Skip to main content
PMC home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1986 Sep;78(3):736–742. doi: 10.1172/JCI112634

Role of plasma gelsolin and the vitamin D-binding protein in clearing actin from the circulation.

S E Lind, D B Smith, P A Janmey, T P Stossel
PMCID: PMC423663  PMID: 3018044

Abstract

We determined the plasma kinetics of both actin and complexes of actin with the two high affinity actin-binding proteins of plasma, gelsolin, and vitamin D-binding protein (DBP). Actin is cleared rapidly from the plasma by the liver (half-disappearance time, 0.5 h). Using radiolabeled actin-binding proteins, we found that actin accelerated the clearance of both plasma gelsolin and the vitamin D-binding protein. In separate experiments we found that DBP-actin complexes were cleared more quickly than gelsolin-actin complexes, at a rate comparable to the clearance of actin from the blood. A low affinity interaction (dissociation constant, 2.9 X 10(-4) M) between actin and fibronectin was found, suggesting that little actin will bind to fibronectin in plasma. We conclude that while plasma gelsolin and DBP may both clear actin from the circulation, DBP appears to play a more important role. By so doing, DBP may conserve the filament-severing activity of plasma gelsolin.

Full text

PDF
736

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Carlson T. H., Atencio A. C., Simon T. L. In vivo behavior of radioiodinated rabbit antithrombin III. Demonstration of a noncirculating vascular compartment. J Clin Invest. 1984 Jul;74(1):191–199. doi: 10.1172/JCI111401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chaponnier C., Borgia R., Rungger-Brändle E., Weil R., Gabbiani G. An actin-destabilizing factor is present in human plasma. Experientia. 1979 Aug 15;35(8):1039–1041. doi: 10.1007/BF01949928. [DOI] [PubMed] [Google Scholar]
  3. Chaponnier C., Kohler L., Gabbiani G. Fixation of human anti-actin autoantibodies on skeletal muscle fibres. Clin Exp Immunol. 1977 Feb;27(2):278–284. [PMC free article] [PubMed] [Google Scholar]
  4. Chaponnier C., Patebex P., Gabbiani G. Human plasma actin-depolymerizing factor. Purification, biological activity and localization in leukocytes and platelets. Eur J Biochem. 1985 Jan 15;146(2):267–276. doi: 10.1111/j.1432-1033.1985.tb08649.x. [DOI] [PubMed] [Google Scholar]
  5. De Scheerder I., Vandekerckhove J., Robbrecht J., Algoed L., De Buyzere M., De Langhe J., De Schrijver G., Clement D. Post-cardiac injury syndrome and an increased humoral immune response against the major contractile proteins (actin and myosin). Am J Cardiol. 1985 Oct 1;56(10):631–633. doi: 10.1016/0002-9149(85)91024-0. [DOI] [PubMed] [Google Scholar]
  6. Dillon B. C., Estes J. E., Saba T. M., Blumenstock F. A., Cho E., Lee S. K., Lewis E. P. Actin-induced reticuloendothelial phagocytic depression as mediated by its interaction with fibronectin. Exp Mol Pathol. 1983 Apr;38(2):208–223. doi: 10.1016/0014-4800(83)90086-2. [DOI] [PubMed] [Google Scholar]
  7. Emerson D. L., Arnaud P., Galbraith R. M. Evidence of increased Gc:actin complexes in pregnant serum: a possible result of trophoblast embolism. Am J Reprod Immunol. 1983 Dec;4(4):185–189. doi: 10.1111/j.1600-0897.1983.tb00276.x. [DOI] [PubMed] [Google Scholar]
  8. Fechheimer M., Daiss J. L., Cebra J. J. Interaction of immunoglobulin with actin. Mol Immunol. 1979 Nov;16(11):881–888. doi: 10.1016/0161-5890(79)90086-5. [DOI] [PubMed] [Google Scholar]
  9. Glass C. K., Pittman R. C., Keller G. A., Steinberg D. Tissue sites of degradation of apoprotein A-I in the rat. J Biol Chem. 1983 Jun 10;258(11):7161–7167. [PubMed] [Google Scholar]
  10. Haddad J. G., Fraser D. R., Lawson D. E. Vitamin D plasma binding protein. Turnover and fate in the rabbit. J Clin Invest. 1981 May;67(5):1550–1560. doi: 10.1172/JCI110186. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Haddad J. G. Human serum binding protein for vitamin D and its metabolites (DBP): evidence that actin is the DBP binding component in human skeletal muscle. Arch Biochem Biophys. 1982 Feb;213(2):538–544. doi: 10.1016/0003-9861(82)90581-1. [DOI] [PubMed] [Google Scholar]
  12. Haddad J. G., Kowalski M. A., Sanger J. W. Actin affinity chromatography in the purification of human, avian and other mammalian plasma proteins binding vitamin D and its metabolites (Gc globulins). Biochem J. 1984 Mar 15;218(3):805–810. doi: 10.1042/bj2180805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Harris D. A., Schwartz J. H. Characterization of brevin, a serum protein that shortens actin filaments. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6798–6802. doi: 10.1073/pnas.78.11.6798. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Janmey P. A., Chaponnier C., Lind S. E., Zaner K. S., Stossel T. P., Yin H. L. Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking. Biochemistry. 1985 Jul 2;24(14):3714–3723. doi: 10.1021/bi00335a046. [DOI] [PubMed] [Google Scholar]
