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Journal articles on the topic 'Tropomyosins'

Author: Grafiati

Published: 4 June 2021

Last updated: 21 February 2023

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1

Papia, Francesco, Chiara Bellia, and Carina Gabriela Uasuf. "Tropomyosin: A panallergen that causes a worldwide allergic problem." Allergy and Asthma Proceedings 42, no. 5 (September 1, 2021): e145-e151. http://dx.doi.org/10.2500/aap.2021.42.210057.

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Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins. The highly heat-stable tropomyosins comprise the major allergens in crustaceans and mollusks, which make them important food allergens in exposed populations. Tropomyosins are responsible for a widespread immunoglobulin E cross-reactivity among allergens from different sources. Allergic tropomyosins are expressed in many species, including parasites and ins

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2

Fenderson, P. G., V. A. Fischetti, and M. W. Cunningham. "Tropomyosin shares immunologic epitopes with group A streptococcal M proteins." Journal of Immunology 142, no. 7 (April 1, 1989): 2475–81. http://dx.doi.org/10.4049/jimmunol.142.7.2475.

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Abstract Tropomyosin is an alpha-helical coiled-coil protein with structural similarities to the streptococcal M protein. In order to show serologic cross-reactivity between streptococcal M proteins and tropomyosin, we selected from a panel of murine mAb those which reacted with M proteins and tropomyosins in the ELISA. Western blots were used to study the reactions of each mAb with human and rabbit cardiac and rabbit skeletal tropomyosins. The antibodies were further characterized for their reactions with the additional autoantigens myosin, actin, keratin, and DNA. Five mAb were found which r

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3

Gunning, Peter, Geraldine O’neill, and Edna Hardeman. "Tropomyosin-Based Regulation of the Actin Cytoskeleton in Time and Space." Physiological Reviews 88, no. 1 (January 2008): 1–35. http://dx.doi.org/10.1152/physrev.00001.2007.

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Tropomyosins are rodlike coiled coil dimers that form continuous polymers along the major groove of most actin filaments. In striated muscle, tropomyosin regulates the actin-myosin interaction and, hence, contraction of muscle. Tropomyosin also contributes to most, if not all, functions of the actin cytoskeleton, and its role is essential for the viability of a wide range of organisms. The ability of tropomyosin to contribute to the many functions of the actin cytoskeleton is related to the temporal and spatial regulation of expression of tropomyosin isoforms. Qualitative and quantitative chan

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4

Asturias, Juan A., Nuria Gómez-Bayón, M. Carmen Arilla, Alberto Martínez, Ricardo Palacios, Fernando Sánchez-Gascón, and Jorge Martínez. "Molecular Characterization of American Cockroach Tropomyosin (Periplaneta americana Allergen 7), a Cross-Reactive Allergen." Journal of Immunology 162, no. 7 (April 1, 1999): 4342–48. http://dx.doi.org/10.4049/jimmunol.162.7.4342.

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Abstract Inhalation of allergens produced by the American cockroach (Periplaneta americana) induces IgE Ab production and the development of asthma in genetically predisposed individuals. The cloning and expression in Escherichia coli of P. americana tropomyosin allergen have been achieved. The protein shares high homology with other arthropod tropomyosins (80% identity) but less homology with vertebrate ones (50% identity). The recombinant allergen was produced in E. coli as a nonfusion protein with a yield of 9 mg/l of bacterial culture. Both natural and recombinant tropomyosins were purifie

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5

Humayun-Zakaria, Nada, Roland Arnold, Anshita Goel, Douglas Ward, Stuart Savill, and Richard Bryan. "Tropomyosins: Potential Biomarkers for Urothelial Bladder Cancer." International Journal of Molecular Sciences 20, no. 5 (March 4, 2019): 1102. http://dx.doi.org/10.3390/ijms20051102.

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Despite the incidence and prevalence of urothelial bladder cancer (UBC), few advances in treatment and diagnosis have been made in recent years. In this review, we discuss potential biomarker candidates: the tropomyosin family of genes, encoded by four loci in the human genome. The expression of these genes is tissue-specific. Tropomyosins are responsible for diverse cellular roles, most notably based upon their interplay with actin to maintain cellular processes, integrity and structure. Tropomyosins exhibit a large variety of splice forms, and altered isoform expression levels have been asso

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6

Shafique, Rubaba Hamid, Muhammad Inam, Muhammad Ismail, and Farhana Riaz Chaudhary. "Group 10 Allergens (Tropomyosins) from House-Dust Mites May Cause Covariation of Sensitization to Allergens from Other Invertebrates." Allergy & Rhinology 3, no. 2 (January 2012): ar.2012.3.0036. http://dx.doi.org/10.2500/ar.2012.3.0036.

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Group 10 allergens (tropomyosins) have been assumed to be a major cause of cross-reactivity between house-dust mites (HDMs) and other invertebrates. Despite all of the published data regarding the epidemiology, percent IgE binding and level of sensitization in the population, the role of tropomyosin as a cross-reactive allergen in patients with multiple allergy syndrome still remains to be elucidated. Homology between amino acid sequences reported in allergen databases of selected invertebrate tropomyosins was determined with Der f 10 as the reference allergen. The 66.9 and 54.4% identities we

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7

Goins, Lauren M., and R. Dyche Mullins. "A novel tropomyosin isoform functions at the mitotic spindle and Golgi in Drosophila." Molecular Biology of the Cell 26, no. 13 (July 2015): 2491–504. http://dx.doi.org/10.1091/mbc.e14-12-1619.

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Most eukaryotic cells express multiple isoforms of the actin-binding protein tropomyosin that help construct a variety of cytoskeletal networks. Only one nonmuscle tropomyosin (Tm1A) has previously been described in Drosophila, but developmental defects caused by insertion of P-elements near tropomyosin genes imply the existence of additional, nonmuscle isoforms. Using biochemical and molecular genetic approaches, we identified three tropomyosins expressed in Drosophila S2 cells: Tm1A, Tm1J, and Tm2A. The Tm1A isoform localizes to the cell cortex, lamellar actin networks, and the cleavage furr

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8

Anthony, D. T., R. J. Jacobs-Cohen, G. Marazzi, and L. L. Rubin. "A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors." Journal of Cell Biology 106, no. 5 (May 1, 1988): 1713–21. http://dx.doi.org/10.1083/jcb.106.5.1713.

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Muscle cells infected at the permissive temperature with temperature-sensitive mutants of Rous sarcoma virus and shifted to the non-permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269). Work described in this paper demonstrates that the virally-infected cells are missing a 37-kD peptide which reacts with an anti-tropomyosin antiserum. Using a monoclonal antibody specific for the missing peptide, we show that this tropomyosin is absent from fibroblasts and is dist

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9

Shanti, K. N., B. M. Martin, S. Nagpal, D. D. Metcalfe, and P. V. Rao. "Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes." Journal of Immunology 151, no. 10 (November 15, 1993): 5354–63. http://dx.doi.org/10.4049/jimmunol.151.10.5354.

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Abstract The major heat-stable shrimp allergen (designated as Sa-II), capable of provoking IgE-mediated immediate type hypersensitivity reactions after the ingestion of cooked shrimp, has been shown to be a 34-kDa heat-stable protein containing 300 amino acid residues. Here, we report that a comparison of amino acid sequences of different peptides generated by proteolysis of Sa-II revealed an 86% homology with tropomyosin from Drosophila melanogaster, suggesting that Sa-II could be the shrimp muscle protein tropomyosin. To establish that Sa-II is indeed tropomyosin, the latter was isolated fro

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10

Yamashiro-Matsumura, S., and F. Matsumura. "Characterization of 83-kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin." Journal of Cell Biology 106, no. 6 (June 1, 1988): 1973–83. http://dx.doi.org/10.1083/jcb.106.6.1973.

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Nonmuscle caldesmon purified from cultured rat cells shows a molecular weight of 83,000 on SDS gels, Stokes radius of 60.5 A, and sedimentation coefficient (S20,w) of 3.5 in the presence of reducing agents. These values give a native molecular weight of 87,000 and a frictional ratio of 2.04, suggesting that the molecule is a monomeric, asymmetric protein. In the absence of reducing agents, the protein is self-associated, through disulfide bonds, into oligomers with a molecular weight of 230,000 on SDS gels. These S-S oligomers appear to be responsible for the actin-bundling activity of nonmusc

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11

Bareja, Ilina, Hugo Wioland, Miro Janco, Philip R. Nicovich, Antoine Jégou, Guillaume Romet-Lemonne, James Walsh, and Till Böcking. "Dynamics of Tpm1.8 domains on actin filaments with single-molecule resolution." Molecular Biology of the Cell 31, no. 22 (October 15, 2020): 2452–62. http://dx.doi.org/10.1091/mbc.e19-10-0586.

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Characterization of the kinetics of Tpm1.8 binding to actin filaments with single-molecule resolution. This work provides molecular insight into actin–tropomyosin filament formation and the role of tropomyosins in regulating actin filament dynamics.

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12

Heeley, D. H., G. K. Dhoot, and S. V. Perry. "Factors determining the subunit composition of tropomyosin in mammalian skeletal muscle." Biochemical Journal 226, no. 2 (March 1, 1985): 461–68. http://dx.doi.org/10.1042/bj2260461.

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Adult rat fast-twitch skeletal muscle such as extensor digitorum longus contains alpha- and beta-tropomyosin subunits, as is the case in the corresponding muscles of rabbit. Adult rat soleus muscle contains beta-, gamma- and delta-tropomyosins, but no significant amounts of alpha-tropomyosin. Evidence for the presence of phosphorylated forms of at least three of the four tropomyosin subunit isoforms was obtained, particularly in developing muscle. Immediately after birth alpha- and beta-tropomyosins were the major components of skeletal muscle, in both fast-twitch and slow-twitch muscles. Diff

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13

Drees, B., C. Brown, B. G. Barrell, and A. Bretscher. "Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions." Journal of Cell Biology 128, no. 3 (February 1, 1995): 383–92. http://dx.doi.org/10.1083/jcb.128.3.383.

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Sequence analysis of chromosome IX of Saccharomyces cerevisiae revealed an open reading frame of 166 residues, designated TPM2, having 64.5% sequence identity to TPM1, that encodes the major form of tropomyosin in yeast. Purification and characterization of Tpm2p revealed a protein with the characteristics of a bona fide tropomyosin; it is present in vivo at about one sixth the abundance of Tpm1p. Biochemical and sequence analysis indicates that Tpm2p spans four actin monomers along a filament, whereas Tpmlp spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-

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14

Lin, J. J., D. M. Helfman, S. H. Hughes, and C. S. Chou. "Tropomyosin isoforms in chicken embryo fibroblasts: purification, characterization, and changes in Rous sarcoma virus-transformed cells." Journal of Cell Biology 100, no. 3 (March 1, 1985): 692–703. http://dx.doi.org/10.1083/jcb.100.3.692.

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Seven polypeptides (a, b, c, 1, 2, 3a, and 3b) have been previously identified as tropomyosin isoforms in chicken embryo fibroblasts (CEF) (Lin, J. J.-C., Matsumura, F., and Yamashiro-Matsumura, S., 1984, J. Cell. Biol., 98:116-127). Spots a and c had identical mobility on two-dimensional gels with the slow-migrating and fast-migrating components, respectively, of chicken gizzard tropomyosin. However, the remaining isoforms of CEF tropomyosin were distinct from chicken skeletal and cardiac tropomyosins on two-dimensional gels. The mixture of CEF tropomyosin has been isolated by the combination

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15

Jeong, Kyoung Yong, Jongweon Lee, In-Yong Lee, Han-Il Ree, Chein-Soo Hong, and Tai-Soon Yong. "Analysis of Amino Acid Sequence Variations and Immunoglobulin E-Binding Epitopes of German Cockroach Tropomyosin." Clinical Diagnostic Laboratory Immunology 11, no. 5 (September 2004): 874–78. http://dx.doi.org/10.1128/cdli.11.5.874-878.2004.

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ABSTRACT The allergenicities of tropomyosins from different organisms have been reported to vary. The cDNA encoding German cockroach tropomyosin (Bla g 7) was isolated, expressed, and characterized previously. In the present study, the amino acid sequence variations in German cockroach tropomyosin were analyzed in order to investigate its influence on allergenicity. We also undertook the identification of immunodominant peptides containing immunoglobulin E (IgE) epitopes which may facilitate the development of diagnostic and immunotherapeutic strategies based on the recombinant proteins. Two-d

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16

Gunning, Peter W., and Edna C. Hardeman. "Tropomyosins." Current Biology 27, no. 1 (January 2017): R8—R13. http://dx.doi.org/10.1016/j.cub.2016.11.033.

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MacLeod, A. R., and C. Gooding. "Human hTM alpha gene: expression in muscle and nonmuscle tissue." Molecular and Cellular Biology 8, no. 1 (January 1988): 433–40. http://dx.doi.org/10.1128/mcb.8.1.433-440.1988.

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We have isolated a cDNA clone from a human skeletal muscle library which contains the complete protein-coding sequence of a skeletal muscle alpha-tropomyosin. This cDNA sequence defines a fourth human tropomyosin gene, the hTM alpha gene, which is distinct from the hTMnm gene encoding a closely related isoform of skeletal muscle alpha-tropomyosin. In cultured human fibroblasts, the hTM alpha gene encodes both skeletal-muscle- and smooth-muscle-type alpha-tropomyosins by using an alternative mRNA-splicing mechanism.

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MacLeod, A. R., and C. Gooding. "Human hTM alpha gene: expression in muscle and nonmuscle tissue." Molecular and Cellular Biology 8, no. 1 (January 1988): 433–40. http://dx.doi.org/10.1128/mcb.8.1.433.

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We have isolated a cDNA clone from a human skeletal muscle library which contains the complete protein-coding sequence of a skeletal muscle alpha-tropomyosin. This cDNA sequence defines a fourth human tropomyosin gene, the hTM alpha gene, which is distinct from the hTMnm gene encoding a closely related isoform of skeletal muscle alpha-tropomyosin. In cultured human fibroblasts, the hTM alpha gene encodes both skeletal-muscle- and smooth-muscle-type alpha-tropomyosins by using an alternative mRNA-splicing mechanism.

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19

Schrock, Dillon C. "Tropomyosins are critical mediators of CD8+ T cell synaptic actomyosin organization." Journal of Immunology 206, no. 1_Supplement (May 1, 2021): 14.05. http://dx.doi.org/10.4049/jimmunol.206.supp.14.05.

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Abstract CD8+ T cells are a critical arm of the adaptive immune system because they kill virally-infected and transformed cells. Their function is critically dependent on their ability to form stable interactions with antigen-presenting cells (APCs). These interactions are mediated by a highly-organized structure at the T cell: APC interface termed the immunological synapse (IS). The IS itself is organized largely by the underlying actin cytoskeleton. Perturbation of either the Arp2/3-dependent branched network of the distal region or of the formin-derived arc network of the peripheral region

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Galán-Freyle, Nataly, Jesús Olivero-Verbel, and Liney Díaz-López. "Modeling of allergen proteins found in sea food products." Food Science and Technology 32, no. 2 (March 20, 2012): 393–400. http://dx.doi.org/10.1590/s0101-20612012005000032.

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Shellfish are a source of food allergens, and their consumption is the cause of severe allergic reactions in humans. Tropomyosins, a family of muscle proteins, have been identified as the major allergens in shellfish and mollusks species. Nevertheless, few experimentally determined three-dimensional structures are available in the Protein Data Base (PDB). In this study, 3D models of several homologous of tropomyosins present in marine shellfish and mollusk species (Chaf 1, Met e1, Hom a1, Per v1, and Pen a1) were constructed, validated, and their immunoglobulin E binding epitopes were identifi

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Bakin, Andrei V., Alfiya Safina, Cammie Rinehart, Cecilia Daroqui, Huferesh Darbary та David M. Helfman. "A Critical Role of Tropomyosins in TGF-β Regulation of the Actin Cytoskeleton and Cell Motility in Epithelial Cells". Molecular Biology of the Cell 15, № 10 (жовтень 2004): 4682–94. http://dx.doi.org/10.1091/mbc.e04-04-0353.

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We have investigated transforming growth factor beta (TGF-β)–mediated induction of actin stress fibers in normal and metastatic epithelial cells. We found that stress fiber formation requires de novo protein synthesis, p38Mapk and Smad signaling. We show that TGF-β via Smad and p38Mapk up-regulates expression of actin-binding proteins including high-molecular-weight tropomyosins, α-actinin and calponin h2. We demonstrate that, among these proteins, tropomyosins are both necessary and sufficient for TGF-β induction of stress fibers. Silencing of tropomyosins with short interfering RNAs (siRNAs)

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Mokronosova, Marina A., and Tatiana M. Zheltikova. "Clinical and immunological characteristics of sensitization to tropomyosins." Russian Journal of Allergy 18, no. 1 (March 15, 2021): 73–78. http://dx.doi.org/10.36691/rja1399.

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Tropomyosins are a family of allergenic proteins found in large quantities in all invertebrates. Tropomyosins sensitization causes a life-threatening allergic reaction up to anaphylaxis after eating seafood. Identifying the source of primary sensitization is important to predict the allergic reaction severity. This article describes a clinical case of chronic recurrent urticaria in an 8-year-old boy with tropomyosins sensitization. An 8-year-old boy was diagnosed with the following: controlled atopic phenotype bronchial asthma, food allergy (oral allergy syndrome), and chronic recurrent

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Kreuz, A. J., A. Simcox, and D. Maughan. "Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants." Journal of Cell Biology 135, no. 3 (November 1, 1996): 673–87. http://dx.doi.org/10.1083/jcb.135.3.673.

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Drosophila indirect flight muscle (IFM) contains two different types of tropomyosin: a standard 284-amino acid muscle tropomyosin, Ifm-TmI, encoded by the TmI gene, and two &gt; 400 amino acid tropomyosins, TnH-33 and TnH-34, encoded by TmII. The two IFM-specific TnH isoforms are unique tropomyosins with a COOH-terminal extension of approximately 200 residues which is hydrophobic and rich in prolines. Previous analysis of a hypomorphic TmI mutant, Ifm(3)3, demonstrated that Ifm-TmI is necessary for proper myofibrillar assembly, but no null TmI mutant or TmII mutant which affects the TnH is

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Cooper, H. L., N. Feuerstein, M. Noda, and R. H. Bassin. "Suppression of tropomyosin synthesis, a common biochemical feature of oncogenesis by structurally diverse retroviral oncogenes." Molecular and Cellular Biology 5, no. 5 (May 1985): 972–83. http://dx.doi.org/10.1128/mcb.5.5.972-983.1985.

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To identify proteins whose production may be altered as a common event in the expression of structurally diverse oncogenes, we compared two-dimensional electropherograms of newly synthesized proteins from NIH/3T3 cell lines transformed by a variety of retroviral oncogenes, from cellular revertant lines, and from a line (433.3) which expresses the v-ras oncogene in response to corticosteroids. Most alterations in the synthesis of specific proteins detected by this approach appeared to be the result of selection during prolonged cultivation and were probably unrelated to the transformation proce

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Cooper, H. L., N. Feuerstein, M. Noda, and R. H. Bassin. "Suppression of tropomyosin synthesis, a common biochemical feature of oncogenesis by structurally diverse retroviral oncogenes." Molecular and Cellular Biology 5, no. 5 (May 1985): 972–83. http://dx.doi.org/10.1128/mcb.5.5.972.

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To identify proteins whose production may be altered as a common event in the expression of structurally diverse oncogenes, we compared two-dimensional electropherograms of newly synthesized proteins from NIH/3T3 cell lines transformed by a variety of retroviral oncogenes, from cellular revertant lines, and from a line (433.3) which expresses the v-ras oncogene in response to corticosteroids. Most alterations in the synthesis of specific proteins detected by this approach appeared to be the result of selection during prolonged cultivation and were probably unrelated to the transformation proce

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Palani, Saravanan, Darius V. Köster, Tomoyuki Hatano, Anton Kamnev, Taishi Kanamaru, Holly R. Brooker, Juan Ramon Hernandez-Fernaud, et al. "Phosphoregulation of tropomyosin is crucial for actin cable turnover and division site placement." Journal of Cell Biology 218, no. 11 (October 9, 2019): 3548–59. http://dx.doi.org/10.1083/jcb.201809089.

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Tropomyosin is a coiled-coil actin binding protein key to the stability of actin filaments. In muscle cells, tropomyosin is subject to calcium regulation, but its regulation in nonmuscle cells is not understood. Here, we provide evidence that the fission yeast tropomyosin, Cdc8, is regulated by phosphorylation of a serine residue. Failure of phosphorylation leads to an increased number and stability of actin cables and causes misplacement of the division site in certain genetic backgrounds. Phosphorylation of Cdc8 weakens its interaction with actin filaments. Furthermore, we show through in vi

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Gunning, P. W., V. Ferguson, K. J. Brennan, and E. C. Hardeman. "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle." Journal of Cell Science 114, no. 3 (February 1, 2001): 513–24. http://dx.doi.org/10.1242/jcs.114.3.513.

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Muscle differentiation is characterized by the induction of genes encoding contractile structural proteins and the repression of nonmuscle isoforms from these gene families. We have examined the importance of this regulated order of gene expression by expressing the two sarcomeric muscle actins characteristic of the differentiated state, i.e. alpha-skeletal and alpha-cardiac actin, in C2 mouse myoblasts. Precocious accumulation of transcripts and proteins for a group of differentiation-specific genes was elicited by alpha-skeletal actin only: four muscle tropomyosins, two muscle actins, desmin

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Watakabe, A., R. Kobayashi, and D. M. Helfman. "N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin." Journal of Cell Science 109, no. 9 (September 1, 1996): 2299–310. http://dx.doi.org/10.1242/jcs.109.9.2299.

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We have identified and characterized two proteins in rat brain that bind to the neuron-specific tropomyosin isoform, TMBr3. The two proteins were identified by blot overlay assay, in which the proteins immobilized on the membrane were probed by epitope-tagged TMBr3, followed by detection with anti-epitope antibody. We have purified these proteins using a TMBr3 affinity column. Peptide sequencing as well as immunoblotting showed that one of the two proteins is identical to tropomodulin, a tropomyosin-binding protein originally identified in erythrocytes. The cDNA for the other protein was clone

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González-Fernández, Juan, Beatriz Veleiro, Alvaro Daschner, and Carmen Cuéllar. "Are fish tropomyosins allergens?" Annals of Allergy, Asthma & Immunology 116, no. 1 (January 2016): 74–76. http://dx.doi.org/10.1016/j.anai.2015.09.017.

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Hu, Shiqiong, Hanna Grobe, Zhenhuan Guo, Yu-Hsiu Wang, Bryant L. Doss, Meng Pan, Benoit Ladoux, Alexander D. Bershadsky, and Ronen Zaidel-Bar. "Reciprocal regulation of actomyosin organization and contractility in nonmuscle cells by tropomyosins and alpha-actinins." Molecular Biology of the Cell 30, no. 16 (July 22, 2019): 2025–36. http://dx.doi.org/10.1091/mbc.e19-02-0082.

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Contractile arrays of actin and myosin II filaments drive many essential processes in nonmuscle cells, including migration and adhesion. Sequential organization of actin and myosin along one dimension is followed by expansion into a two-dimensional network of parallel actomyosin fibers, in which myosin filaments are aligned to form stacks. The process of stack formation has been studied in detail. However, factors that oppose myosin stack formation have not yet been described. Here, we show that tropomyosins act as negative regulators of myosin stack formation. Knockdown of any or all tropomyo

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Had, L., C. Faivre-Sarrailh, C. Legrand, J. Mery, J. Brugidou, and A. Rabie. "Tropomyosin isoforms in rat neurons: the different developmental profiles and distributions of TM-4 and TMBr-3 are consistent with different functions." Journal of Cell Science 107, no. 10 (October 1, 1994): 2961–73. http://dx.doi.org/10.1242/jcs.107.10.2961.

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Antipeptide antisera specific for TM-4 and TMBr-3, the two tropomyosin isoforms in neurons, were used to investigate the concentrations and distributions of these F-actin-binding proteins in neurons in vitro and in vivo. TM-4 and TMBr-3 tropomyosins had different developmental profiles. TM-4 was found mainly in immature stages, while the concentration of TMBr-3 increased with maturation. The two isoforms also had different subcellular distributions. TM-4 was concentrated in the growth cones of cultured neurons and, in vivo, in areas where neurites were growing. Later, when development was comp

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Borovikov, Yurii, Olga Karpicheva, Armen Simonyan, Stanislava Avrova, Elena Rogozovets, Vladimir Sirenko, and Charles Redwood. "The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies." International Journal of Molecular Sciences 19, no. 12 (December 10, 2018): 3975. http://dx.doi.org/10.3390/ijms19123975.

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Point mutations in genes encoding isoforms of skeletal muscle tropomyosin may cause nemaline myopathy, cap myopathy (Cap), congenital fiber-type disproportion (CFTD), and distal arthrogryposis. The molecular mechanisms of muscle dysfunction in these diseases remain unclear. We studied the effect of the E173A, R90P, E150A, and A155T myopathy-causing substitutions in γ-tropomyosin (Tpm3.12) on the position of tropomyosin in thin filaments, and the conformational state of actin monomers and myosin heads at different stages of the ATPase cycle using polarized fluorescence microscopy. The E173A, R9

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Palani, Saravanan, Darius Koester, and Mohan K. Balasubramanian. "Phosphoregulation of tropomyosin-actin interaction revealed using a genetic code expansion strategy." Wellcome Open Research 5 (July 7, 2020): 161. http://dx.doi.org/10.12688/wellcomeopenres.16082.1.

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Tropomyosins are coiled-coil proteins that regulate the stability and / or function of actin cytoskeleton in muscle and non-muscle cells through direct binding of actin filaments. Recently, using the fission yeast, we discovered a new mechanism by which phosphorylation of serine 125 of tropomyosin (Cdc8), reduced its affinity for actin filaments thereby providing access for the actin severing protein Adf1/Cofilin to actin filaments causing instability of actin filaments. Here we use a genetic code expansion strategy to directly examine this conclusion. We produced in Escherichia coli Cdc8-trop

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Weinberger, R. P., R. C. Henke, O. Tolhurst, P. L. Jeffrey, and P. Gunning. "Induction of neuron-specific tropomyosin mRNAs by nerve growth factor is dependent on morphological differentiation." Journal of Cell Biology 120, no. 1 (January 1, 1993): 205–15. http://dx.doi.org/10.1083/jcb.120.1.205.

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We have examined the expression of brain-specific tropomyosins during neuronal differentiation. Both TmBr-1 and TmBr-3 were shown to be neuron specific. TmBr-1 and TmBr-3 mRNA levels increased during the most active phase of neurite outgrowth in the developing rat cerebellum. In PC12 cells stimulated by nerve growth factor (NGF) to differentiate to the neuronal phenotype, TmBr-1 and TmBr-3 levels increased with an increasing degree of morphological differentiation. Induction of TmBr-1 and TmBr-3 expression only occurred under conditions where PC12 cells were permitted to extend neurites. NGF w

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Suma, Yota, Shoichiro Ishizaki, Yuji Nagashima, Ying Lu, Hideki Ushio, and Kazuo Shiomi. "Comparative analysis of barnacle tropomyosin: Divergence from decapod tropomyosins and role as a potential allergen." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 147, no. 2 (June 2007): 230–36. http://dx.doi.org/10.1016/j.cbpb.2007.01.004.

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Yong Jeong, Kyoung, Chein-Soo Hong, and Tai-Soon Yong. "Allergenic Tropomyosins and Their Cross-Reactivities." Protein & Peptide Letters 13, no. 8 (August 1, 2006): 835–45. http://dx.doi.org/10.2174/092986606777841244.

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Arruda, L. Karla. "The Right Timing for Shrimp Tropomyosins." International Archives of Allergy and Immunology 160, no. 4 (November 21, 2012): 331–33. http://dx.doi.org/10.1159/000345363.

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Ferraz, Conchita, Joannes Sri Widada, and Jean-Pierre Liautard. "Purification and characterization of recombinant tropomyosins." Journal of Chromatography A 539, no. 2 (January 1991): 465–73. http://dx.doi.org/10.1016/s0021-9673(01)83956-x.

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Vejborg, R. M., N. Bernbom, L. Gram, and P. Klemm. "Anti-adhesive properties of fish tropomyosins." Journal of Applied Microbiology 105, no. 1 (July 2008): 141–50. http://dx.doi.org/10.1111/j.1365-2672.2007.03718.x.

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Swenson, Charles A., and Nancy C. Stellwagen. "Flexibility of smooth and skletal tropomyosins." Biopolymers 28, no. 5 (May 1989): 955–63. http://dx.doi.org/10.1002/bip.360280504.

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NOVY, R., L. LIU, C. LIN, D. HELFMAN, and J. LIN. "Expression of smooth muscle and nonmuscle tropomyosins in Escherichia coli and characterization of bacterially produced tropomyosins." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1162, no. 3 (March 26, 1993): 255–65. http://dx.doi.org/10.1016/0167-4838(93)90289-4.

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Jeong, Kyoung Yong, Heeyu Hwang, Jongweon Lee, In-Yong Lee, Dong Soo Kim, Chein-Soo Hong, Han-Il Ree, and Tai-Soon Yong. "Allergenic Characterization of Tropomyosin from the Dusky Brown Cockroach, Periplaneta fuliginosa." Clinical Diagnostic Laboratory Immunology 11, no. 4 (July 2004): 680–85. http://dx.doi.org/10.1128/cdli.11.4.680-685.2004.

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ABSTRACTHousehold arthropods are one of the most common causes of allergic diseases. Four species of cockroaches are found to reside in Korean homes, but published work deals almost exclusively with the German and American cockroaches. This study was undertaken to investigate the cross-reactive allergenic components of the dusky brown cockroach,Periplaneta fuliginosa. Enzyme-linked immunosorbent assay (ELISA) inhibition and immunoblot analyses for the dusky brown cockroach were performed withBlattella germanicaandDermatophagoides farinaeallergic sera. cDNA encoding tropomyosin, which is a well

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Côté, A., J. P. Doucet, and J. M. Trifaró. "Adrenal Medullary Tropomyosins: Purification and Biochemical Characterization." Journal of Neurochemistry 46, no. 6 (October 5, 2006): 1771–82. http://dx.doi.org/10.1111/j.1471-4159.1986.tb08495.x.

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Fath, Thomas. "Tropomodulins and tropomyosins – organizers of cellular microcompartments." BioMolecular Concepts 4, no. 1 (February 1, 2013): 89–101. http://dx.doi.org/10.1515/bmc-2012-0037.

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AbstractEukaryotic cells show a remarkable compartmentalization into compartments such as the cell nucleus, the Golgi apparatus, the endoplasmic reticulum, and endosomes. However, organelle structures are not the only means by which specialized compartments are formed. Recent research shows a critical role for diverse actin filament populations in defining functional compartments, here referred to as microcompartments, in a wide range of cells. These microcompartments are involved in regulating fundamental cellular functions including cell motility, plasma membrane organization, and cellular m

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Araya, Esteban, Christine Berthier, Edward Kim, Trevor Yeung, Xiaorong Wang, and David M. Helfman. "Regulation of Coiled-Coil Assembly in Tropomyosins." Journal of Structural Biology 137, no. 1-2 (January 2002): 176–83. http://dx.doi.org/10.1006/jsbi.2002.4463.

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Colpan, Mert, Natalia A. Moroz, and Alla S. Kostyukova. "Tropomodulins and tropomyosins: working as a team." Journal of Muscle Research and Cell Motility 34, no. 3-4 (July 5, 2013): 247–60. http://dx.doi.org/10.1007/s10974-013-9349-6.

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Jeong, Kyoung Yong, Hye-Yung Yum, In-Yong Lee, Han-Il Ree, Chein-Soo Hong, Dong Soo Kim, and Tai-Soon Yong. "Molecular Cloning and Characterization of Tropomyosin, a Major Allergen of Chironomus kiiensis, a Dominant Species of Nonbiting Midges in Korea." Clinical Diagnostic Laboratory Immunology 11, no. 2 (March 2004): 320–24. http://dx.doi.org/10.1128/cdli.11.2.320-324.2004.

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ABSTRACT Chironomids are widely and abundantly distributed in the vicinity of standing waters. Larvae of Chironomus and some other genera are known to contain hemoglobins, which have been described as a major allergen, and the adults that have no hemoglobins also have been reported to contain allergens. In this study, we tried to establish the role of chironomid allergy and characterize the allergen of Chironomus kiiensis adults. Skin tests using C. kiiensis adult extracts were performed on patients with allergic symptoms. A cDNA library of C. kiiensis adults was screened with C. kiiensis immu

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Bach, Cuc T. T., Sarah Creed, Jessie Zhong, Maha Mahmassani, Galina Schevzov, Justine Stehn, Lauren N. Cowell, et al. "Tropomyosin Isoform Expression Regulates the Transition of Adhesions To Determine Cell Speed and Direction." Molecular and Cellular Biology 29, no. 6 (January 5, 2009): 1506–14. http://dx.doi.org/10.1128/mcb.00857-08.

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ABSTRACT The balance of transition between distinct adhesion types contributes to the regulation of mesenchymal cell migration, and the characteristic association of adhesions with actin filaments led us to question the role of actin filament-associating proteins in the transition between adhesive states. Tropomyosin isoform association with actin filaments imparts distinct filament structures, and we have thus investigated the role for tropomyosins in determining the formation of distinct adhesion structures. Using combinations of overexpression, knockdown, and knockout approaches, we establi

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Robaszkiewicz, Katarzyna, Małgorzata Śliwinska, and Joanna Moraczewska. "Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin." International Journal of Molecular Sciences 21, no. 12 (June 16, 2020): 4285. http://dx.doi.org/10.3390/ijms21124285.

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In striated muscle the extent of the overlap between actin and myosin filaments contributes to the development of force. In slow twitch muscle fibers actin filaments are longer than in fast twitch fibers, but the mechanism which determines this difference is not well understood. We hypothesized that tropomyosin isoforms Tpm1.1 and Tpm3.12, the actin regulatory proteins, which are specific respectively for fast and slow muscle fibers, differently stabilize actin filaments and regulate severing of the filaments by cofilin-2. Using in vitro assays, we showed that Tpm3.12 bound to F-actin with alm

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Drees, B. "Distinct and essential functions of tropomyosins in yeast." Trends in Cell Biology 5, no. 5 (May 1995): 195. http://dx.doi.org/10.1016/s0962-8924(00)88996-5.

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