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. 1987 Mar 1;104(3):565–572. doi: 10.1083/jcb.104.3.565

Immunolocalization of MP70 in lens fiber 16-17-nm intercellular junctions

PMCID: PMC2114558  PMID: 3818793

Abstract

Thin section electron microscopy reveals two different types of membrane interactions between the fiber cells of bovine lens. Monoclonal antibodies against lens membrane protein MP70 (Kistler et al., 1985, J. Cell Biol., 101:28-35) bound exclusively to the 16-17-nm intercellular junctions. MP70 localization was most dramatic in the lens outer cortex and strongly reduced deeper in the lens. In contrast, the 12-nm double membrane structures and single membranes were consistently unlabeled. In freeze-fracture replicas with adherent cortical fiber membranes, MP70 was immunolocalized in the junctional plaques which closely resemble the gap junctions in other tissues. MP70 is thus likely to be associated with intercellular communication in the lens.

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Selected References

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

  1. FitzGerald P. G., Bok D., Horwitz J. The distribution of the main intrinsic membrane polypeptide in ocular lens. Curr Eye Res. 1985 Nov;4(11):1203–1218. doi: 10.3109/02713688509003365. [DOI] [PubMed] [Google Scholar]
  2. Fitzgerald P. G., Bok D., Horwitz J. Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens. J Cell Biol. 1983 Nov;97(5 Pt 1):1491–1499. doi: 10.1083/jcb.97.5.1491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Garner W. H., Hilal S. K., Lee S. W., Spector A. Sodium-23 magnetic resonance imaging of the eye and lens. Proc Natl Acad Sci U S A. 1986 Mar;83(6):1901–1905. doi: 10.1073/pnas.83.6.1901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Goodenough D. A., Dick J. S., 2nd, Lyons J. E. Lens metabolic cooperation: a study of mouse lens transport and permeability visualized with freeze-substitution autoradiography and electron microscopy. J Cell Biol. 1980 Aug;86(2):576–589. doi: 10.1083/jcb.86.2.576. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Goodenough D. A. Lens gap junctions: a structural hypothesis for nonregulated low-resistance intercellular pathways. Invest Ophthalmol Vis Sci. 1979 Nov;18(11):1104–1122. [PubMed] [Google Scholar]
  6. Kistler J., Gilbert K., Brooks H. V., Jolly R. D., Hopcroft D. H., Bullivant S. Membrane interlocking domains in the lens. Invest Ophthalmol Vis Sci. 1986 Oct;27(10):1527–1534. [PubMed] [Google Scholar]
  7. Kistler J., Kirkland B., Bullivant S. Identification of a 70,000-D protein in lens membrane junctional domains. J Cell Biol. 1985 Jul;101(1):28–35. doi: 10.1083/jcb.101.1.28. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kistler J., Kirkland B., Gilbert K., Bullivant S. Aging of lens fibers. Mapping membrane proteins with monoclonal antibodies. Invest Ophthalmol Vis Sci. 1986 May;27(5):772–780. [PubMed] [Google Scholar]
  9. Kuszak J. R., Rae J. L., Pauli B. U., Weinstein R. S. Rotary replication of lens gap junction. J Ultrastruct Res. 1982 Nov;81(2):249–256. doi: 10.1016/s0022-5320(82)90080-6. [DOI] [PubMed] [Google Scholar]
  10. Kuszak J., Alcala J., Maisel H. The surface morphology of embryonic and adult chick lens-fiber cells. Am J Anat. 1980 Dec;159(4):395–410. doi: 10.1002/aja.1001590406. [DOI] [PubMed] [Google Scholar]
  11. Lo W. K., Harding C. V. Square arrays and their role in ridge formation in human lens fibers. J Ultrastruct Res. 1984 Mar;86(3):228–245. doi: 10.1016/s0022-5320(84)90103-5. [DOI] [PubMed] [Google Scholar]
  12. Paul D. L., Goodenough D. A. Preparation, characterization, and localization of antisera against bovine MP26, an integral protein from lens fiber plasma membrane. J Cell Biol. 1983 Mar;96(3):625–632. doi: 10.1083/jcb.96.3.625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rae J. L., Thomson R. D., Eisenberg R. S. The effect of 2-4 dinitrophenol on cell to cell communication in the frog lens. Exp Eye Res. 1982 Dec;35(6):597–609. doi: 10.1016/s0014-4835(82)80073-0. [DOI] [PubMed] [Google Scholar]
  14. Sas D. F., Sas M. J., Johnson K. R., Menko A. S., Johnson R. G. Junctions between lens fiber cells are labeled with a monoclonal antibody shown to be specific for MP26. J Cell Biol. 1985 Jan;100(1):216–225. doi: 10.1083/jcb.100.1.216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Zampighi G., Simon S. A., Robertson J. D., McIntosh T. J., Costello M. J. On the structural organization of isolated bovine lens fiber junctions. J Cell Biol. 1982 Apr;93(1):175–189. doi: 10.1083/jcb.93.1.175. [DOI] [PMC free article] [PubMed] [Google Scholar]

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