Studies on actin-actin and actin-myosin interaction

Bailin, Gary; Bárány, Michael

doi:10.1016/0005-2795(67)90461-8

Cited by 25 publications

(12 citation statements)

References 29 publications

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“…It can be assumed that the concentration needed for rigour developmenit is considerably lower than that needed for depression of contraction. Myosin ATPase activity (Blum, 1962), the F-actin/myosin interaction (Bailin & Barany, 1967) and the troponin-tropomyosin interaction (Yasui, Fuchs & Briggs, 1968) are all influenced by -SH inhibitors and are possible molecular sites of action of NEM associated with contractile depression.…”

Section: Discussionmentioning

confidence: 99%

Effects of sulphydryl inhibitors on frog sartorius muscle: N‐ethylmaleimide

Kirsten

Kuperman

1970

British J Pharmacology

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Summary . The characteristic action of the –SH inhibitor, N‐ethylmaleimide (NEM), is muscle rigour. The dose‐response curve indicates a biphasic effect with maximum rigour tension produced by 10 mm NEM; beyond 1.0 mm there was an inverse relationship between dose and response. . NEM produces a membrane depolarization unrelated to rigour development. . NEM causes a sustained increase in 45Ca efflux from whole muscle. Pretreatment of a muscle with ethylenediamine tetra‐acetic acid (EDTA, 5 mm) to remove membrane calcium does not alter the NEM induced 45Ca efflux. . It is suggested that the primary site of NEM action is inhibition of calcium uptake by the sarcoplasmic reticulum thereby producing rigour. At concentrations above 1.0 mm, NEM may affect the myofilaments.

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Section: Discussionmentioning

confidence: 99%

Effects of sulphydryl inhibitors on frog sartorius muscle: N‐ethylmaleimide

Kirsten

Kuperman

1970

British J Pharmacology

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“…The effects that particular Redox reagents have on actin varies considerably depending on which of these small molecules are bound and/or the presence of filamentous versus globular forms of actin. For example, while treatment with hydrogen peroxide and other oxidants greatly reduces the ability of Ca 2+ ‐bound G‐actin to polymerize [DalleDonne et al, ; Milzani et al, ; Milzani et al, ; Lassing et al, ; Hung et al, ], Mg 2+ ‐bound G‐actin is largely resistant to the adverse effects of hydrogen peroxide and related oxidants [Balin and Barany ; Muhlrad et al, ; Hung et al, ; Hung et al, ]. These differences appear to be due to changes in the conformation and surface exposed residues present when actin is polymerized in the presence of Ca 2+ versus Mg 2+ , and those residues that are exposed in G‐actin versus F‐actin [Lusty and Fasold ; Collins and Elzinga, ; Konno and Morales ; Lin et al, ; Dalle‐Donne et al, ; Guan et al, ; Guan et al, ; Lassing et al, ; Takamoto et al, ].…”

Section: Actin—a Target Of Redox Speciesmentioning

confidence: 99%

“…A and C; [reviewed in Terman and Kashina, ]. For example, oxidation of Cys‐374 often occurs in purified actin samples with air‐exposure, aging, and freeze‐thawing [Balin and Barany, ; Ishiwata, ; Xu et al, ; Tang et al, ] and this results in disulfide bond formation between two actin monomers [Ishiwata, ; Tang et al, ]. Reducing agents such as DTT reverse these effects and are added to purified actin samples to prevent this abnormal dimerization.…”

Section: Actin—redox Susceptible Residues and Redox Effectorsmentioning

confidence: 99%

Actin filaments—A target for redox regulation

et al. 2016

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Actin and its ability to polymerize into dynamic filaments is critical for the form and function of cells throughout the body. While multiple proteins have been characterized as affecting actin dynamics through non-covalent means, actin and its protein regulators are also susceptible to covalent modifications of their amino acid residues. In this regard, oxidation-reduction (Redox) intermediates have emerged as key modulators of the actin cytoskeleton with multiple different effects on cellular form and function. Here, we review work implicating Redox intermediates in post-translationally altering actin and discuss what is known regarding how these alterations affect the properties of actin. We also focus on two of the best characterized enzymatic sources of these Redox intermediates – the NADPH oxidase NOX and the flavoprotein monooxygenase MICAL – and detail how they have both been identified as altering actin, but share little similarity and employ different means to regulate actin dynamics. Finally, we discuss the role of these enzymes and redox signaling in regulating the actin cytoskeleton in vivo and highlight their importance for neuronal form and function in health and disease.

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“…Several lines of evidence suggested that the SHs are involved in the polymerization of G-actin (Katz and Mommaerts, 1962;Drabikowski and Gergely, 1963)) nucleotide binding (Strohman and Samorodin, 1962;Katz, 1963;Kuehl and Gergely, 1969), and myosin combination (Perry and Cotterill, 1964;Bailin and Barany, 1967). However, some papers reported that modification of two or three cysteine residues of actin with (2-aminoethy1)isothiouronium (Seraydarian et al, 1968), with an azo dye (Lusty and Fasold, 1969) or with iodoacetate or iodoacetamide (Bridgen, 1972) exhibited no effect on the ability of G-actin to polymerize and bind myosin, nucleotide, and calcium ion.…”

Section: Resultsmentioning

confidence: 99%

Effect of storage temperatures on the formation of disulfides and denaturation of milkfish myosin (Chanos chanos)

Chen¹,

Hwang²,

Jiang³

1989

J. Agric. Food Chem.

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soybean 11s globulin. Agric. Biol. Chem. 1977,41, 647-653. Pleitz, P.; Damaschun, G. The structure of the 11s seed globulins from various plant species: Comparative investigations by physical methods. Stud. Biophys. 1986,116, 153-173. Richarz, R.; Wuthrich, K. High-field 13C nuclear magnetic resonance studies at 90.5 MHz of the basic pancreatic trypsin inhibitor. Biochemistry 1978, 17, 2263-2269. Spitz, H. D. A new approach for sample preparation of protein hydrolyzates for amino acid analysis. Anal. Biochem. 1973, Staswick, P. E.; Hermodson, M. A.; Nielsen, N. C. Identification of the acidic and basic subunit complexes of glycinin. J. Biol. Chem. 1981,256, 8752-8755. Staswick, P. E.; Hermodson, M. A,; Nielsen, N. C. Identification of the cystines which link the acidic and basic components of the glycinin subunits. J. Biol. Chem. 1984,259, 13431-13435. Thanh, V. H.; Shibasaki, K. Major proteins of soybean seeds. A straightforward fractionation and characterization, J. Agric. Food Chem. 1976,24, 1117-1121. Utsumi, S.; Inaba, H.; Mori, T. Heterogeneity of soybean glycinin. Phytochemistry 1981, 20, 585-589. Van Binst, G.; Biesemans, M.; Barel, A. 0. Comparative carbon-13 nuclear magnetic resonance study at 67.9 MHz on lysozyme 56, 66-73. (Human and Egg-white) and a-lactalbumin (Human and Bovine) in their native and denatured state. Bull. SOC. Chim. Belg. Van Kleef, F. S. M. Thermally induced protein gelation: Gelation and rheological characterization of high concentrated ovalbumin and soybean protein gels. Biopolymers 1986, 25, 31-59. Vold, R. L.; Waugh, J. S.; Klein, M. P.; Phelps, D. E. Measurements of spin relaxation in complex systems. J. Chem. Phys. 1968, 48, 3831-3832. Wittebort, R. J.; Rothgeb, T. M.; Szabo, A.; Gurd, F. R. N.Aliphatic groups of sperm whale myoglobin: W-NMR study. Briggs, D. R. Studies on the cold-insoluble fraction of the water-extractable soybean proteins. 11. Factors influencing conformation changes in the 11s component. Arch.The effects of frozen storage temperatures on the formation of disulfides and the denaturation of myosin, extracted from milkfish (Chanos chanos) dorsal muscle, were investigated. The activities of Ca-ATPase and Mg(Ca)-ATPase and solubility in 0.6 M KCl decreased, and the total NaF3H4-soluble and -insoluble proteins increased a t a much higher rate a t -20 "C than at -35 "C. During freezing, the total SHs of samples a t -20 "C decreased significantly, but not a t -35 "C. The decreasing rate of total SHs a t -20 "C was significantly faster than a t -35 "C during storage.

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Studies on actin-actin and actin-myosin interaction

Cited by 25 publications

References 29 publications

Effects of sulphydryl inhibitors on frog sartorius muscle: N‐ethylmaleimide

Effects of sulphydryl inhibitors on frog sartorius muscle: N‐ethylmaleimide

Actin filaments—A target for redox regulation

Effect of storage temperatures on the formation of disulfides and denaturation of milkfish myosin (Chanos chanos)

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