Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1977 Feb 1;72(2):482–492. doi: 10.1083/jcb.72.2.482

Distribution of anionic sites on the oviduct ciliary membrane

PMCID: PMC2111014  PMID: 833205

Abstract

Polycationic ferritin (PCF) was used as a visual probe for anionic sites on the oviduct ciliary membrane. The binding of PCF to ciliary membranes was dependent on the concentration of the probe in the incubation media. At low concentrations (0.08-0.16 mg/ml), PCF was bound exclusively to the tip of the cilium whereas at higher concentrations (0.32-0.64 mg/ml), ferritin was located at the tip and at the base around the transition region, with occasional scattered clumps on the remainder of the membrane. The base and tip binding was fount to be associated with special surface modifications of the membrane in these regions. At the tip, PCF was bound to a filamentous glycocalyx termed the ciliary crown. Base binding was associated with a system of five to six 140-A high ridges, each of which encircled the membrane of the transition region. The ridges were equally spaced (approxamately 245 A spacing) along the length of the transition region. Since pretreatment of oviduct with either neuraminidase or protease blocked the binding of the probe, the PCF-binding sites appear to be negatively charged glycoproteins or mucopolysaccharides.

Full Text

The Full Text of this article is available as a PDF (2.8 MB).

Selected References

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

  1. Brummett A. R., Dumont J. N. Oogenesis in Xenopus laevis (Daudin). III. Localization of negative charges on the surface of developing oocytes. J Ultrastruct Res. 1976 Apr;55(1):4–16. doi: 10.1016/s0022-5320(76)80077-9. [DOI] [PubMed] [Google Scholar]
  2. Danon D., Goldstein L., Marikovsky Y., Skutelsky E. Use of cationized ferritin as a label of negative charges on cell surfaces. J Ultrastruct Res. 1972 Mar;38(5):500–510. doi: 10.1016/0022-5320(72)90087-1. [DOI] [PubMed] [Google Scholar]
  3. Dirksen E. R., Satir P. Ciliary activity in the mouse oviduct as studied by transmission and scanning electron microscopy. Tissue Cell. 1972;4(3):389–403. doi: 10.1016/s0040-8166(72)80017-x. [DOI] [PubMed] [Google Scholar]
  4. Flower N. E. Particles within membranes: a freeze-etch view. J Cell Sci. 1971 Sep;9(2):435–441. doi: 10.1242/jcs.9.2.435. [DOI] [PubMed] [Google Scholar]
  5. Hill F. G., Outka D. E. The structure and origin of mastigonemes in Ochromonas minute and Monas sp. J Protozool. 1974 May;21(2):299–312. doi: 10.1111/j.1550-7408.1974.tb03658.x. [DOI] [PubMed] [Google Scholar]
  6. Mehrishi J. N. Molecular aspects of the mammalian cell surface. Prog Biophys Mol Biol. 1972;25:1–70. doi: 10.1016/0079-6107(72)90013-2. [DOI] [PubMed] [Google Scholar]
  7. Nicolson G. L. Anionic sites of human erythrocyte membranes. I. Effects of trypsin, phospholipase C, and pH on the topography of bound positively charged colloidal particles. J Cell Biol. 1973 May;57(2):373–387. doi: 10.1083/jcb.57.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Snell W. J. Mating in Chlamydomonas: a system for the study of specific cell adhesion. I. Ultrastructural and electrophoretic analyses of flagellar surface components involved in adhesion. J Cell Biol. 1976 Jan;68(1):48–69. doi: 10.1083/jcb.68.1.48. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Snell W. J. Mating in Chlamydomonas: a system for the study of specific cell adhesion. II. A radioactive flagella-binding assay for quantitation of adhesion. J Cell Biol. 1976 Jan;68(1):70–79. doi: 10.1083/jcb.68.1.70. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES