. We provide evidence that Cdc42, a small GTPase that regulates actin dynamics, controls Golgi-to-ER protein transport. We located GFP-Cdc42 in the lateral portions of Golgi cisternae and in COPI-coated and noncoated Golgi-associated transport intermediates. Overexpression of Cdc42 and its activated form Cdc42V12 inhibited the retrograde transport of Shiga toxin from the Golgi complex to the ER,

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Takano, Kazunori, Haruko Watanabe-Takano, Shiro Suetsugu, et al. "Nebulin and N-WASP Cooperate to Cause IGF-1–Induced Sarcomeric Actin Filament Formation." Science 330, no. 6010 (2010): 1536–40. http://dx.doi.org/10.1126/science.1197767.

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Insulin-like growth factor 1 (IGF-1) induces skeletal muscle maturation and enlargement (hypertrophy). These responses require protein synthesis and myofibril formation (myofibrillogenesis). However, the signaling mechanisms of myofibrillogenesis remain obscure. We found that IGF-1–induced phosphatidylinositol 3-kinase–Akt signaling formed a complex of nebulin and N-WASP at the Z bands of myofibrils by interfering with glycogen synthase kinase-3β in mice. Although N-WASP is known to be an activator of the Arp2/3 complex to form branched actin filaments, the nebulin–N-WASP complex caused actin

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Guerra, Susana, Miguel Aracil, Raquel Conde, Antonio Bernad, and Mariano Esteban. "Wiskott-Aldrich Syndrome Protein Is Needed for Vaccinia Virus Pathogenesis." Journal of Virology 79, no. 4 (2005): 2133–40. http://dx.doi.org/10.1128/jvi.79.4.2133-2140.2005.

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ABSTRACT Smallpox, caused by variola virus, was a devastating disease in humans, but how the virus evolved a strategy to spread to tissue remains unknown. Through the use of microarrays, we identified the gene encoding the Wiskott-Aldrich syndrome protein (WASP), one of the five known WASP family members, which has been induced in the course of infection of human cells with different strains of vaccinia virus (VV) (S. Guerra, L. A. López-Fernández, A. Pascual-Montano, M. Muñoz, K. Harshman, and M. Esteban, J. Virol. 77:6493-6506, 2003; S. Guerra, L. A. López-Fernández, R. Conde, A. Pascua

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Sturge, Justin, Jocelyne Hamelin та Gareth E. Jones. "N-WASP activation by a β1-integrin-dependent mechanism supports PI3K-independent chemotaxis stimulated by urokinase-type plasminogen activator". Journal of Cell Science 115, № 4 (2002): 699–711. http://dx.doi.org/10.1242/jcs.115.4.699.

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Urokinase-type plasminogen activator (uPA)-uPA receptor (uPAR) and epidermal growth factor (EGF)-EGF receptor (EGFR) expression is highly correlated with breast cancer metastasis. Phosphoinositide 3-kinase (PI3K),small Rho GTPases, such as Cdc42 and Rac1, and neuronal Wiskott Aldrich syndrome protein (N-WASP) are key effectors that regulate dynamic changes in the actin cytoskeleton and cell migration. uPA- and EGF-stimulated chemotaxis,cytoskeletal rearrangements and activation of Cdc42, Rac1 and N-WASP were studied in the highly metastatic human breast cancer cell line MDA MB 231. These studi

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Burton, Elizabeth A., Timothy N. Oliver, and Ann Marie Pendergast. "Abl Kinases Regulate Actin Comet Tail Elongation via an N-WASP-Dependent Pathway." Molecular and Cellular Biology 25, no. 20 (2005): 8834–43. http://dx.doi.org/10.1128/mcb.25.20.8834-8843.2005.

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ABSTRACT Microbial pathogens have evolved diverse strategies to modulate the host cell cytoskeleton to achieve a productive infection and have proven instrumental for unraveling the molecular machinery that regulates actin polymerization. Here we uncover a mechanism for Shigella flexneri-induced actin comet tail elongation that links Abl family kinases to N-WASP-dependent actin polymerization. We show that the Abl kinases are required for Shigella actin comet tail formation, maximal intracellular motility, and cell-to-cell spread. Abl phosphorylates N-WASP, a host cell protein required for act

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Cai, Guo-Qiang, Chu-Fang Chou, Meng Hu та ін. "Neuronal Wiskott-Aldrich syndrome protein (N-WASP) is critical for formation of α-smooth muscle actin filaments during myofibroblast differentiation". American Journal of Physiology-Lung Cellular and Molecular Physiology 303, № 8 (2012): L692—L702. http://dx.doi.org/10.1152/ajplung.00390.2011.

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Myofibroblasts are implicated in pathological stromal responses associated with lung fibrosis. One prominent phenotypic marker of fully differentiated myofibroblasts is the polymerized, thick cytoplasmic filaments containing newly synthesized α-smooth muscle actin (α-SMA). These α-SMA-containing cytoplasmic filaments are important for myofibroblast contractility during tissue remodeling. However, the molecular mechanisms regulating the formation and maturation of α-SMA-containing filaments have not been defined. This study demonstrates a critical role for neuronal Wiskott-Aldrich syndrome prot

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Shu, Zhou, Michelle Lazzaro, Chaohong Liu, et al. "The Actin Cytoskeleton Controls FcgRIIB-Mediated Inhibition of B-Cell Signaling." Journal of Immunology 198, no. 1_Supplement (2017): 52.1. http://dx.doi.org/10.4049/jimmunol.198.supp.52.1.

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Abstract FcgRIIB is a major inhibitory coreceptor of B cell receptor (BCR), and its deficiency leads to B cell autoimmunity. Upon colligated with the BCR by immune complexes (ICs), this coreceptor activates SH2-containing inositol-5 phosphatase (SHIP) and inhibits BCR clustering in lipid rafts. However, the molecular mechanisms underlying FcgRIIB-mediated inhibition of BCR activation remain elusive. This study reveals a critical role of the actin cytoskeleton in FcgRIIB-mediated inhibition. Upon interacting with ICs tethered to lipid bilayers, an actomyosin ring is quickly formed surrounding t

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SOBCZAK, JOBER FERNANDO, DIEGO GALVÃO DE PÁDUA, GERMAN ANTONIO VILLANUEVA- BONILLA, FRANCISCO AGEU DE SOUSA NÓBREGA, and YURI FANCHINI MESSAS. "Two new species of Zatypota (Hymenoptera: Ichneumonidae, Pimplinae) sharing the same host spider in Northeast Brazil." Zootaxa 4609, no. 1 (2019): 169. http://dx.doi.org/10.11646/zootaxa.4609.1.9.

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Some polysphinctine wasps of the genus Zatypota complete their life cycles upon theridiid host spiders. The host range of these wasps is usually species-specific, although in some less common associations more than one wasp species interacts with the same host spider. Here we describe and illustrate the polysphinctine wasps Zatypota baezae sp. n. and Zatypota mulunguensis sp. n. (Hymenoptera: Ichneumonidae), both koinobiont ectoparasitoids of the spider Anelosimus baeza (Theridiidae). The two parasitoid wasps show the same development time (12 days) which was longer when compared with other pa

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