Relevant bibliographies by topics / Apha Smooth Muscle Actin

Academic literature on the topic 'Apha Smooth Muscle Actin'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Apha Smooth Muscle Actin"

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Puzdrova, V. A., T. V. Kudryashova, D. K. Gaynullina, S. V. Mochalov, C. Aalkjaer, H. Nilsson, A. V. Vorotnikov, R. Schubert, and O. S. Tarasova. "Trophic action of sympathetic nerves reduces arterial smooth muscle Ca2+sensitivity during early post-natal development in rats." Acta Physiologica 212, no. 2 (July 3, 2014): 128–41. http://dx.doi.org/10.1111/apha.12331.

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Gown, A. M., A. M. Vogel, D. Gordon, and P. L. Lu. "A smooth muscle-specific monoclonal antibody recognizes smooth muscle actin isozymes." Journal of Cell Biology 100, no. 3 (March 1, 1985): 807–13. http://dx.doi.org/10.1083/jcb.100.3.807.

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Injection of chicken gizzard actin into BALB/c mice resulted in the isolation of a smooth muscle-specific monoclonal antibody designated CGA7. When assayed on methanol-Carnoy's fixed, paraffin-embedded tissue, it bound to smooth muscle cells and myoepithelial cells, but failed to decorate striated muscle, endothelium, connective tissue, epithelium, or nerve. CGA7 recognized microfilament bundles in early passage cultures of rat aortic smooth muscle cells and human leiomyosarcoma cells but did not react with human fibroblasts. In Western blot experiments, CGA7 detected actin from chicken gizzard and monkey ileum, but not skeletal muscle or fibroblast actin. Immunoblots performed on two-dimensional gels demonstrated that CGA7 recognizes gamma-actin from chicken gizzard and alpha- and gamma-actin from rat colon muscularis. This antibody was an excellent tissue-specific smooth muscle marker.
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Chistiakov, D. A., A. N. Orekhov, and Y. V. Bobryshev. "Vascular smooth muscle cell in atherosclerosis." Acta Physiologica 214, no. 1 (February 25, 2015): 33–50. http://dx.doi.org/10.1111/apha.12466.

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Wong, Jean Z., Janet Woodcock-Mitchell, John Mitchell, Patricia Rippetoe, Sheryl White, Marlene Absher, Linda Baldor, John Evans, Kirk M. McHugh, and Robert B. Low. "Smooth muscle actin and myosin expression in cultured airway smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 274, no. 5 (May 1, 1998): L786—L792. http://dx.doi.org/10.1152/ajplung.1998.274.5.l786.

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In this study, the expression of smooth muscle actin and myosin was examined in cultures of rat tracheal smooth muscle cells. Protein and mRNA analyses demonstrated that these cells express α- and γ-smooth muscle actin and smooth muscle myosin and nonmuscle myosin-B heavy chains. The expression of the smooth muscle specific actin and myosin isoforms was regulated in the same direction when growth conditions were changed. Thus, at confluency in 1 or 10% serum-containing medium as well as for low-density cells (50–60% confluent) deprived of serum, the expression of the smooth muscle forms of actin and myosin was relatively high. Conversely, in rapidly proliferating cultures at low density in 10% serum, smooth muscle contractile protein expression was low. The expression of nonmuscle myosin-B mRNA and protein was more stable and was upregulated only to a small degree in growing cells. Our results provide new insight into the molecular basis of differentiation and contractile function in airway smooth muscle cells.
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Sulbarán, Guidenn, Lorenzo Alamo, Antonio Pinto, Gustavo Márquez, Franklin Méndez, Raúl Padrón, and Roger Craig. "An invertebrate smooth muscle with striated muscle myosin filaments." Proceedings of the National Academy of Sciences 112, no. 42 (October 6, 2015): E5660—E5668. http://dx.doi.org/10.1073/pnas.1513439112.

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Muscle tissues are classically divided into two major types, depending on the presence or absence of striations. In striated muscles, the actin filaments are anchored at Z-lines and the myosin and actin filaments are in register, whereas in smooth muscles, the actin filaments are attached to dense bodies and the myosin and actin filaments are out of register. The structure of the filaments in smooth muscles is also different from that in striated muscles. Here we have studied the structure of myosin filaments from the smooth muscles of the human parasite Schistosoma mansoni. We find, surprisingly, that they are indistinguishable from those in an arthropod striated muscle. This structural similarity is supported by sequence comparison between the schistosome myosin II heavy chain and known striated muscle myosins. In contrast, the actin filaments of schistosomes are similar to those of smooth muscles, lacking troponin-dependent regulation. We conclude that schistosome muscles are hybrids, containing striated muscle-like myosin filaments and smooth muscle-like actin filaments in a smooth muscle architecture. This surprising finding has broad significance for understanding how muscles are built and how they evolved, and challenges the paradigm that smooth and striated muscles always have distinctly different components.
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Skalli, O., P. Ropraz, A. Trzeciak, G. Benzonana, D. Gillessen, and G. Gabbiani. "A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation." Journal of Cell Biology 103, no. 6 (December 1, 1986): 2787–96. http://dx.doi.org/10.1083/jcb.103.6.2787.

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A monoclonal antibody (anti-alpha sm-1) recognizing exclusively alpha-smooth muscle actin was selected and characterized after immunization of BALB/c mice with the NH2-terminal synthetic decapeptide of alpha-smooth muscle actin coupled to keyhole limpet hemocyanin. Anti-alpha sm-1 helped in distinguishing smooth muscle cells from fibroblasts in mixed cultures such as rat dermal fibroblasts and chicken embryo fibroblasts. In the aortic media, it recognized a hitherto unknown population of cells negative for alpha-smooth muscle actin and for desmin. In 5-d-old rats, this population is about half of the medial cells and becomes only 8 +/- 5% in 6-wk-old animals. In cultures of rat aortic media SMCs, there is a progressive increase of this cell population together with a progressive decrease in the number of alpha-smooth muscle actin-containing stress fibers per cell. Double immunofluorescent studies carried out with anti-alpha sm-1 and anti-desmin antibodies in several organs revealed a heterogeneity of stromal cells. Desmin-negative, alpha-smooth muscle actin-positive cells were found in the rat intestinal muscularis mucosae and in the dermis around hair follicles. Moreover, desmin-positive, alpha-smooth muscle actin-negative cells were identified in the intestinal submucosa, rat testis interstitium, and uterine stroma. alpha-Smooth muscle actin was also found in myoepithelial cells of mammary and salivary glands, which are known to express cytokeratins. Finally, alpha-smooth muscle actin is present in stromal cells of mammary carcinomas, previously considered fibroblastic in nature. Thus, anti-alpha sm-1 antibody appears to be a powerful probe in the study of smooth muscle differentiation in normal and pathological conditions.
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Conley, Catharine A. "Leiomodin and tropomodulin in smooth muscle." American Journal of Physiology-Cell Physiology 280, no. 6 (June 1, 2001): C1645—C1656. http://dx.doi.org/10.1152/ajpcell.2001.280.6.c1645.

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Evidence is accumulating to suggest that actin filament remodeling is critical for smooth muscle contraction, which implicates actin filament ends as important sites for regulation of contraction. Tropomodulin (Tmod) and smooth muscle leiomodin (SM-Lmod) have been found in many tissues containing smooth muscle by protein immunoblot and immunofluorescence microscopy. Both proteins cofractionate with tropomyosin in the Triton-insoluble cytoskeleton of rabbit stomach smooth muscle and are solubilized by high salt. SM-Lmod binds muscle tropomyosin, a biochemical activity characteristic of Tmod proteins. SM-Lmod staining is present along the length of actin filaments in rat intestinal smooth muscle, while Tmod stains in a punctate pattern distinct from that of actin filaments or the dense body marker α-actinin. After smooth muscle is hypercontracted by treatment with 10 mM Ca2+, both SM-Lmod and Tmod are found near α-actinin at the periphery of actin-rich contraction bands. These data suggest that SM-Lmod is a novel component of the smooth muscle actin cytoskeleton and, furthermore, that the pointed ends of actin filaments in smooth muscle may be capped by Tmod in localized clusters.
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Reneman, Robert S. "Preface to ‘Electrical propagation in smooth muscle organs’." Acta Physiologica 213, no. 2 (December 19, 2014): 346. http://dx.doi.org/10.1111/apha.12433.

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Lammers, W. J., and G. J. van der Vusse. "Introduction to ‘Electrical propagation in smooth muscle organs’." Acta Physiologica 213, no. 2 (December 17, 2014): 347–48. http://dx.doi.org/10.1111/apha.12434.

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Hansson, G. K., M. Hellstrand, L. Rymo, L. Rubbia, and G. Gabbiani. "Interferon gamma inhibits both proliferation and expression of differentiation-specific alpha-smooth muscle actin in arterial smooth muscle cells." Journal of Experimental Medicine 170, no. 5 (November 1, 1989): 1595–608. http://dx.doi.org/10.1084/jem.170.5.1595.

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Differentiation of muscle cells is characterized morphologically by the acquisition of contractile filaments and characteristic shape changes, and on the molecular level by induction of the expression of several genes, including those for the muscle-specific alpha-actin isoforms. IFN-gamma is an inhibitor of proliferation for several cells, including vascular smooth muscle, and is also an inducer of differentiated properties for several hematopoietic cells. We have therefore investigated whether IFN-gamma affects the expression of alpha-smooth muscle actin in cultured arterial smooth muscle cells. Cells exposed to IFN-gamma show a reduction of alpha-smooth muscle actin-containing stress fibers, as detected by immunofluorescence. The effect was observed in all phases of the cell cycle, and was caused by a reduction of the synthesis of alpha-smooth muscle actin protein as revealed by two-dimensional electrophoretic analysis of actin isoforms. RNA hybridization using a cRNA probe that hybridizes to all actin mRNAs showed that IFN-gamma-treated cells have a reduced content of the 1.7-kb mRNA that codes for alpha-smooth muscle actin, and to a lesser extent, also of the 2.1-kb mRNA encoding the beta and gamma-cytoplasmic actins. The reduction of alpha-smooth muscle actin mRNA was confirmed using an alpha-smooth muscle actin-specific cRNA probe. The reduction of alpha-smooth muscle actin mRNA occurs within 12 h, and is dependent on protein synthesis, since cycloheximide treatment reversed the effect. The inhibition of this mRNA species was dose dependent, and detectable by RNA hybridization at a dose of 50 U/ml IFN-gamma. These results suggest that the differentiation of arterial smooth muscle cells is not necessarily coupled to an inhibition of cellular proliferation. Instead, IFN-gamma may regulate the expression of several genes that control both proliferation and expression of differentiation markers.
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Dissertations / Theses on the topic "Apha Smooth Muscle Actin"

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Black, Jason Edward. "Association of smooth muscle myosin and its carboxyl isoforms with actin isoforms in aorta smooth muscle." Huntington, WV : [Marshall University Libraries], 2007. http://www.marshall.edu/etd/descript.asp?ref=803.

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Theses (Ph. D.)--Marshall University, 2007.
Title from document title page. Includes abstract. Document formatted into pages: contains xiii, 124 pages including illustrations. Includes vitae. Bibliographical references at the end of Chapters 1-3.
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Brown-Turner, Dawn Leah. "Regulation of alpha- and beta-actin isoforms in the contracting A7r5 smooth muscle cell." [Huntington, WV : Marshall University Libraries], 2009. http://www.marshall.edu/etd/descript.asp?ref=1009.

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Pieri, Maria. "Regulation of vascular smooth muscle actin cytoskeleton by Hic-5." Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/regulation-of-vascular-smooth-muscle-actin-cytoskeleton-by-hic5(3309e74d-0a10-4d04-b741-a99f64075620).html.

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Vascular smooth muscle cells (VSMC) constitute an important component of blood vessels and are primarily responsible for vessel contraction. In vascular disorders such as hypertension and atherosclerosis as well as pregnancy and exercise, VSMC demonstrate increased capacity to proliferate and migrate, resulting in vascular remodelling. The actin cytoskeleton is an important component of vascular contractility and is also essential for proliferation and migration of VSMC. Vasoactive agonists such as Endothelin-1 (ET-1) and Noradrenaline (NA), have been shown to mediate VSMC contraction through changes in actin cytoskeleton and focal adhesion (FA) remodelling, and have also been reported to cause VSMC migration in the appropriate setting. The aim of this study was to investigate the signalling mechanisms responsible for FA dependent actin cytoskeleton remodelling of VSMC in response to ET-1 and NA, with a special focus on Hydrogen peroxide-inducible clone 5 (Hic-5). The latter is a FA protein shown to regulate actin cytoskeleton dynamics in small arteries in response to Noradrenaline (NA) and the response of VSMC to arterial injury and abdominal aortic aneurysm. We have shown that Src-dependent tyrosine phosphorylation of Hic-5 regulated its subcellular localisation in mouse embryonic fibroblasts and VSMC, but was not responsible for the effects of ET-1 and NA on actin filament remodelling or Hic-5 redistribution in VSMC. ET-1 stimulation caused an increase in Hic-5 localisation at FAs concurrent with an increase in the density of actin filaments, whereas NA stimulation caused a decrease in Hic-5 localisation at FAs in VSMC concurrent with actin filament redistribution at the cell cortex. Hic-5 was the FA protein that demonstrated the most dramatic changes in subcellular localisation in response to ET-1 and NA, when compared to paxillin (Hic-5 homologue) or vinculin (classical FA marker). NA-mediated changes in Hic-5 localisation and actin filament distribution were more pronounced compared to ET-1-mediated changes. Further investigation into the NA-induced changes suggested that actin filament disassembly preceded Hic-5 relocalisation from FAs to the cytosol. These results show that vasoactive peptides cause Hic-5 relocalisation and actin filament rearrangement in VSMCs in an agonist-dependent manner. Given that VSMC FA remodelling and actin cytoskeleton reorganisation occur during contraction and arterial remodelling, our data identify Hic-5 as a key regulator of these processes in response to NA and ET-1. Furthermore, these data have implications in agonist- specific VSM function such as migration and contraction.
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Fultz, Michael E. "Actin and myosin remodeling in the A7r5 smooth muscle cell." Huntington, WV : [Marshall University Libraries], 2002. http://www.marshall.edu/etd/descript.asp?ref=126.

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Thesis (Ph. D.)--Marshall University, 2002.
Title from document title page. Document formatted into pages; contains ix, 128 p. Includes abstract. Bibliographical references are at the end of each chapter.
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Thatcher, Sean Eric. "MLCK/actin interaction in the contracting A7r5 cell and vascular smooth muscle." Huntington, WV : [Marshall University Libraries], 2007. http://www.marshall.edu/etd/descript.asp?ref=736.

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Theses (Ph. D.)--Marshall University, 2007.
Title from document title page. Includes abstract. Document formatted into pages: contains x, 102 pages including illustrations. Bibliographical references at the end of each chapter.
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Li, Chenwei. "PKC[alpha] translocation and actin remodeling in contracting A7r5 smooth muscle cells." Huntington, WV : [Marshall University Libraries], 2002. http://www.marshall.edu/etd/descript.asp?ref=62.

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Thesis (Ph. D.)--Marshall University, 2002.
Title from document title page. Document formatted into pages; contains xi, 136 p. with illustrations. Includes abstract. Includes bibliographical references (p. 120-136).
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SARIHAN, PRIYANKA, and R. Clark Lantz. "THE EFFECT OF ARSENIC ON SMOOTH MUSCLE ACTIN IN THE LUNG." Thesis, The University of Arizona, 2008. http://hdl.handle.net/10150/192233.

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Lee, Sang Hoon. "Proteoglycans mediate smooth muscle a-Actin gene expression in BC3H1 Myogenic cells /." The Ohio State University, 1994. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487859879938747.

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Qu, Guang. "Vascular Smooth Muscle (alpha)-Actin Utilization: Functional Significance in BC3H1 Myogenic Cell Differentiation /." The Ohio State University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487931512617692.

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Polikandriotis, John Anastasios. "Elucidating the regulation of vascular smooth muscle alpha-actin gene expression in fibroblasts." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1078857443.

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Thesis (Ph. D.)--Ohio State University, 2004.
Title from first page of PDF file. Document formatted into pages; contains xiv, 177 p.; also includes graphics (some col.). Includes bibliographical references (p. 160-177).
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Books on the topic "Apha Smooth Muscle Actin"

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Kazuhiro, Kohama, and Sasaki Yasuharu, eds. Molecular mechanisms of smooth muscle contraction. Austin, Tex: R.G. Landes Co., 1999.

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Narani, Nazanin. TGF-B1 regulation of alpha-smooth muscle actin expression in fibroblasts is dependent on the deformability of the substrate. [Toronto: University of Toronto, Faculty of Dentistry], 1997.

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Wang, Jiaxu. Regulation of [alpha]-smooth muscle actin by mechanical force. 2005.

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Zhao, Xiao-Han. Mechanical induction of alpha-smooth muscle actin expression involves the rho-rho kinase pathway. 2006.

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Book chapters on the topic "Apha Smooth Muscle Actin"

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Dąbrowska, Renata. "Actin and Thin-Filament-Associated Proteins in Smooth Muscle." In Airways Smooth Muscle: Biochemical Control of Contraction and Relaxation, 31–59. Basel: Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7681-0_2.

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Ye, Li-Hong, Kohichi Hayakawa, Tsuyoshi Okagaki, and Kazuhiro Kohama. "Actin-Binding Property of Myosin Light Chain Kinase and Its Role in Regulating Actin-Myosin Interaction of Smooth Muscle." In Regulation of the Contractile Cycle in Smooth Muscle, 159–73. Tokyo: Springer Japan, 1995. http://dx.doi.org/10.1007/978-4-431-65880-1_10.

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Hahn, H., and J. Fingerle. "Changes of smooth muscle α-actin expression in an organ culture system of rabbit thoracic aorta." In Arteriosklerotische Gefäßerkrankungen, 253–63. Wiesbaden: Vieweg+Teubner Verlag, 1992. http://dx.doi.org/10.1007/978-3-663-19646-4_28.

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Tesic, N., U. Kamensek, G. Sersa, and M. Cemazar. "Evaluation of Smooth Muscle γ Actin Promoter Suitability for Tissue-Specific Gene Delivery of Interleukin 12." In 1st World Congress on Electroporation and Pulsed Electric Fields in Biology, Medicine and Food & Environmental Technologies, 317–20. Singapore: Springer Singapore, 2016. http://dx.doi.org/10.1007/978-981-287-817-5_70.

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Stephens, Newman L., and He Jiang. "Velocity of translation of single actin filaments (AF) by myosin heads from antigen-sensitized airway smooth muscle." In The Cellular Basis of Cardiovascular Function in Health and Disease, 41–46. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5765-4_6.

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Thurston, Gavin, and Danielle Jean-Guillaume. "Methods for Visualizing Intact Blood Vessels Using Immunofluorescent Localization of PECAM (CD31) and α-Smooth Muscle Actin." In Methods in Endothelial Cell Biology, 337–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18725-4_30.

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Wunderlich, K., M. Knorr, H. J. Thiel, P. C. Dartsch, H. D. Weiss, and E. Betz. "Culture conditions induce the expression of smooth muscle α-actin in lens epithelial cells from the bovine eye." In Arteriosklerotische Gefäßerkrankungen, 435–41. Wiesbaden: Vieweg+Teubner Verlag, 1992. http://dx.doi.org/10.1007/978-3-663-19646-4_50.

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Kinner, B., J. Zaleskas, T. Freyman, K. P. Thon, and M. Spector. "Wachstumsfaktoren regulieren die Expression von Smooth Muscle Actin und die Kontraktilität humaner Chondrozyten in einer Kollagen-Glycosaminoglycan Matrix." In Chirurgisches Forum 2002, 457–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56158-0_117.

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Zevgolis, V. G., T. G. Sotiroudis, and A. E. Evangelopoulos. "Phosphorylase Kinase from Bovine Stomach Smooth Muscle: A Ca2+-Dependent Protein Kinase Associated with an Actin-Like Molecule." In Calcium Transport and Intracellular Calcium Homeostasis, 321–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-83977-1_30.

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Narani, N., P. D. Arora, A. Lew, L. Luo, M. Glogauer, B. Ganss, and C. A. G. McCulloch. "Transforming Growth Factor-β Induction of α-Smooth Muscle Actin Is Dependent on the Deformability of the Collagen Matrix." In Current Topics in Pathology, 47–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-58456-5_6.

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Conference papers on the topic "Apha Smooth Muscle Actin"

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Du, Y., and A. M. Al-Jumaily. "Smooth Muscle Stiffness Variation Due to External Oscillation." In ASME 2006 International Mechanical Engineering Congress and Exposition. ASMEDC, 2006. http://dx.doi.org/10.1115/imece2006-15795.

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The static and dynamic stiffnesses of contracted trachea smooth muscles are determined before, during and after length oscillations in isometric contraction. An appropriate Neural Network model is developed to normalize the data. The results indicate that the dynamic stiffness has the tendency of decreasing as the frequency and/or amplitude of external excitation increases. However, the static stiffness decreases with an increase in the frequency and amplitude of excitation until it reaches a critical value of frequency where no variation in stiffness is observed. It is postulated that the tissue elasticity and inertia are the main contributors to the dynamic stiffness while the myosin-actin cross bridge cycling is the main contributor to the static stiffness.
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MATSUI, TSUBASA S., SHINJI DEGUCHI, and MASAAKI SATO. "MICRO-VISCOELASTIC MEASUREMENT OF FLUORESCENTLY LABELED ACTIN BUNDLES ISOLATED FROM SMOOTH MUSCLE CELLS." In Proceedings of the Tohoku University Global Centre of Excellence Programme. IMPERIAL COLLEGE PRESS, 2012. http://dx.doi.org/10.1142/9781848169067_0014.

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Mbikou, P., and A. M. Al-Jumaily. "Effect of Mechanical Length Oscillations on Airways Smooth Muscle Reactivity and Crossbridge Cycling." In ASME 2011 International Mechanical Engineering Congress and Exposition. ASMEDC, 2011. http://dx.doi.org/10.1115/imece2011-63142.

