Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1987 Jun 1;104(6):1563–1568. doi: 10.1083/jcb.104.6.1563

Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits

PMCID: PMC2114517  PMID: 2438286

Abstract

Monoclonal antibodies specific for each of the flagellar tektins were prepared and used to determine whether structures similar to tektin filaments are present in cells lacking cilia or flagella. This analysis was performed by double-label immunofluorescence microscopy of several cell lines and by immunoblots of protein fractions. Two of the four anti-tektin antibodies, the antibodies 3-7-1 and 3-10-1, which bind different epitopes of the C-tektin, label 3T3, HeLa, PtK2, and BHK-21 cells as well as myotubes. The antibody 3-7-1 stains intermediate filament structures in the cells and binds vimentin or desmin in preparations of cytoskeletal proteins; whereas the antibody 3-10-1 stains nuclear envelopes in the cells and binds lamin A and C in preparations of cytoskeletal proteins or nuclear lamina. Structural similarities between the C-tektin and intermediate filament proteins probably are extended to more than two epitopes because polyclonal antibodies anti-vimentin and anti-desmin bind to C-tektin. These polyclonal antibodies also bind to A-tektin. The cross-reaction of monoclonal and polyclonal antibodies binding to epitopes in tektin and intermediate filament components and the existence of a high content of alpha-helical structure in the tektin subunits (Linck, R. W., and G. L. Langevin, 1982, J. Cell Sci., 58:1-22) indicate that tektin and intermediate filaments are homologous in several parts of their structure.

Full Text

The Full Text of this article is available as a PDF (1.8 MB).

Selected References

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

  1. Aebi U., Cohn J., Buhle L., Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 1986 Oct 9;323(6088):560–564. doi: 10.1038/323560a0. [DOI] [PubMed] [Google Scholar]
  2. Dwyer N., Blobel G. A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei. J Cell Biol. 1976 Sep;70(3):581–591. doi: 10.1083/jcb.70.3.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fischbach G. D. Synapse formation between dissociated nerve and muscle cells in low density cell cultures. Dev Biol. 1972 Jun;28(2):407–429. doi: 10.1016/0012-1606(72)90023-1. [DOI] [PubMed] [Google Scholar]
  4. Fisher D. Z., Chaudhary N., Blobel G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6450–6454. doi: 10.1073/pnas.83.17.6450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Geisler N., Kaufmann E., Fischer S., Plessmann U., Weber K. Neurofilament architecture combines structural principles of intermediate filaments with carboxy-terminal extensions increasing in size between triplet proteins. EMBO J. 1983;2(8):1295–1302. doi: 10.1002/j.1460-2075.1983.tb01584.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gerace L., Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell. 1980 Jan;19(1):277–287. doi: 10.1016/0092-8674(80)90409-2. [DOI] [PubMed] [Google Scholar]
  7. Gibbons I. R., Fronk E. A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella. J Biol Chem. 1979 Jan 10;254(1):187–196. [PubMed] [Google Scholar]
  8. Linck R. W., Albertini D. F., Kenney D. M., Langevin G. L. Tektin filaments: chemically unique filaments of sperm flagellar microtubules. Prog Clin Biol Res. 1982;80:127–132. doi: 10.1002/cm.970020724. [DOI] [PubMed] [Google Scholar]
  9. Linck R. W., Amos L. A., Amos W. B. Localization of tektin filaments in microtubules of sea urchin sperm flagella by immunoelectron microscopy. J Cell Biol. 1985 Jan;100(1):126–135. doi: 10.1083/jcb.100.1.126. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Linck R. W. Flagellar doublet microtubules: fractionation of minor components and alpha-tubulin from specific regions of the A-tubule. J Cell Sci. 1976 Mar;20(2):405–439. doi: 10.1242/jcs.20.2.405. [DOI] [PubMed] [Google Scholar]
  11. Linck R. W., Langevin G. L. Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules. J Cell Sci. 1982 Dec;58:1–22. doi: 10.1242/jcs.58.1.1. [DOI] [PubMed] [Google Scholar]
  12. McKeon F. D., Kirschner M. W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 1986 Feb 6;319(6053):463–468. doi: 10.1038/319463a0. [DOI] [PubMed] [Google Scholar]
  13. Meza I., Huang B., Bryan J. Chemical heterogeneity of protofilaments forming the outer doublets from sea urchin flagella. Exp Cell Res. 1972 Oct;74(2):535–540. doi: 10.1016/0014-4827(72)90413-2. [DOI] [PubMed] [Google Scholar]
  14. Ottaviano Y., Gerace L. Phosphorylation of the nuclear lamins during interphase and mitosis. J Biol Chem. 1985 Jan 10;260(1):624–632. [PubMed] [Google Scholar]
  15. Piperno G., Huang B., Ramanis Z., Luck D. J. Radial spokes of Chlamydomonas flagella: polypeptide composition and phosphorylation of stalk components. J Cell Biol. 1981 Jan;88(1):73–79. doi: 10.1083/jcb.88.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Piperno G., LeDizet M., Chang X. J. Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J Cell Biol. 1987 Feb;104(2):289–302. doi: 10.1083/jcb.104.2.289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Piperno G. Monoclonal antibodies to dynein subunits reveal the existence of cytoplasmic antigens in sea urchin egg. J Cell Biol. 1984 May;98(5):1842–1850. doi: 10.1083/jcb.98.5.1842. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Starger J. M., Brown W. E., Goldman A. E., Goldman R. D. Biochemical and immunological analysis of rapidly purified 10-nm filaments from baby hamster kidney (BHK-21) cells. J Cell Biol. 1978 Jul;78(1):93–109. doi: 10.1083/jcb.78.1.93. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wehland J., Schröder H. C., Weber K. Amino acid sequence requirements in the epitope recognized by the alpha-tubulin-specific rat monoclonal antibody YL 1/2. EMBO J. 1984 Jun;3(6):1295–1300. doi: 10.1002/j.1460-2075.1984.tb01965.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Witman G. B., Carlson K., Berliner J., Rosenbaum J. L. Chlamydomonas flagella. I. Isolation and electrophoretic analysis of microtubules, matrix, membranes, and mastigonemes. J Cell Biol. 1972 Sep;54(3):507–539. doi: 10.1083/jcb.54.3.507. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES