Relevant bibliographies by topics / Microfilament proteins

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  2. Dissertations / Theses
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  5. Conference papers

Academic literature on the topic 'Microfilament proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Microfilament proteins"

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Huang, Xiaolan, Rongmei Qu, Yan Peng, Yuchao Yang, Tingyu Fan, Bing Sun, Asmat Ullah Khan, et al. "Mechanical Sensing Element PDLIM5 Promotes Osteogenesis of Human Fibroblasts by Affecting the Activity of Microfilaments." Biomolecules 11, no. 5 (May 19, 2021): 759. http://dx.doi.org/10.3390/biom11050759.

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Human skin fibroblasts (HSFs) approximate the multidirectional differentiation potential of mesenchymal stem cells, so they are often used in differentiation, cell cultures, and injury repair. They are an important seed source in the field of bone tissue engineering. However, there are a few studies describing the mechanism of osteogenic differentiation of HSFs. Here, osteogenic induction medium was used to induce fibroblasts to differentiate into osteoblasts, and the role of the mechanical sensitive element PDLIM5 in microfilament-mediated osteogenic differentiation of human fibroblasts was evaluated. The depolymerization of microfilaments inhibited the expression of osteogenesis-related proteins and alkaline phosphatase activity of HSFs, while the polymerization of microfilaments enhanced the osteogenic differentiation of HSFs. The evaluation of potential protein molecules affecting changes in microfilaments showed that during the osteogenic differentiation of HSFs, the expression of PDLIM5 increased with increasing induction time, and decreased under the state of microfilament depolymerization. Lentivirus-mediated PDLIM5 knockdown by shRNA weakened the osteogenic differentiation ability of HSFs and inhibited the expression and morphological changes of microfilament protein. The inhibitory effect of knocking down PDLIM5 on HSF osteogenic differentiation was reversed by a microfilament stabilizer. Taken together, these data suggest that PDLIM5 can mediate the osteogenic differentiation of fibroblasts by affecting the formation and polymerization of microfilaments.
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Ashworth, Sharon L., Sarah E. Wean, Silvia B. Campos, Constance J. Temm-Grove, Erica L. Southgate, Bernadette Vrhovski, Peter Gunning, Ron P. Weinberger, and Bruce A. Molitoris. "Renal ischemia induces tropomyosin dissociation-destabilizing microvilli microfilaments." American Journal of Physiology-Renal Physiology 286, no. 5 (May 2004): F988—F996. http://dx.doi.org/10.1152/ajprenal.00168.2003.

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Ischemic-induced cell injury results in rapid duration-dependent actin-depolymerizing factor (ADF)/cofilin-mediated disruption of the apical microvilli microfilament cores. Because intestinal microvillar microfilaments are bound and stabilized in the terminal web by the actin-binding protein tropomyosin, we questioned whether a protective effect of tropomyosin localization to the terminal web of the proximal tubule microfilament cores is disrupted during ischemic injury. With tropomyosin-specific antibodies, we examined rat cortical sections under physiological conditions and following ischemic injury by confocal microscopy. In addition, Western blot analysis of cortical extracts and urine was undertaken. Our studies demonstrated the presence of tropomyosin isoforms in the proximal tubule microvillar terminal web under physiological conditions and their dissociation in response to 25 min of ischemic injury. This correlated with the excretion of tropomyosin-containing plasma membrane vesicles in urine from ischemic rats. In addition, we noted increased tropomyosin Triton X-100 solubility following ischemia in cortical extracts. These studies suggest tropomyosin binds to and stabilizes the microvillar microfilament core in the terminal web under physiological conditions. With the onset of ischemic injury, we propose that tropomyosin dissociates from the microfilament core providing access to microfilaments in the terminal web for F-actin binding, severing and depolymerizing actions of ADF/cofilin proteins.
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Collings, David A., and Geoffrey O. Wasteneys. "Actin microfilament and microtubule distribution patterns in the expanding root of Arabidopsis thaliana." Canadian Journal of Botany 83, no. 6 (June 1, 2005): 579–90. http://dx.doi.org/10.1139/b05-032.

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Determination of the precise role(s) of actin microfilaments in the control of cell shape and elongation in the root tips of the model genetic system Arabidopsis thaliana (L.) Heynh is frustrated by inadequate microscopy imaging techniques. In this paper, we documented both microfilaments and microtubules in the root tips of Arabidopsis by double immunofluorescence labelling and computer-generated reconstruction of confocal image series. Our procedure, which complements the use of recently developed fluorescent reporter proteins, revealed hitherto undescribed aspects of the Arabidopsis microfilament cytoskeleton that may provide important clues about mechanisms behind cell elongation. We found that preservation of extensive arrays of transverse cortical microfilaments depends on unperturbed microtubule organization. Compared with ordinary epidermal cells, cells situated in the trichoblast or hair-forming cell files were comparatively devoid of endoplasmic microfilaments when in the distal elongation zone, well before hair formation begins. Computer-aided reconstructions also revealed that the nonexpanding end walls of cells in the distal elongation zone have radially oriented microtubules and randomly arranged microfilaments. In dividing cells, microfilaments became more prominent in the cell cortex, and subtle differences between microtubule and microfilament organization were seen within the phragmoplast. These observations will form the basis of understanding the roles of the cytoskeleton in controlling elongation in root tissues. In light of the many Arabidopsis mutants with altered root morphology, our methods offer a reliable approach to assess the function of cytoskeletal proteins and signalling systems in root morphogenesis.Key words: actin microfilaments, Arabidopsis thaliana, distal elongation zone, microtubules, phragmoplast, roots.
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Lakkakorpi, P. T., and H. K. Väänänen. "Calcitonin, prostaglandin E2, and dibutyryl cyclic adenosine 3',5'-monophosphate disperse the specific microfilament structure in resorbing osteoclasts." Journal of Histochemistry & Cytochemistry 38, no. 10 (October 1990): 1487–93. http://dx.doi.org/10.1177/38.10.2169493.

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Bone resorbing osteoclasts form a specific microfilament structure at the attachment area, in which vinculin and talin appear as a double-circle structure and F-actin fills the space between these circles. This distribution of microfilaments is associated with the resorption lacunae, and F-actin, vinculin, and talin zones correspond roughly to the edges of the lacunae. In the present work, we examined by immunofluorescence the effects of calcitonin (CT) and prostaglandin E2 (PGE2), inhibitors of osteoclastic activity, as well as dibutyryl cyclic AMP (Bt2cAMP) and cytochalasin B, on the microfilament organization in resorbing osteoclasts. CT, PGE2, and Bt2cAMP rapidly dispersed the specific microfilament structure in resorbing osteoclasts. All microfilament proteins studied (vinculin, talin, and F-actin) spread to the central areas of the original circles. The effect of CT was dose dependent. The effects of CT and PGE2 could be reversed, but recovery was slower after CT treatment than after PGE2 treatment. Cytochalasin B entirely destroyed the F-actin organization but only partially the vinculin organization. The results suggest that one structural change leading to the inactivation of the osteoclasts caused by CT and PGE2 is the disintegration of the microfilament structure at the attachment area of resorbing osteoclasts.
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Samuelsson, Steven J., Paul W. Luther, David W. Pumplin, and Robert J. Bloch. "Macromolecular specializations that mediate lateral interactions between microfilaments and the membrane at focal contacts." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (August 1992): 724–25. http://dx.doi.org/10.1017/s0424820100124021.

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Focal contacts are membrane specializations of cultured cells where stress fibers terminate and where the cell is most closely applied to the substrate. The organization of this cytoskeletal-membrane-extracellular matrix assembly has been well characterized. Immunofluorescence microscopy has shown that two focal contact-specific proteins, vinculin and talin, colocalize with microfilaments for several microns before the stress fiber terminates. This result raises the question of whether microfilament-membrane interactions are limited to the ends of microfilaments, or if lateral interactions also occur. We addressed this question by examining the cytoplasmic surface of isolated focal contacts in detail.
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Schevzov, Galina, Bernadette Vrhovski, Nicole S. Bryce, Sarah Elmir, Min Ru Qiu, Geraldine M. O'Neill, Nan Yang, Nicole M. Verrills, Maria Kavallaris, and Peter W. Gunning. "Tissue-specific Tropomyosin Isoform Composition." Journal of Histochemistry & Cytochemistry 53, no. 5 (May 2005): 557–70. http://dx.doi.org/10.1369/jhc.4a6505.2005.

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Four distinct genes encode tropomyosin (Tm) proteins, integral components of the actin microfilament system. In non-muscle cells, over 40 Tm isoforms are derived using alternative splicing. Distinct populations of actin filaments characterized by the composition of these Tm isoforms are found differentially sorted within cells ( Gunning et al. 1998b ). We hypothesized that these distinct intracellular compartments defined by the association of Tm isoforms may allow for independent regulation of microfilament function. Consequently, to understand the molecular mechanisms that give rise to these different microfilaments and their regulation, a cohort of fully characterized isoform-specific Tm antibodies was required. The characterization protocol initially involved testing the specificity of the antibodies on bacterially produced Tm proteins. We then confirmed that these Tm antibodies can be used to probe the expression and subcellular localization of different Tm isoforms by Western blot analysis, immunofluorescence staining of cells in culture, and immunohistochemistry of paraffin wax-embedded mouse tissues. These Tm antibodies, therefore, have the capacity to monitor specific actin filament populations in a range of experimental systems.
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Mykkänen, Olli-Matti, Mikaela Grönholm, Mikko Rönty, Maciej Lalowski, Paula Salmikangas, Heli Suila, and Olli Carpén. "Characterization of Human Palladin, a Microfilament-associated Protein." Molecular Biology of the Cell 12, no. 10 (October 2001): 3060–73. http://dx.doi.org/10.1091/mbc.12.10.3060.

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Actin-containing microfilaments control cell shape, adhesion, and contraction. In striated muscle, α-actinin and other Z-disk proteins coordinate the organization and functions of actin filaments. In smooth muscle and nonmuscle cells, periodic structures termed dense bodies and dense regions, respectively, are thought to serve functions analogous to Z-discs. We describe here identification and characterization of human palladin, a protein expressed mainly in smooth muscle and nonmuscle and distributed along microfilaments in a periodic manner consistent with dense regions/bodies. Palladin contains three Ig-domains most homologous to the sarcomeric Z-disk protein myotilin. The N terminus includes an FPPPP motif recognized by the Ena-Vasp homology domain 1 domain in Ena/vasodilatator-stimulated phosphoprotein (VASP)/Wiscott-Aldrich syndrome protein (WASP) protein family. Cytoskeletal proteins with FPPPP motif target Ena/VASP/WASP proteins to sites of actin modulation. We identified palladin in a yeast two-hybrid search as an ezrin-associated protein. An interaction between palladin and ezrin was further verified by affinity precipitation and blot overlay assays. The interaction was mediated by the α-helical domain of ezrin and by Ig-domains 2–3 of palladin. Ezrin is typically a component of the cortical cytoskeleton, but in smooth muscle cells it is localized along microfilaments. These cells express palladin abundantly and thus palladin may be involved in the microfilament localization of ezrin. Palladin expression was up-regulated in differentiating dendritic cells (DCs), coinciding with major cytoskeletal and morphological alterations. In immature DCs, palladin localized in actin-containing podosomes and in mature DCs along actin filaments. The regulated expression and localization suggest a role for palladin in the assembly of DC cytoskeleton.
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Ji, Jun-Yuan, Marjan Haghnia, Cory Trusty, Lawrence S. B. Goldstein, and Gerold Schubiger. "A Genetic Screen for Suppressors and Enhancers of the Drosophila Cdk1-Cyclin B Identifies Maternal Factors That Regulate Microtubule and Microfilament Stability." Genetics 162, no. 3 (November 1, 2002): 1179–95. http://dx.doi.org/10.1093/genetics/162.3.1179.

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Abstract Coordination between cell-cycle progression and cytoskeletal dynamics is important for faithful transmission of genetic information. In early Drosophila embryos, increasing maternal cyclin B leads to higher Cdk1-CycB activity, shorter microtubules, and slower nuclear movement during cycles 5-7 and delays in nuclear migration to the cortex at cycle 10. Later during cycle 14 interphase of six cycB embryos, we observed patches of mitotic nuclei, chromosome bridges, abnormal nuclear distribution, and small and large nuclei. These phenotypes indicate disrupted coordination between the cell-cycle machinery and cytoskeletal function. Using these sensitized phenotypes, we performed a dosage-sensitive genetic screen to identify maternal proteins involved in this process. We identified 10 suppressors classified into three groups: (1) gene products regulating Cdk1 activities, cdk1 and cyclin A; (2) gene products interacting with both microtubules and microfilaments, Actin-related protein 87C; and (3) gene products interacting with microfilaments, chickadee, diaphanous, Cdc42, quail, spaghetti-squash, zipper, and scrambled. Interestingly, most of the suppressors that rescue the astral microtubule phenotype also reduce Cdk1-CycB activities and are microfilament-related genes. This suggests that the major mechanism of suppression relies on the interactions among Cdk1-CycB, microtubule, and microfilament networks. Our results indicate that the balance among these different components is vital for normal early cell cycles and for embryonic development. Our observations also indicate that microtubules and cortical microfilaments antagonize each other during the preblastoderm stage.
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Temm-Grove, C. J., B. M. Jockusch, M. Rohde, K. Niebuhr, T. Chakraborty, and J. Wehland. "Exploitation of microfilament proteins by Listeria monocytogenes: microvillus-like composition of the comet tails and vectorial spreading in polarized epithelial sheets." Journal of Cell Science 107, no. 10 (October 1, 1994): 2951–60. http://dx.doi.org/10.1242/jcs.107.10.2951.

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Effective cell-to-cell spreading of the facultative intracellular pathogen Listeria monocytogenes requires the interaction between bacteria and the microfilament system of the host cell. By recruiting actin filaments into a ‘comet tail’ localized at one pole of the bacterial cell wall, Listeria become mobile and propel themselves through the cytoplasm. They create protrusions at the plasma membrane that can invaginate adjacent cells. In this work, we have analysed the structural composition of Listeria-recruited microfilaments in various epithelial cell lines by immunofluorescence microscopy. The microfilament-crosslinking proteins alpha-actinin, fimbrin and villin were localized around bacteria as soon as actin filaments could be detected on the bacterial surface. Surprisingly, the same was found for ezrin/radixin, proteins involved in linking microfilaments to the plasma membrane. We found that in a polarized cell line derived from brush border kidney epithelium (LLC-PK1), the actin filaments surrounding intracytoplasmic motile bacteria show the same immunoreactivity as the brush border-like microvilli, when analysed by a specific actin antibody. The successful invasion of polarized LLC-PK1 islets is vectorial, i.e. it progresses predominantly from the periphery of the islets towards the centre. Infection of the peripheral cells is sufficient for infiltration of the entire cellular islets, without any further contact with the extracellular milieu. This is in contrast to nonpolarized epithelial sheets, which can be invaded from the apical surface of any individual cell. The importance of active bacterial motility in this vectorial spreading is emphasized by our finding that an isogenic Listeria mutant that is unable to recruit actin filaments cannot colonize polarized epithelial layers but accumulates in the peripheral cells of the islets.
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Hüttelmaier, Stefan, Susanne Illenberger, Irina Grosheva, Manfred Rüdiger, Robert H. Singer, and Brigitte M. Jockusch. "Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins." Journal of Cell Biology 155, no. 5 (November 26, 2001): 775–86. http://dx.doi.org/10.1083/jcb.200105044.

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By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complexes with the microfilament-associated proteins vinculin, metavinculin, and α-actinin and colocalizes with vinculin/metavinculin and α-actinin at microfilament attachment sites, such as cell–cell and cell matrix contacts of epithelial cells and fibroblasts, respectively, and in costameres of skeletal muscle. The NH2-terminal part of raver1 contains three RNA recognition motifs with homology to members of the heterogeneous nuclear RNP (hnRNP) family. Raver1 colocalizes with polypyrimidine tract binding protein (PTB)/hnRNPI, a protein involved in RNA splicing of microfilament proteins, in the perinucleolar compartment and forms complexes with PTB/hnRNPI. Hence, raver1 is a dual compartment protein, which is consistent with the presence of nuclear location signal and nuclear export sequence motifs in its sequence. During muscle differentiation, raver1 migrates from the nucleus to the costamere. We propose that raver1 may coordinate RNA processing and targeting as required for microfilament anchoring in specific adhesion sites.
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Dissertations / Theses on the topic "Microfilament proteins"

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Cherezova, Lidia Nikolayevna. "Determining the effects of phosphorylation on AFAP-110 function." Morgantown, W. Va. : [West Virginia University Libraries], 2002. http://etd.wvu.edu/templates/showETD.cfm?recnum=2492.

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Thesis (M.S.)--West Virginia University, 2002.
Title from document title page. Document formatted into pages; contains v, 105 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Baisden, Joseph M. "AFAP-110 is a cSrc activator." Morgantown, W. Va. : [West Virginia University Libraries], 2003. http://etd.wvu.edu/templates/showETD.cfm?recnum=2766.

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Thesis (Ph. D.)--West Virginia University, 2003.
Title from document title page. Document formatted into pages; contains v, 149 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Cawston, Erin, and n/a. "A role for filamin-C in the function of the type 2A serotonin receptor." University of Otago. Dunedin School of Medicine, 2008. http://adt.otago.ac.nz./public/adt-NZDU20080313.141311.

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The serotonin receptor 2A (5-HT₂[A]) is a member of the G-protein coupled receptor family and is of interest due to its role in physiological functions such as smooth muscle contraction, platelet aggregation, thermoregulation, learning and memory. More importantly, 5-HT₂[A] has also been implicated in CNS disorders including schizophrenia, depression and anxiety. A yeast two-hybrid screen had previously been carried out to identify proteins that interacted with 5-HT₂[A] and therefore may modulate intracellular function. The cytoskeletal actin-binding protein filamin-C was identified as a possible 5-HT₂[A] interacting partner. The aim of the research in this thesis was to further investigate the potential interaction between 5-HT₂[A] and filamin-C and to investigate functional roles for the interaction. A fragment of human filamin-C, aa 2162-2725, was shown to interact with the C-terminus of human 5-HT₂[A] using two in vitro techniques, the yeast-two hybrid system and a GST capture assay. The region of filamin-C needed to bind to 5-HT₂[A] was narrowed to the start of repeat 20, aa 2251, through to aa 2424 at the beginning of repeat 22 and comprises 182 residues. The 5-HT₂[A] region needed to bind to filamin-C was ascertained via yeast two-hybrid to be 31 amino acids between 394-423. Work was performed to determine whether FLNC mRNA was expressed in neural and glial cells and whether FLNC and HTR2A mRNA were co-expressed in any cells. FLNC mRNA was identified in seven out of eight neural and glial cell lines and western blot analysis confirmed this finding at the protein level. Two cell lines, U-118MG and A172, were found to contain both HTR2A and FLNC mRNA. Co-immunoprecipitation experiments showed endogenous filamin-C bound to endogenous 5-HT₂[A] and this complex could be precipitated using anti-filamin-C antibody. Additionally, a GST-5-HT₂[A] fusion complex was found to bind to endogenous filamin-C from U-118MG cells. Immunofluorescent labelling of cells was used to study filamin-C and 5-HT₂[A] proteins in vivo. U-118MG cells showed staining for 5-HT₂[A] around the membrane of the cell, as well as in the cytoplasm, whereas filamin-C staining occurred in the cytoplasm. Co-localisation analysis identified some areas of overlap between 5-HT₂[A] and filamin-C in the cytoplasm of U-118MG cells. The functional role for the 5-HT₂[A]/filamin-C colocalisation was investigated. It was postulated that filamin-C may be involved in the internalisation of 5-HT₂[A]. To test this hypothesis, an in vivo model system was used to investigate whether disruption of the filamin-C/5-HT₂[A] interaction affects internalisation of the receptor. The key preliminary findings of this study, which used expression of a competitor peptide, to disrupt and co-interact, suggested that the filamin-C/5-HT₂[A] interaction is not essential for the internalisation of receptors in response to ligand binding. However, this interaction was important for delivery or maintenance of 5-HT₂[A] to the cell membrane, and expression of the competing peptide caused an accumulation of cytoplasmic 5-HT₂[A].
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Qian, Yong. "Identification of the function of the carboxy terminus of AFAP-110 in regulating AFAP-110's self-association, cell localization and the integrity of actin filaments." Morgantown, W. Va. : [West Virginia University Libraries], 1999. http://etd.wvu.edu/templates/showETD.cfm?recnum=1102.

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Thesis (Ph. D.)--West Virginia University, 1999.
Title from document title page. Document formatted into pages; contains vi, 163 p. : ill. (some col.) Vita. Includes abstract. Includes bibliographical references.
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Cook, Leslie. "Filamin A Associates with the JAK2/PAK1 Complex and the JAK2/SH2B1β Complex." University of Toledo / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1229110703.

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Lee, Yongkuk. "Biomolecular shuttles under dielectrophoretic forces." Morgantown, W. Va. : [West Virginia University Libraries], 2008. http://hdl.handle.net/10450/5742.

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Thesis (M.S.)--West Virginia University, 2008.
Title from document title page. Document formatted into pages; contains ix, 115 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 103-105).
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Behmoaram, Emy. "Biological studies of fascin function in cancer cell invasion and cancer progression." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=111596.

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The process of metastasis is initiated through the acquisition of inherent and autonomous motile and invasive properties by tumor cells. These phenomena are initiated through a balance between forward cancer cell membrane protrusion and tail retraction, and occur via cell cytoskeleton remodeling, actin reorganization, and coordinated focal adhesion assembly and disassembly events. Among the vast network of cytoskeletal proteins, the actin-bundling protein fascin plays a major function in cell cytoskeleton remodeling. It is a 55-kDa protein involved in the formation of filopodia and cell migration, and found to be upregulated in many cancers. We report herein key functions for fascin in the regulation of prostate and breast cancer progression. Fascin expression is upregulated in localized and hormone refractory prostate cancer, responsible for a more aggressive clinical course. In addition, functional dissection of fascin reveals a novel function in the regulation of focal adhesion turnover dynamics, by modulating the phosphorylation state of central focal adhesion proteins through a potential collaboration with the protein tyrosine phosphatase, PEST. Together, our data support the importance of fascin in cancer cell invasion and as a significant prognostic marker and a potential therapeutic target for aggressive cancers.
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Skehan, Brian M. "Functional Elements of EspFu, an Enterohemorrhagic E. coli Effector that Stimulates Actin Assembly: A Dissertation." eScholarship@UMMS, 2009. https://escholarship.umassmed.edu/gsbs_diss/443.

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Enterohemorrhagic Escherichia coli O157:H7 (EHEC) is an attaching and effacing pathogen that upon attachment to host cells, induce characteristic attaching and effacing lesions and formation of F-actin rich pedestals beneath sites of bacterial attachment. EHEC harbors a Type III secretion system through which it delivers dozens of effectors into the host cell. The two secreted effectors critical for EHEC-mediated actin pedestal formation are the translocated intimin receptor (Tir) and EspFU. EspFU consists of an N-terminal secretion signal and a C-terminus containing six tandem 47-residue proline-rich repeats, each of which can bind and activate the actin nucleation promoting factor N-WASP. Structural and functional analyses described here have identified the mechanism of N-WASP activation by EspFU and the minimal domains and specific residues required for this activity. While EspFU and Tir are the only bacterial effectors required for F-actin pedestal formation, recruitment of EspFU to Tir is mediated by an unidentified putative host factor. To identify the host factor responsible for linking these two effectors, a combination of in vitro and functional assays were used to identify the host factor, IRTKS and the residues required for these interactions were defined. Further, the presence of at least two 47-residue repeats in all characterized clinical isolates of canonical EHEC strains led us to address the minimal requirements for EspFU functional domains to promote recruitment to Tir and N-WASP activation. Here we show that two proline-rich elements of EspFU are required for recruitment of EspFU by IRTKS to sites of bacterial attachment. Furthermore, once artificially clustered at the membrane, a single N-WASP binding element of EspFU can induce actin pedestal formation.
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Hallstrom, Kelly N. "The Epithelial Transmembrane Protein PERP Is Required for Inflammatory Responses to S. typhimurium Infection: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/807.

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Salmonella enterica subtype Typhimurium (S. Typhimurium) is one of many non-typhoidal Salmonella enterica strains responsible for over one million cases of salmonellosis in the United States each year. These Salmonella strains are also a leading cause of diarrheal disease in developing countries. Nontyphoidal salmonellosis induces gastrointestinal distress that is characterized histopathologically by an influx of polymorphonuclear leukocytes (PMNs), the non-specific effects of which lead to tissue damage and contribute to diarrhea. Prior studies from our lab have demonstrated that the type III secreted bacterial effector SipA is a key regulator of PMN influx during S. Typhimurium infection and that its activity requires processing by caspase-3. Although we established caspase-3 activity is required for the activation of inflammatory pathways during S. Typhimurium infection, the mechanisms by which caspase-3 is activated remain incompletely understood. Most challenging is the fact that SipA is responsible for activating caspase-3, which begs the question of how SipA can activate an enzyme it requires for its own activity. In the present study, we describe our findings that the eukaryotic tetraspanning membrane protein PERP is required for the S. Typhimuriuminduced influx of PMNs. We further show that S. Typhimurium infection induces PERP accumulation at the apical surface of polarized colonic epithelial cells, and that this accumulation requires SipA. Strikingly, PERP accumulation occurs in the absence of caspase-3 processing of SipA, which is the first time we have shown SipA mediates a cellular event without first requiring caspase-3 processing. Previous work demonstrates that PERP mediates the activation of caspase-3, and we find that PERP is required for Salmonella-induced caspase-3 activation. Our combined data support a model in which SipA triggers caspase-3 activation via its cellular modulation of PERP. Since SipA can set this pathway in motion without being cleaved by caspase-3, we propose that PERP-mediated caspase-3 activation is required for the activation of SipA, and thus is a key step in the inflammatory response to S. Typhimurium infection. Our findings further our understanding of how SipA induces inflammation during S. Typhimurium infection, and also provide additional insight into how type III secreted effectors manipulate host cells.
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Hallstrom, Kelly N. "The Epithelial Transmembrane Protein PERP Is Required for Inflammatory Responses to S. typhimurium Infection: A Dissertation." eScholarship@UMMS, 2010. http://escholarship.umassmed.edu/gsbs_diss/807.

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Salmonella enterica subtype Typhimurium (S. Typhimurium) is one of many non-typhoidal Salmonella enterica strains responsible for over one million cases of salmonellosis in the United States each year. These Salmonella strains are also a leading cause of diarrheal disease in developing countries. Nontyphoidal salmonellosis induces gastrointestinal distress that is characterized histopathologically by an influx of polymorphonuclear leukocytes (PMNs), the non-specific effects of which lead to tissue damage and contribute to diarrhea. Prior studies from our lab have demonstrated that the type III secreted bacterial effector SipA is a key regulator of PMN influx during S. Typhimurium infection and that its activity requires processing by caspase-3. Although we established caspase-3 activity is required for the activation of inflammatory pathways during S. Typhimurium infection, the mechanisms by which caspase-3 is activated remain incompletely understood. Most challenging is the fact that SipA is responsible for activating caspase-3, which begs the question of how SipA can activate an enzyme it requires for its own activity. In the present study, we describe our findings that the eukaryotic tetraspanning membrane protein PERP is required for the S. Typhimuriuminduced influx of PMNs. We further show that S. Typhimurium infection induces PERP accumulation at the apical surface of polarized colonic epithelial cells, and that this accumulation requires SipA. Strikingly, PERP accumulation occurs in the absence of caspase-3 processing of SipA, which is the first time we have shown SipA mediates a cellular event without first requiring caspase-3 processing. Previous work demonstrates that PERP mediates the activation of caspase-3, and we find that PERP is required for Salmonella-induced caspase-3 activation. Our combined data support a model in which SipA triggers caspase-3 activation via its cellular modulation of PERP. Since SipA can set this pathway in motion without being cleaved by caspase-3, we propose that PERP-mediated caspase-3 activation is required for the activation of SipA, and thus is a key step in the inflammatory response to S. Typhimurium infection. Our findings further our understanding of how SipA induces inflammation during S. Typhimurium infection, and also provide additional insight into how type III secreted effectors manipulate host cells.
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Books on the topic "Microfilament proteins"

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G, Dos Remedios Cristobal, and Chhabra Deepak, eds. Actin-binding proteins and disease. New York: Springer, 2008.

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G, Dos Remedios Cristobal, and Chhabra Deepak, eds. Actin-binding proteins and disease. New York: Springer, 2008.

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1935-, Ishikawa Harunori, Hatano Sadashi 1929-, Satō Hidemi 1926-, and Yamada Conference (10th : 1984 : Nagoya-shi, Japan), eds. Cell motility: Mechanism and regulation. New York: A.R. Liss, 1986.

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Eichinger, Ludwig, Christoph S. Clemen, and Vasily Rybakin. Coronin Family of Proteins. Springer, 2010.

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C.G. dos Remedios (Editor) and D. D. Thomas (Editor), eds. Molecular Interactions of Actin: Actin Structure and Actin-Binding Proteins (Results and Problems in Cell Differentiation). Springer, 2000.

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Actin-binding proteins and disease. New York: Springer, 2008.

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Chhabra, Deepak, and Cris dos Remedios. Actin-Binding Proteins and Disease. Springer London, Limited, 2008.

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(Editor), D. D. Thomas, and C.G. dos Remedios (Editor), eds. Molecular Interactions of Actin: Actin-Myosin Interaction and Actin-Based Regulation (Results and Problems in Cell Differentiation). Springer, 2002.

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Microscopic origin of the elasticity of F-actin networks. 2007.

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Lin, Yi-Chia. Elasticity of biopolymer networks. 2009.

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Book chapters on the topic "Microfilament proteins"

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Isenberg, G. "Ca-Dependent and Ca-Independent F-Actin Capping Proteins Determine Microfilament Assembly in Neuronal Cells." In Calcium Electrogenesis and Neuronal Functioning, 271–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70744-5_25.

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Schoepper, Beate, Christiane Weigt, and Albrecht Wegner. "Regulation of Microfilament Assembly." In Cellular Regulation by Protein Phosphorylation, 421–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75142-4_51.

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Maciver, Sutherland K. "Microfilament organization and actin-binding proteins." In The Cytoskeleton: A Multi-Volume Treatise, 1–45. Elsevier, 1995. http://dx.doi.org/10.1016/s1874-6020(06)80004-2.

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Ampe, Christophe, and Joël Vandekerckhove. "Assaying binding and covalent modifications of cytoskeletal proteins." In Cytoskeleton: signalling and cell regulation, 9–36. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780199637829.003.0002.

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Abstract Cytoskeletal dynamics are essential for cell survival. The microfilament system is one of the major players in cell motility processes. It exerts force for movement either by the action of molecular motors on relatively stable filaments or by dynamic turnover of actin filaments. In the latter case processes such as filament polymerization, depolymerization. and bundling are regulated in a temporal and spatial manner, governed by actin-binding proteins. The complexity of the actin system arises from the multitude of actin-binding proteins, often with partly overlapping activities, displaying multiple functions or effects on actin polymerization, depending on the intracellular environment. Therefore, detailed biochemical studies of individual actin-binding proteins and their interaction with actin or with regulatory ligands are necessary to understand cellular motility phenomena. The field is now slowly progressing towards in vitro studies with more than one actin-binding protein, because it is dear that in cells these proteins either compete with each other or have additive or co-operative effects on aetin reorganization.
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Hock, Rick S. "Filamin." In Guidebook to the Cytoskeletal and Motor Proteins, 94–96. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.0029.

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Abstract Filamin, a major component of the microfilament network, plays a critical role in determining the three-dimensional arrangement of actin filaments in vivo and in vitro (reviewed in ref. 1). This actin-cross-linking protein was first isolated from avian smooth muscleand has been purified from many sources including platelets, macrophages, guinea-pig vas deferens, baby hamster kidney (BHK-21) cells, thyroid gland, Hela cells, and motile Dictyostelium amoebae. Filamin is now known to exist in most cell types as a family of isoforms. The number of isoforms has not been defined, although multiple isoforms are apparently present within a single human cell type, Hela cells. Also, isoform switching occurs during myogenesis.
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Benarroch, Eduardo E. "Cytoskeleton." In Neuroscience for Clinicians, edited by Eduardo E. Benarroch, 126–43. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780190948894.003.0008.

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The cytoskeleton consists primarily of microfilaments, microtubules, and intermediate filaments. Actin microfilaments have major role in growth, maintenance, and dynamic changes of growth cones and dendrites; stabilization of proteins at specific membrane locations; and vesicle dynamics during endocytosis and exocytosis. Microtubules provide the major tracks for intracellular transport and local cues for positioning of mitochondria and other organelles. The intermediate filaments in neurons are the neurofilaments that have a major role in regulating axonal caliber and mechanical stability. Glial fibrillary acid protein is a primary component of intermediate filaments in astrocytes. Nuclear lamins participate in regulation of the chromatin organization, trafficking of transcription factors across the nuclear envelope, and transduction of mechanical signals. Mutations affecting these cytoskeletal proteins produce a wide range of neurologic disorders, including neurodevelopmental disorders, peripheral neuropathies, myopathies, and leukodystrophy. All components of the cytoskeleton are involved in adult-onset neurodegenerative disorders.
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Aktories, K. "Introduction." In Guidebook to Protein Toxins and Their Use in Cell Biology, 63–65. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198599555.003.0022.

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Abstract Many cellular functions depend on the cytoskeleton. The cytoskeleton controls the shape and the spatial organization of the cell. It participates in all kinds of cellular movement and transport and is involved in processes like endo-and exocytosis, vesicle transport, cell-cell contact, and mitosis. The cytoskeleton consists of a fibre network that is formed of three major filament systems which are highly dynamic structures: the microfilaments, the micro-tubules, and the intermediate filaments. Rapid structural changes of these cytoskeletal proteins are based on their ability to polymerize and depolymerize. Much of what we know about functions of these proteins has been learned from the use of cytotoxins which have been applied as cell biological tools. The group of cytoskeleton-affecting toxins comprises agents which act directly on elements of the cytoskeleton but also toxins that affect regulatory components (e.g. low molecular mass GTP-binding proteins) which control the organization of the cytoskeleton. The toxins can be subdivided into protein toxins with enzymatic activity, protein toxins without apparent enzymic activity, and small non-proteinaceous compounds which bind to the cytoskeleton proteins. The bacterial protein toxins appear to act predominantly on the actin cytoskeleton.
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Parry, David A. D. "Structural features of IF proteins." In Guidebook to the Cytoskeletal and Motor Proteins, 285–90. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.0093.

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Abstract Intermediate filaments (IF), a constituent of almost all eukaryotic cells, are one of three major classes of intra-cellular filaments, the others being the microtubules (about 25 nm in diameter) and the actin-containing microfilaments (about 10 nm in diameter). Initially, the intermediate filaments (IF) were thought to be intermediate in size between the microtubules and the micro-filaments, hence their name, but subsequent structural characterization showed that discrimination on the basis of size was uncertain since IF and microfilaments have similar diameters. Intermediate filaments are not restricted to the cytoplasm but are found also within the nuclear envelope. Generally, however, long sinuous bundles of IF extend from the outer surface of the cell nucleus to the adhesion plaques or desmosomes on the inner surface of the cell membrane.
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Haddad, John G., and Nancy E. Cooke. "Vitamin D-binding/Gc protein." In Guidebook to the Cytoskeletal and Motor Proteins, 179–81. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.0057.

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Abstract This plasma a-globulin is in the albumin, a-fetoprotein family and is synthesized predominantly in the liver. It circulates at a 20-fold higher titre than its mot/mot, vitamin D sterol-ligands, thereby providing their conservation, solubility, and transport in the blood. The protein also binds globular actin at high affinity and constitutes, along with gelsolin, a plasma-actin-scavenger system. Cell surface associations and metabolism of the protein suggest its cellular entry into phagolysosomes, although its direct cellular injection causes a reversible disassembly of microfilaments. Preliminary findings suggest that this protein’s absence in an experimental murine null homozygote can lead to abnormalities in monocytelmacrophage development and activation, as previously suggested by its behaviour as a co-chemotaxin and macrophage activator.
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Reinhard, Matthias, Thomas Jarchau, Kathrin Reinhard, and Ulrich Walter. "VASP." In Guidebook to the Cytoskeletal and Motor Proteins, 168–71. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780198599579.003.0054.

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Abstract VASP, a praline-rich protein substrate of both cAMP- and cGMP-dependent protein kinases, is expressed in most mammalian cell types and tissues. Particularly high VASP levels are detected in human platelets. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions such as the leading edge. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation.
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Conference papers on the topic "Microfilament proteins"

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Dejana, E., L. R. Languino, S. Colella, E. Plow, M. Ginsberg, and P. C. Marchisio. "THE LOCALIZATION OF PLATELET GpIIb-IIIa RELATED PROTEINS IN ENDOTHELIAL CELL ADHESION STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642814.

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Different laboratories bave reported that human endothelial cells (EC) synthesize and express surface proteins biochemically and immunologically related to platelet GpIIb-IIIa. However the functional role of this glycoprotein complex in EC has not yet been elucidated. In this study we investigated whether these molecules are involved in the process of EC adhesion to different substrata. Cultured human umbilical vein ECs ,seeded on purified fibrinogen(fg), or vitronectin(VN) coated coverslips, adhered ,underwent spreading, organization of thick microfilament bundles and formation of focal contacts as shown by immunofluorescence and interference reflection microscopy.Polyclonal antibodies raised against human platelet GpIIb-IIIa and cross reacting with the EC form, showed by immunofluorescence a discrete and well organized distribution at cell adhesion structures, Indeed they distributed at vinculin rich focal contacts at the membrane insertion of microfilament bundles of stress fiber type.They were also found at cell to cell contacts and in a diffuse pattern at the dorsal surface of EC.GpIIb-IIIa antibodies added to EC suspensions prior to plating inhibited EC adhesion and spreading in a concentration dependent way. This effect was present at different degrees when EC were seeded on fg or VN being clearly more evident on VN and somehow less apparent on fg.In addition when the antibodies were added to confluent EC monolayers for 24 h they disrupted cell to cell contacts and caused cell rounding and detachment Preimmune serum or control antibodies able to bind to EC external membrane but which did not recognized GpIIb-IIIa proteins were unable to inhibit EC attachment and spreading. These results indicate that EC GpIIb-IIIa complex is involved in the adhesion mechanism of these cells to extracellular matrix proteins.
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Muszbek, L., R. Adåny, M. A. Glukhova, M. G. Frid, A. E. Kabakov, and V. E. Kot-e-liansky. "THE IDENTIFICATION OF VIMENTIN, AN INTERMEDIATE,FILAMENT SUBUNIT PROTEIN IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643900.

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In platelets the presence of basic subunit proteins of microtubules as well as microfilaments has been verified a long time ago and it was also shown that both of these cytoskeletal systems go through a tremendous reorganization during the activation process. Surprisingly, none of the components of intermediate filaments has so far been identified in these cells, perhaps because platelets were considered too motile to have intermediate filaments, the most static structures among the three major cytoskeletal systems. By using two different monoclonal antibodies (II C4 and II D8) here we attempted to establish if vimen-tin, an intermediate filament subunit protein present in most differentiating cells, in cells grown in tissue culture and in certain fully differentiated cells also exists in human platelets The IgM type antibodies were characterized by various immuno-morphological and immunobiochemical techniques. They labelled selectively colcemid-sensitive filamentous structures in fibroblasts, in endothelial cells and in vascular but not myometrium smooth muscle and were shown to be monospecific against epitopes on vimentin in fibroblast homogenate. When whole platelet homogenate was submitted to high resolution gradient SDS PAGE and then electroblotted to nitrocellulose sheet, both antibodies reacted with a single protein band of 55 kD that comigrated with fibroblast vimentin. By immunofluorescence microscopy an annular ring-like structure was stained for vimentin that suggests a membran skeletal role for this protein. During pseu-dopode formation a redistribution of vimentin could be observed. Parallel with the disappearance of ring-like structures vimentin appears in pseudopodia suggesting that like in the case of other filamentous systems platelet activation induces a structural reorganization of the intermediate filaments, as well.
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Buehler, Markus J., and Zhao Qin. "Hierarchical Structure Controls Nanomechanical Properties of Vimentin Intermediate Filaments." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13102.

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Intermediate filaments (IFs), in addition to microtubules and microfilaments, are one of the three major components of the cytoskeleton in eukaryotic cells, playing a vital role in mechanotransduction and in providing mechanical stability to cells (Figure 1) [1]. Despite the importance of IF mechanics for cell biology and cell mechanics, the structural basis for their mechanical properties remains unknown. Specifically, our understanding of fundamental filament properties, such as the basis for their great extensibility, stiffening properties, and their exceptional mechanical resilience remains limited. This has prevented us from answering fundamental structure-function relationship questions related to the biomechanical role of intermediate filaments, which is crucial to link structure and function in the protein material’s biological context.
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Chang, Jun Keun, and Dong Chul Han. "Etiological Expression of Heat Shock Protein 70 (HSP70) in Human Endothelial Cells With Hemodynamic Shear Stress." In ASME 1999 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1999. http://dx.doi.org/10.1115/imece1999-0368.

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Abstract The expression of heat shock protein 70 (hsp70) and the polymerization of the actin cytoskeleton of human umbilical vein endothelial cells (HUVECs) were investigated with the endothelial cell-extracellular matrix system and the laminar flow chamber appratus. Shear stress-induced polymerization of the actin cytoskeleton of HUVEC was summarized with the formation of the ‘dense peripheral band’ after 5 min exposure of flow, shear-induced focal contact formation at the proximal periphery, and the aligned actin microfilament formation to the direction of flow. In contrast to the intranucleous expression of hsp70 with the conventioanl heat shock, perinuclear expression of hsp70 was detected with the laser scanning confocal microscope and the western blotting of HUVECs exposed to 15 dyne/cm2 shear stress for 1 hour. Expression of hsp70 in perinuclear region increased with proportional to the magnitude of shear stress. The polymerization of cytoplasmic actin cytoskeleton and the cytoplasmic expression of hsp70 may prevent the cellular damage from the pathophysiological stimulus that initiate vascular cell disease, such as the atherosclerosis. Consequently, three-dimensional intracellular expression and the localization of protein and organelles play an important role in the signal transduction generated by the mechanical cue, such as fluid shear stress.
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Buehler, Markus J., and Je´re´mie Bertaud. "Hierarchical Structure Controls Nanomechanical Properties of Vimentin Intermediate Filaments." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13103.

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Intermediate filaments (often abbreviated as IFs), in addition to microtubules and microfilaments, are one of the three major components of the cytoskeleton in eukaryotic cells (Figure 1). It has been suggested that intermediate filaments are crucial in defining key mechanical functions of cells such as cell migration, cell division and mechanotransduction, and have also been referred to as the “safety belts of cells” reflecting their role in preventing exceedingly large cell stretch [1, 2]. Vimentin is a specific type of this protein filament found in fibroblasts, leukocytes, and blood vessel endothelial cells, representing the most widely distributed type of intermediate filaments. Several diseases have been linked to the structure and density of intermediate filaments. Here we report a systematic study of the effects of intermediate filaments on cell mechanics, specifically focused on changes in the density of filaments. We compare the results with experimental studies in vimentin deficient cells, showing good qualitative agreement.
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Buehler, Markus J., and Zhao Qin. "Structure Prediction and Nanomechanical Properties of Human Vimentin Intermediate Filament Dimers." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-204824.

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Intermediate filaments (IFs), in addition to microtubules (MTs) and microfilaments (MFs), are one of the three major components of the cytoskeleton in eukaryotic cells. As the basic building block of IFs, the properties of the IF dimmer re crucial to fully understand the molecular basis for the properties of the IF network in cells. However, the structure of IF dimers remains unknown, which has thus far prevented the elucidation of its nanomechanical properties, in particular molecular-level mechanisms of deformation. Here we present the development of a full atomistic molecular model of the vimentin dimmer, a coiled-coil structure consisting of four alpha-helixes (AHs). The structure is found to be stable in molecular dynamics simulation after an extensive equilibration process. After careful structure prediction, the behavior of the IF dimer under mechanical stress is investigated; including studies of changing the pulling velocity and a detailed analysis of the associated deformation and rupture mechanisms. Most notably, we observe a transition of AHs to beta-sheets (BSs) under mechanical deformation, as has been observed indirectly in earlier experimental studies. Our result helps to better understand the structure and fracture mechanism of this important protein filament.
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Horvåth, A., G. M. Asyee, A. Sturk, and L. Muszbek. "ASSOCIATION OF VINCULIN TO THE PLATELET CYTOSKELET0N DURING RELEASE REACTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643901.

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Vinculin is an Mr 130 kD protein, which in various cell types is located at the membrane attachment site of microfilaments and has been implicated in membrane-cytoskeleton interaction. Though we have previously verified its presence in platelets and showed that in resting platelets it is localized submembra-neously and around the ±-granules, its relation to the cytos-keleton is still to be elucidated. It has been also revealed by biochemical studies that in resting bovine gel filtered platelets vinculin is not cytoskeletal component, however about 50% of the total vinculin content became incorporated into the cytoskeleton during thrombin activation. To establish if its association to the cytoskeleton occured during pseudopode formation, aggregation or release reaction, cytoskeletons were prepared from platelets activated in various conditions and the time course of vinculin incorporation was analyzed by immuno-blotting. When pseudopode formation was inhibited by cytochalasin B pretreatment but neither aggregation nor release reaction induced by thrombin was prevented, the amount of vinculin in the Triton insoluble residue even increased. Phorbol myristate acetate (PMA), which induces pseudopode but not contractile gel formation, is a strong stimulus for aggregation, but induces only a slight release of the granule content. In parallel, only a low amount of vinculin was recovered in the cytoskeletal fraction following PMA induced aggregation. In contrast, when release reaction elicited by thrombin occured in the absence of aggregation the association of vinculin did not diminished.The results clearly demonstrate, that platelet shape change and pseudopode formation are not prerequisites of the incorporation of vinculin into the cytoskeleton, which occurs parallel to the release reaction.
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Braun, M., M. Fountoulakis, I. Seidel, T. Höller, K. Yeghiazaryan, H. Schild, W. Kuhn, and O. Golubnitschaja. "Differential expression of microfilamental network-associated proteins in circulating leukocytes of patients with benign and malignant breast tumorsversuscontrols as revealed by clinical proteomics: potential application to early and predictive diagnosis." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-2037.

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Shibatay, N., K. Tanaka, K. Okamoto, and T. Onji. "REORGANIZATION OF ACTIN AND MYOSIN IN THE ACTIVATED PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643539.

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This study was done to clarify the intracellular dynamic arrangements of myosin(My) and actin(Ac) in activation process of human platelets (PLs) from unactivated to activated stage (clot retraction) in electron microscopy. The observation of unactivated PLs was done either in the fresh whole blood fixed directly with 0.1 % glutaraldehyde or in PLs isolated by gel filtration of platelet rich plasma(PRP) containing prostaglandin I2 (10 ng/ml). The isolated PLs mounted on a glass cover slip were used as activated PLs (adrerent ones). The contracted PLs were prepared in PRP incubated with thrombin (0.5 u/ml) and 20 mM CaCl- for 10-60 min. Treating PLs with 0.15 % Triton X-100 containing 0.05 % glutaraldehyde produced cytoskeleton. My and F-Ac were identified by an indirect immuno-cytochemical method using the specific antibody (rabbit IgG) against PL-My and protein A-gold and by demonstration of in “arrow-head” decoration by Ishikawa's method using skeletal meromyosin (HMM), respectively. [Results] (1) Unactivated PLs. Mys in monomer or oligomer distributed homogenously in scare association with cytoskeleton. Cytoskeletons were exclusively composed of F-Ac networks of crossolinked short filaments which were thinly distributed in the cytoplasm with partial connection to the cell membrance. (2) Surface activated spreading PLs. PLs adhered to the glass cover slip in dendritic forms. Mys were densely located around granulomere and formed linear arrays associated with F-Ac filaments of the cytoskeleton surrounding the granulomere and running straightly in cytoplasm. (3) Contracted PLs. Activated PLs protruded several filopodia in which networks or bundles of F-Ac filaments were found connecting to extracellular fibrin strand through cell membrene. Microfilaments formed arrow-head decoration with HMM pointing toward the cell body. The cytoskeleton in contracted PLs contained thick filaments of My-polymers attaching to F-Ac filaments end by end. It is concluded that the reorganization of Ac-My is the basis for the shape change, secretion and clot retraction of activated PLs.
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