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Superimposition of length fluctuations on contracted ASM have shown to reduce active force and stiffness. This effect is usually attributed to disruption of the actomyosin crossbridge cycle; however no direct experimental data is available to support this hypothesis. This in vitro study investigated the effect of the mechanical strains on 1) the ASM reactivity and 2) on the actin-myosin crossbridges. Experiments were carried out on maximally contracted bovine ASM subjected to length strains at various frequency in the range from 10 to 100Hz, superimposed on normal tidal stretches (frequency 0.33Hz, amplitude 4%). An organ bath system was used to apply strains and measure the force; immunofluorescence technique was performed to assess the crossbridges. The results show that superimposed length strains increase breathing relaxation effect with an optimal effect obtained at 50Hz. The cholinergic stimulation promotes actin-myosin connection, and length stretches promote the detachment of those crossbridges.
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Koopmans, Tim, Kuldeep Kumawat, Andrew Halayko, and Reinoud Gosens. "Regulation of actin dynamics by WNT-5A: Implications for human airway smooth muscle contraction." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa3986.

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Rohena-Rivera, Krizia, Maria M. Sanchez-Vazquez, Joseph Casillas-Gonzalez, Nemesis Merly, Mariela Perez-Quintana, and Magaly Martinez-Ferrer. "Abstract 1433: CCL4 alters migration and induces the expression of alpha smooth muscle actin." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1433.

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Janulaityte, Ieva, Andrius Januskevicius, Reinoud Gosens, Virginija Kalinauskaite-Zukauske, Rokas Stonkus, and Kestutis Malakauskas. "Eosinophils promote airway smooth muscle cells contractility and a-actin gene expression in asthma." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa970.

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Schroer, Alison K., and W. David Merryman. "Integrin-Focal Adhesion Coupling and Substrate Stiffness Affect Smooth Muscle Alpha Actin Expression in Fibroblasts." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80887.

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Fibroblast cells play a key role in producing and maintaining connective tissue throughout the body. The ability of these cells to differentiate into a more active myofibroblastic phenotype is important during development and wound healing, but prolonged myofibroblast activation can lead to overproduction of extracellular matrix proteins and stiffening of the surrounding tissue. This stiffening can cause heightened differentiation of neighboring fibroblast through force transduction pathways and can lead to detrimental fibrotic pathologies in many organ systems. Atherosclerosis, interstitial lung disease, cirrhosis and heart valve disease are fibrotic diseases that cause significant cost and mortality in our society. Understanding the processes by which cells sense and respond to substrate stiffness is crucial to the treatment of connective tissue diseases. One primary indicator of the myofibroblastic phenotype is the production of α smooth muscle actin (αSMA) bundles called stress fibers which help transmit stress inside the cell and increases the contractility of the cells and their surrounding tissue [1].
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Brook, Bindi S., and Oliver E. Jensen. "A Mechanistic Model For Disruption Of Actin-Myosin Connectivity In An Airway Smooth Muscle Cell." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1255.

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Mordon, Serge R., Alexandre Capon, Laurence Fleurisse, and Collette Creusy. "Granulation tissue exhibits differences in alpha-smooth muscle actin expression after laser-assisted skin closure (LASC)." In BiOS 2001 The International Symposium on Biomedical Optics, edited by R. Rox Anderson, Kenneth E. Bartels, Lawrence S. Bass, C. Gaelyn Garrett, Kenton W. Gregory, Abraham Katzir, Nikiforos Kollias, et al. SPIE, 2001. http://dx.doi.org/10.1117/12.427797.

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Dharmawan, Fredy Budhi, Sugeng Supriadi, Bambang Pontjo Priosoeryanto, and Benny Syariefsyah Latief. "Immunohistochemical response towards alpha smooth muscle actin post magnesium ECAP miniplate and screw implantation in bone tissue." In SECOND INTERNATIONAL CONFERENCE OF MATHEMATICS (SICME2019). Author(s), 2019. http://dx.doi.org/10.1063/1.5096682.

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Reports on the topic "Apha Smooth Muscle Actin"

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Broadley, Caroline, Debra A. Gonzalez, Rhada Nair, and Jeffrey M. Davidson. Canine Vocal Fold Fibroblasts in Culture: Expression of alpha-Smooth Muscle Actin and Modulation of Elastin Synthesis. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada302739.

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