Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1982 Jan;79(2):432–435. doi: 10.1073/pnas.79.2.432

alpha-Actinin and membrane glycoprotein IIIa are different proteins in human blood platelets.

B G Langer, L L Leung, P A Gonnella, V T Nachmias, R L Nachman, F A Pepe
PMCID: PMC345757  PMID: 6176993

Abstract

It has been suggested that a platelet protein that is very similar to muscle alpha-actinin is identical to the membrane glycoprotein IIIa (GPIIIa) of platelets and is responsible for anchoring actin filaments directly into the plasma membrane of platelets. To determine if alpha-actinin and GPIIIa are related in platelets, we analyzed the purified proteins on 5% sodium dodecyl sulfate/polyacrylamide gels. The two proteins differ in mobility in both the unreduced and reduced states, and they stain differently with silver stain. In addition, alpha-actinin is a prominent component of the detergent-insoluble cytoskeletons of platelets, whereas GPIIIa is absent from these structures. By using monospecific antisera to the individual proteins, it was demonstrated that alpha-actinin and GPIIIa are immunologically distinct. We conclude that alpha-actinin and GPIIIa are different proteins in human blood platelets and that it is unlikely that alpha-actinin is an integral membrane protein.

Full text

PDF
432

Images in this article

433Image
on p.433
434Image
on p.434

Selected References

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

  1. Bretscher A., Weber K. Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy. J Cell Biol. 1978 Dec;79(3):839–845. doi: 10.1083/jcb.79.3.839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Burridge K., Feramisco J. R. Microinjection and localization of a 130K protein in living fibroblasts: a relationship to actin and fibronectin. Cell. 1980 Mar;19(3):587–595. doi: 10.1016/s0092-8674(80)80035-3. [DOI] [PubMed] [Google Scholar]
  3. Craig S. W., Lancashire C. L. Comparison of intestinal brush-border 95-Kdalton polypeptide and alpha-actinins. J Cell Biol. 1980 Mar;84(3):655–667. doi: 10.1083/jcb.84.3.655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Feramisco J. R. Microinjection of fluorescently labeled alpha-actinin into living fibroblasts. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3967–3971. doi: 10.1073/pnas.76.8.3967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Geiger B. A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell. 1979 Sep;18(1):193–205. doi: 10.1016/0092-8674(79)90368-4. [DOI] [PubMed] [Google Scholar]
  6. Gerrard J. M., Schollmeyer J. V., Phillips D. R., White J. G. alpha-Actinin deficiency in thrombasthenia: possible identity of alpha-actinin and glycoprotein III. Am J Pathol. 1979 Mar;94(3):509–528. [PMC free article] [PubMed] [Google Scholar]
  7. Gonnella P. A., Nachmias V. T. Platelet activation and microfilament bundling. J Cell Biol. 1981 Apr;89(1):146–151. doi: 10.1083/jcb.89.1.146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Holmes G. R., Goll D. E., Suzuki A. Effect of -actinin on actin viscosity. Biochim Biophys Acta. 1971 Nov 2;253(1):240–253. doi: 10.1016/0005-2728(71)90250-7. [DOI] [PubMed] [Google Scholar]
  9. Jockusch B. M., Burger M. M., DaPrada M., Richards J. G., Chaponnier C., Gabbiani G. alpha-Actinin attached to membranes of secretory vesicles. Nature. 1977 Dec 15;270(5638):628–629. doi: 10.1038/270628a0. [DOI] [PubMed] [Google Scholar]
  10. Kawamura M., Masaki T., Nonomura Y., Maruyama K. An electron microscopic study of the action of the 6S component of alpha-actinin on F-actin. J Biochem. 1970 Oct;68(4):577–580. doi: 10.1093/oxfordjournals.jbchem.a129388. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Langer B. G., Pepe F. A. New, rapid methods for purifying alpha-actinin from chicken gizzard and chicken pectoral muscle. J Biol Chem. 1980 Jun 10;255(11):5429–5434. [PubMed] [Google Scholar]
  13. Lazarides E., Burridge K. Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell. 1975 Nov;6(3):289–298. doi: 10.1016/0092-8674(75)90180-4. [DOI] [PubMed] [Google Scholar]
  14. Leung L. L., Kinoshita T., Nachman R. L. Isolation, purification, and partial characterization of platelet membrane glycoproteins IIb and IIIa. J Biol Chem. 1981 Feb 25;256(4):1994–1997. [PubMed] [Google Scholar]
  15. McEver R. P., Baenziger N. L., Majerus P. W. Isolation and quantitation of the platelet membrane glycoprotein deficient in thrombasthenia using a monoclonal hybridoma antibody. J Clin Invest. 1980 Dec;66(6):1311–1318. doi: 10.1172/JCI109983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Merril C. R., Goldman D., Sedman S. A., Ebert M. H. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science. 1981 Mar 27;211(4489):1437–1438. doi: 10.1126/science.6162199. [DOI] [PubMed] [Google Scholar]
  17. Moore P. B., Ownby C. L., Carraway K. L. Interactions of cytoskeletal elements with the plasma membrane of sarcoma180 ascites tumor cells. Exp Cell Res. 1978 Sep;115(2):331–342. doi: 10.1016/0014-4827(78)90287-2. [DOI] [PubMed] [Google Scholar]
  18. Mooseker M. S., Stephens R. E. Brush-border alpha-actinin? Comparison of two proteins of the microvillus core with alpha-actinin by two-dimensional peptide mapping. J Cell Biol. 1980 Aug;86(2):466–474. doi: 10.1083/jcb.86.2.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mooseker M. S., Tilney L. G. Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells. J Cell Biol. 1975 Dec;67(3):725–743. doi: 10.1083/jcb.67.3.725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Nurden A. T., Caen J. P. The different glycoprotein abnormalities in thrombasthenic and Bernard-Soulier platelets. Semin Hematol. 1979 Jul;16(3):234–250. [PubMed] [Google Scholar]
  21. Parikh I., March S., Cuatercasas P. Topics in the methodology of substitution reactions with agarose. Methods Enzymol. 1974;34:77–102. doi: 10.1016/s0076-6879(74)34009-8. [DOI] [PubMed] [Google Scholar]
  22. Phillips D. R., Jennings L. K., Edwards H. H. Identification of membrane proteins mediating the interaction of human platelets. J Cell Biol. 1980 Jul;86(1):77–86. doi: 10.1083/jcb.86.1.77. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Podlubnaya Z. A., Tskhovrebova L. A., Zaalishtsbvili M. M., Stefanenko G. A. Electron microscopic study of alpha-actinin. J Mol Biol. 1975 Feb 25;92(2):357–359. doi: 10.1016/0022-2836(75)90234-x. [DOI] [PubMed] [Google Scholar]
  24. Sanger J. M., Sanger J. W. Banding and polarity of actin filaments in interphase and cleaving cells. J Cell Biol. 1980 Aug;86(2):568–575. doi: 10.1083/jcb.86.2.568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stromer M. H., Goll D. E. Studies on purified -actinin. II. Electron microscopic studies on the competitive binding of -actinin and tropomyosin to Z-line extracted myofibrils. J Mol Biol. 1972 Jun 28;67(3):489–494. doi: 10.1016/0022-2836(72)90465-2. [DOI] [PubMed] [Google Scholar]
  26. Suzuki A., Goll D. E., Singh I., Allen R. E., Robson R. M., Stromer M. H. Some properties of purified skeletal muscle alpha-actinin. J Biol Chem. 1976 Nov 10;251(21):6860–6870. [PubMed] [Google Scholar]
  27. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wang K. Filamin, a new high-molecular-weight protein found in smooth muscle and nonmuscle cells. Purification and properties of chicken gizzard filamin. Biochemistry. 1977 May 3;16(9):1857–1865. doi: 10.1021/bi00628a015. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES