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. 1979 Jul;37(3):705–709.

Reactivity of smooth-muscle antibodies with F- and G-actin.

P Andersen, J V Small, H K Andersen, A Sobieszek
PMCID: PMC1457738  PMID: 500125

Abstract

The reactivity of human smooth-muscle antibodies (SMA) with F- and G-actin was investigated by means of an enzyme-linked immunosorbent assay (ELISA). Polystyrene tubes were coated with F-actin, G-actin and tropomyosin. The optimal reactivity of SMA with F-actin was achieved with tubes coated with actin concentrations in the range of 10-100 mug/ml, while both lower and higher amounts yielded lower reactivity. The reactivity with G-actin was low and only a little higher than the reactivity with tropomyosin or uncoated tubes, but much lower than the reactivity with F-actin. The differences in reactivity of SMA with F- and G-actin could not be explained by differences in binding of the two forms of actin to the tubes, although 1.7-2.5 times more F-actin than G-actin bound to the polystyrene surface after coating with equivalent amounts of protein. SMA-negative sera did not react with F-actin coated tubes indicating that the binding of antibody was not due to non-immunological binding of immunoglobulins. Human SMA thus react better with F- than with G-actin.

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Selected References

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  1. Andersen P., Small J. V., Sobieszek A. Studies on the specificity of smooth-muscle antibodies. Clin Exp Immunol. 1976 Oct;26(1):57–66. [PMC free article] [PubMed] [Google Scholar]
  2. Bailey K. Tropomyosin: a new asymmetric protein component of the muscle fibril. Biochem J. 1948;43(2):271–279. doi: 10.1042/bj0430271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bray D., Thomas C. The actin content of fibroblasts. Biochem J. 1975 May;147(2):221–228. doi: 10.1042/bj1470221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Celis J. E., Small J. V., Andersen P., Celis A. Microfilament bundles in cultured cells. Correlation with anchorage independence and tumorigenicity in nude mice. Exp Cell Res. 1978 Jul;114(2):335–348. doi: 10.1016/0014-4827(78)90491-3. [DOI] [PubMed] [Google Scholar]
  5. Fagraeus A., Lidman K., Biberfeld G. Reaction of human smooth muscle antibodies with human blood lymphocytes and lymphoid cell lines. Nature. 1974 Nov 15;252(5480):246–247. doi: 10.1038/252246a0. [DOI] [PubMed] [Google Scholar]
  6. Gabbiani G., Ryan G. B., Lamelin J. P., Vassalli P., Majno G., Bouvier C. A., Cruchaud A., Lüscher E. F. Human smooth muscle autoantibody. Its identification as antiactin antibody and a study of its binding to "nonmuscular" cells. Am J Pathol. 1973 Sep;72(3):473–488. [PMC free article] [PubMed] [Google Scholar]
  7. Gabbiani G., Trenchev P., Holborow E. J. Increase of contractile proteins in human cancer cells. Lancet. 1975 Oct 25;2(7939):796–797. doi: 10.1016/s0140-6736(75)80008-0. [DOI] [PubMed] [Google Scholar]
  8. Goldman R. D., Lazarides E., Pollack R., Weber K. The distribution of actin in non-muscle cells. The use of actin antibody in the localization of actin within the microfilament bundles of mouse 3T3 cells. Exp Cell Res. 1975 Feb;90(2):333–344. doi: 10.1016/0014-4827(75)90323-7. [DOI] [PubMed] [Google Scholar]
  9. Johnson G. D., Holborow E. J., Glynn L. E. Antibody to smooth muscle in patients with liver disease. Lancet. 1965 Oct 30;2(7418):878–879. doi: 10.1016/s0140-6736(65)92505-5. [DOI] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Lidman K., Biberfeld G., Fagraeus A., Norberg R., Torstensson R., Utter G., Carlsson L., Luca J., Lindberg U. Anti-actin specificity of human smooth muscle antibodies in chronic active hepatitis. Clin Exp Immunol. 1976 May;24(2):266–272. [PMC free article] [PubMed] [Google Scholar]
  12. Norberg R., Biberfeld G., Fagraeus A., Lidman K., Thorstensson R., Utter G. The reaction of cells with anti-actin sera in relation to the amount of cellular actin. Clin Exp Immunol. 1977 Jun;28(3):512–516. [PMC free article] [PubMed] [Google Scholar]
  13. Sobieszek A., Bremel R. D. Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin. Eur J Biochem. 1975 Jun 16;55(1):49–60. doi: 10.1111/j.1432-1033.1975.tb02137.x. [DOI] [PubMed] [Google Scholar]
  14. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  15. Utter G., Biberfeld P., Norberg R., Thorstensson R., Fagraeus A. Ultrastructure of in vitro formed actin-anti-actin immune complexes. Exp Cell Res. 1978 Jun;114(1):127–133. doi: 10.1016/0014-4827(78)90044-7. [DOI] [PubMed] [Google Scholar]
  16. Voller A., Bidwell D. E., Bartlett A. Enzyme immunoassays in diagnostic medicine. Theory and practice. Bull World Health Organ. 1976;53(1):55–65. [PMC free article] [PubMed] [Google Scholar]

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