  15. Janmey P. A., Lind S. E., Yin H. L., Stossel T. P. Effects of semi-dilute actin solutions on the mobility of fibrin protofibrils during clot formation. Biochim Biophys Acta. 1985 Aug 16;841(2):151–158. doi: 10.1016/0304-4165(85)90016-9. [DOI] [PubMed] [Google Scholar]
  16. Janmey P. A., Stossel T. P., Lind S. E. Sequential binding of actin monomers to plasma gelsolin and its inhibition by vitamin D-binding protein. Biochem Biophys Res Commun. 1986 Apr 14;136(1):72–79. doi: 10.1016/0006-291x(86)90878-8. [DOI] [PubMed] [Google Scholar]
  17. Kawamura M., Maruyama K. Polymorphism of F-actin. I. Three forms of paracrystals. J Biochem. 1970 Dec;68(6):885–899. doi: 10.1093/oxfordjournals.jbchem.a129428. [DOI] [PubMed] [Google Scholar]
  18. Keski-Oja J., Sen A., Todaro G. J. Direct association of fibronectin and actin molecules in vitro. J Cell Biol. 1980 Jun;85(3):527–533. doi: 10.1083/jcb.85.3.527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Koteliansky V. E., Glukhova M. A., Morozkin A. D., Musatov A. P., Shirinsky V. P., Tskhovrebova L. A., Smirnov V. N. A study of actin-fibronectin interaction. FEBS Lett. 1981 Oct 12;133(1):31–35. doi: 10.1016/0014-5793(81)80464-4. [DOI] [PubMed] [Google Scholar]
  20. Kouyama T., Mihashi K. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem. 1981;114(1):33–38. [PubMed] [Google Scholar]
  21. Laki K., Muszbek L. On the interaction of F-actin with fibrin. Biochim Biophys Acta. 1974 Dec 18;371(2):519–525. doi: 10.1016/0005-2795(74)90048-8. [DOI] [PubMed] [Google Scholar]
  22. Lee W. M., Emerson D. L., Werner P. A., Arnaud P., Goldschmidt-Clermont P., Galbraith R. M. Decreased serum group-specific component protein levels and complexes with actin in fulminant hepatic necrosis. Hepatology. 1985 Mar-Apr;5(2):271–275. doi: 10.1002/hep.1840050220. [DOI] [PubMed] [Google Scholar]
  23. Lind S. E., Janmey P. A. Human plasma gelsolin binds to fibronectin. J Biol Chem. 1984 Nov 10;259(21):13262–13266. [PubMed] [Google Scholar]
  24. MATTHEWS C. M. The theory of tracer experiments with 131I-labelled plasma proteins. Phys Med Biol. 1957 Jul;2(1):36–53. doi: 10.1088/0031-9155/2/1/305. [DOI] [PubMed] [Google Scholar]
  25. Nishioka M., Kobayashi K., Uchida M., Nakamura T. A binding activity of actin with human C1q. Biochem Biophys Res Commun. 1982 Oct 15;108(3):1307–1312. doi: 10.1016/0006-291x(82)92142-8. [DOI] [PubMed] [Google Scholar]
  26. Norberg R., Thorstensson R., Utter G., Fagraeus A. F-Actin-depolymerizing activity of human serum. Eur J Biochem. 1979 Oct 15;100(2):575–583. doi: 10.1111/j.1432-1033.1979.tb04204.x. [DOI] [PubMed] [Google Scholar]
  27. Osborne J. C., Jr, Schaefer E. J., Powell G. M., Lee N. S., Zech L. A. Molecular properties of radioiodinated apolipoprotein A-I. J Biol Chem. 1984 Jan 10;259(1):347–353. [PubMed] [Google Scholar]
  28. Pittman R. C., Carew T. E., Glass C. K., Green S. R., Taylor C. A., Jr, Attie A. D. A radioiodinated, intracellularly trapped ligand for determining the sites of plasma protein degradation in vivo. Biochem J. 1983 Jun 15;212(3):791–800. doi: 10.1042/bj2120791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. 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]
  30. Stossel T. P. Contractile proteins in cell structure and function. Annu Rev Med. 1978;29:427–457. doi: 10.1146/annurev.me.29.020178.002235. [DOI] [PubMed] [Google Scholar]
  31. Stossel T. P. Contribution of actin to the structure of the cytoplasmic matrix. J Cell Biol. 1984 Jul;99(1 Pt 2):15s–21s. doi: 10.1083/jcb.99.1.15s. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Thorstensson R., Utter G., Norberg R. Further characterization of the Ca2+-dependent F-actin-depolymerizing protein of human serum. Eur J Biochem. 1982 Aug;126(1):11–16. doi: 10.1111/j.1432-1033.1982.tb06738.x. [DOI] [PubMed] [Google Scholar]
  33. Van Baelen H., Bouillon R., De Moor P. Vitamin D-binding protein (Gc-globulin) binds actin. J Biol Chem. 1980 Mar 25;255(6):2270–2272. [PubMed] [Google Scholar]
  34. Vuento M., Vaheri A. Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions. Biochem J. 1979 Nov 1;183(2):331–337. doi: 10.1042/bj1830331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Webster R. O., Larsen G. L., Henson P. M. In vivo clearance and tissue distribution of C5a and C5a des arginine complement fragments in rabbits. J Clin Invest. 1982 Dec;70(6):1177–1183. doi: 10.1172/JCI110716. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Yin H. L., Kwiatkowski D. J., Mole J. E., Cole F. S. Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin. J Biol Chem. 1984 Apr 25;259(8):5271–5276. [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES