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Gene Review

ACTA1  -  actin, alpha 1, skeletal muscle

Bos taurus

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Disease relevance of ACTA1

  • The energy-transducing NADH-ubiquinone (Q) oxidoreductase of Paracoccus denitrificans is composed of 14 dissimilar subunits and contains at least four iron-sulfur clusters [Yagi, T. (1993) Biochim. Biophys. Acta 1141, 1-17] [1].
  • Hypertension has been linked to opening of the blood-brain barrier and may be related to the expression of the smooth muscle alpha-actin gene in contractile cells at the brain microvasculature [2].
  • Immunological analysis with antibodies raised against NdhK from Synechocystis PCC 6803, a subunit of NDH-1, showed that NdhK in Anabaena PCC 7120 is only present on the plasma membrane, which confirms the results of previous studies [Howitt, C.A., Smith, G.D. & Day, D. A. (1993) Biochim. Biophys. Acta 114], 313-320] [3].
  • Effects of ADP-ribosylation of skeletal muscle alpha-actin by Clostridium perfringens iota toxin and by turkey erythrocyte ADP-ribosyltransferase A on profilin-regulated nucleotide exchange and ATPase activity were compared [4].

High impact information on ACTA1

  • The tendency of L-alpha-hydroxyacid oxidase B to self-associate in vitro (Philips, D.R., J.A. Duley, D.J. Fennell, and R.S. Holmes. 1976. Biochim. Biophys. Acta. 427:679-687) corresponds to the mode of association of cubical protomers to form the so-called marginal plates in renal peroxisomes [5].
  • Neither racemase has cofactors, but they contain essential cysteine residues [Yohda, M., Okada, H. & Kumagai, H. (1991) Biochim. Biophys. Acta 1089, 234-240] [6].
  • A cholate extract of the vesicles was treated with Pronase (1 mg/ml) for 10 min at 37 degrees C and reconstituted using a procedure similar to that described by Wakabayashi and Goshima [Wakabayashi, S. & Goshima, K. (1982) Biochim. Biophys. Acta 693, 125-133] [7].
  • Dd plastin interacted selectively with actin isoforms: it bound to D. discoideum actin and to beta/gamma-actin from bovine spleen but not to alpha-actin from rabbit skeletal muscle [8].
  • The antitumor drug aclacinomycin A was previously shown to inhibit the degradation of ubiquitinated proteins in rabbit reticulocyte lysates with an IC50 of 52 microM (Isoe, T., Naito, M., Shirai, A., Hirai, R., and Tsuruo, T.(1992) Biochim. Biophys. Acta 1117, 131-135) [9].

Biological context of ACTA1

  • Using a different model system mimicking protein-mediated membrane fusion during exocytosis (Bental, M., Lelkes, P.I., Scholma, J., Hoekstra, D., and Wilschut, J. (1984) Biochim. Biophys. Acta 774, 296-300) we found that exposure of chromaffin granules to a genuine metalloendoprotease, thermolysin, impaired their fusion competence with liposomes [10].
  • The kinetic model of Ragan & Cottingham [(1985) Biochim. Biophys. Acta 811, 13-31] for electron transport through a mobile pool of quinone predicts that, under certain conditions, the normal linear dependence of electron flow on the degree of reduction (or oxidation) of the quinone should no longer be found [11].
  • Fresh ECs and SMCs were enzymatically isolated, and their separation verified by immunofluorescent detection of alpha-actin and platelet/endothelium cell adhesion molecule (PECAM) proteins, respectively [12].
  • Collagen production was assayed with [(3)H]-proline incorporation, and SMC phenotype changes with confocal microscopy with a fluorescent alpha-actin antibody [13].
  • The data show that the X-ray structure is compatible with a catalytic mechanism in which all three F1-ATPase catalytic sites must fill with MgATP to initiate steady-state hydrolysis [e.g. Weber and Senior (1996) Biochim. Biophys. Acta 1275, 101-104] [14].

Anatomical context of ACTA1

  • The 10 S DNA polymerase alpha from calf thymus (Masaki, S., and Yoshida, S. (1978) Biochim. Biophys. Acta 521, 74-88) has been purified to near homogeneity [15].
  • Solubilization of basolateral membranes with 1% cholic acid in the presence of 2.5% soybean phospholipids and proteolytic treatment with Pronase (20 micrograms/ml) as described (Wakabayashi, S., and Goshima, K. (1982) Biochim. Biophys. Acta 693, 125-133) allowed partial purification and reconstitution of the Na+-Ca2+ exchange system into liposomes [16].
  • As reported previously [Ito, T., and Sato, H. (1984) Biochim. Biophys. Acta 800, 21-27], we found that D2O stimulates the formation of microtubules from tubulin [17].
  • We reported a rapid, light-stimulated release of calcium from isolated rod outer segments that is apparent only when both the disk membrane and the plasma membrane are made permeable to calcium by adding the ionophore A23187 [Kaupp, U. B., Schnetkamp, P. P. M., & Junge, W. (1979) Biochim. Biophys. Acta 552, 390-403] [18].
  • Differential expression of alpha-actin mRNA and immunoreactive protein in brain microvascular pericytes and smooth muscle cells [2].

Associations of ACTA1 with chemical compounds

  • TNP-Gpp(NH)p and other ribose-modified fluorescent analogs of GTP,3'-O-anthraniloyl-GTP and 3'-O-(N-methylanthraniloyl)-GTP (Hiratsuka, T. (1983) Biochim. Biophys. Acta 742, 496-508), also inhibited the enzymatic activity [19].
  • These findings cannot be reconciled with the tetrahedral Cu(II) model proposed by Greenaway, Chan, and Vincow ((1977) Biochim. Biophys. Acta 490, 62-78, 1977) to explain the unusual EPR spectrum of cytochrome oxidase [20].
  • Evidence for the presence of a functionally important vicinal dithiol in mitochondrial coupling factor B (FB) has been presented earlier (Sanadi, D. R. (1982) Biochim. Biophys. Acta 683, 39-56) [21].
  • (Kormann, A. W., Hurst, R. O., and Flynn, T. G. (1972) Biochim. Biophys. Acta 258, 40-55) for the purification of glycerol dehydrogenase, two enzymes have been purified from the skeletal muscle of male rabbits [22].
  • The molecular weight of this protein and its functional properties were similar to those of the alpha-ketoglutarate carrier isolated by a different method (Bisaccia, Indiveri, C., and Palmieri, F. (1985) Biochim. Biophys. Acta 810, 362-369) [23].

Other interactions of ACTA1


Analytical, diagnostic and therapeutic context of ACTA1


  1. Expression of the 25-kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans. Yano, T., Sled, V.D., Ohnishi, T., Yagi, T. Biochemistry (1994) [Pubmed]
  2. Differential expression of alpha-actin mRNA and immunoreactive protein in brain microvascular pericytes and smooth muscle cells. Boado, R.J., Pardridge, W.M. J. Neurosci. Res. (1994) [Pubmed]
  3. Cloning, analysis and inactivation of the ndhK gene encoding a subunit of NADH quinone oxidoreductase from Anabaena PCC 7120. Howitt, C.A., Whelan, J., Price, G.D., Day, D.A. Eur. J. Biochem. (1996) [Pubmed]
  4. ADP-ribosylation of actin by Clostridium perfringens iota toxin and turkey erythrocyte ADP-ribosyltransferase A: effects on profilin-regulated nucleotide exchange and ATPase activity. Sehr, P., Just, I., Aktories, K. Naunyn Schmiedebergs Arch. Pharmacol. (1996) [Pubmed]
  5. Purification of marginal plates from bovine renal peroxisomes: identification with L-alpha-hydroxyacid oxidase B. Zaar, K., Völkl, A., Fahimi, H.D. J. Cell Biol. (1991) [Pubmed]
  6. Bacterial glutamate racemase has high sequence similarity with myoglobins and forms an equimolar inactive complex with hemin. Choi, S.Y., Esaki, N., Ashiuchi, M., Yoshimura, T., Soda, K. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  7. Identification and partial purification of the cardiac sodium-calcium exchange protein. Hale, C.C., Slaughter, R.S., Ahrens, D.C., Reeves, J.P. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  8. Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes. Prassler, J., Stocker, S., Marriott, G., Heidecker, M., Kellermann, J., Gerisch, G. Mol. Biol. Cell (1997) [Pubmed]
  9. The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. Figueiredo-Pereira, M.E., Chen, W.E., Li, J., Johdo, O. J. Biol. Chem. (1996) [Pubmed]
  10. Oligopeptide inhibitors of metalloendoprotease activity inhibit catecholamine secretion from bovine adrenal chromaffin cells by modulating intracellular calcium homeostasis. Lelkes, P.I., Pollard, H.B. J. Biol. Chem. (1987) [Pubmed]
  11. The effect of rate limitation by cytochrome c on the redox state of the ubiquinone pool in reconstituted NADH: cytochrome c reductase. Reed, J.S., Ragan, C.I. Biochem. J. (1987) [Pubmed]
  12. Freshly isolated bovine coronary endothelial cells do not express the BK Ca channel gene. Gauthier, K.M., Liu, C., Popovic, A., Albarwani, S., Rusch, N.J. J. Physiol. (Lond.) (2002) [Pubmed]
  13. Gamma-irradiation modulates vascular smooth muscle cell and extracellular matrix function: Implications for neointimal development. Heckenkamp, J., Nigri, G.R., Waterman, P.R., Overhaus, M., Kossodo, S.C., Lamuraglia, G.M. J. Vasc. Surg. (2004) [Pubmed]
  14. Nucleotide occupancy of F1-ATPase catalytic sites under crystallization conditions. Löbau, S., Weber, J., Senior, A.E. FEBS Lett. (1997) [Pubmed]
  15. 10 S DNA polymerase alpha of calf thymus shows a microheterogeneity in its large polypeptide component. Masaki, S., Koiwai, O., Yoshida, S. J. Biol. Chem. (1982) [Pubmed]
  16. Partial purification and reconstitution of renal basolateral Na+-Ca2+ exchanger into liposomes. Talor, Z., Arruda, J.A. J. Biol. Chem. (1985) [Pubmed]
  17. Stabilization of tubulin by deuterium oxide. Chakrabarti, G., Kim, S., Gupta, M.L., Barton, J.S., Himes, R.H. Biochemistry (1999) [Pubmed]
  18. Rapid calcium release and proton uptake at the disk membrane of isolated cattle rod outer segments. 1. Stoichiometry of light-stimulated calcium release and proton uptake. Kaupp, U.B., Schnetkamp, P.P., Junge, W. Biochemistry (1981) [Pubmed]
  19. A chromophoric and fluorescent analog of GTP, 2',3'-O-(2,4,6-trinitrocyclohexadienylidene)-GTP, as a spectroscopic probe for the GTP inhibitory site of liver glutamate dehydrogenase. Hiratsuka, T. J. Biol. Chem. (1985) [Pubmed]
  20. Electron spin echo studies of cytochrome c oxidase. Mims, W.B., Peisach, J., Shaw, R.W., Beinert, H. J. Biol. Chem. (1980) [Pubmed]
  21. On the functional role of coupling factor B in the mitochondrial H+ -ATPase. Kantham, B.C., Hughes, J.B., Pringle, M.J., Sanadi, D.R. J. Biol. Chem. (1984) [Pubmed]
  22. Purification and characterization of two aldose reductase isoenzymes from rabbit muscle. Cromlish, J.A., Flynn, T.G. J. Biol. Chem. (1983) [Pubmed]
  23. Monocarboxylate and alpha-ketoglutarate carriers from bovine heart mitochondria. Purification by affinity chromatography on immobilized 2-cyano-4-hydroxycinnamate. Bolli, R., Nałecz, K.A., Azzi, A. J. Biol. Chem. (1989) [Pubmed]
  24. Development and initial characterization of a Bos taurus x B. gaurus interspecific hybrid backcross panel. Riggs, P.K., Owens, K.E., Rexroad, C.E., Amaral, M.E., Womack, J.E. J. Hered. (1997) [Pubmed]
  25. Cyr61 mediates the expression of VEGF, alphav-integrin, and alpha-actin genes through cytoskeletally based mechanotransduction mechanisms in bladder smooth muscle cells. Zhou, D., Herrick, D.J., Rosenbloom, J., Chaqour, B. J. Appl. Physiol. (2005) [Pubmed]
  26. Temporal change in skeletal muscle IGF-I mRNA abundance and nitrogen metabolism responses to abomasal casein infusion in steers. Moloney, A.P., Beermann, D.H., Gerrard, D., Robinson, T.F., Finnerty, K.D. J. Anim. Sci. (1998) [Pubmed]
  27. Sustained orbital shear stress stimulates smooth muscle cell proliferation via the extracellular signal-regulated protein kinase 1/2 pathway. Asada, H., Paszkowiak, J., Teso, D., Alvi, K., Thorisson, A., Frattini, J.C., Kudo, F.A., Sumpio, B.E., Dardik, A. J. Vasc. Surg. (2005) [Pubmed]
  28. Functional sorting of actin isoforms in microvascular pericytes. DeNofrio, D., Hoock, T.C., Herman, I.M. J. Cell Biol. (1989) [Pubmed]
  29. In vivo and mechanical properties of peritoneum/fascia as a novel arterial substitute. Sarac, T.P., Carnevale, K., Smedira, N., Tanquilut, E., Augustinos, P., Patel, A., Naska, T., Clair, D., Ouriel, K. J. Vasc. Surg. (2005) [Pubmed]
  30. Interaction between isolated cytochrome c1 and cytochrome c. Broger, C., Salardi, S., Azzi, A. Eur. J. Biochem. (1983) [Pubmed]
  31. A simple procedure to produce monospecific polyclonal antibodies of high affinity against actin from muscular sources. Polzar, B., Rösch, A., Mannherz, H.G. Eur. J. Cell Biol. (1989) [Pubmed]
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