A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells
Author:
Straub Beate K.1, Boda Judit1, Kuhn Caecilia1, Schnoelzer Martina2, Korf Ulrike2, Kempf Tore2, Spring Herbert3, Hatzfeld Mechthild4, Franke Werner W.1
Affiliation:
1. Division of Cell Biology, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany 2. Protein Analysis Facility, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany 3. Structural Analysis Group, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany 4. Institute for Physiological Chemistry, Medical Faculty, University of Halle, Magdeburger Strasse 18, 06097 Halle/Saale, Germany
Abstract
The anucleate prismoid fiber cells of the eye lens are densely packed to form a tissue in which the plasma membranes and their associated cytoplasmic coat form a single giant cell-cell adhesive complex, the cortex adhaerens. Using biochemical and immunoprecipitation methods in various species (cow, pig, rat), in combination with immunolocalization microscopy, we have identified two different major kinds of cortical complex. In one, the transmembrane glycoproteins N-cadherin and cadherin-11 [which also occur in heterotypic (`mixed') complexes] are associated with α- and β-catenin, plakoglobin (proportions variable among species), p120ctn and vinculin. The other complex contains ezrin, periplakin, periaxin and desmoyokin (and so is called the EPPD complex), usually together with moesin, spectrin(s) and plectin. In sections through lens fiber tissue, the short sides of the lens fiber hexagons appear to be enriched in the cadherin-based complexes, whereas the EPPD complexes also occur on the long sides. Moreover, high resolution double-label fluorescence microscopy has revealed, on the short sides, a finer, almost regular mosaicism of blocks comprising the cadherin-based, catenin-containing complexes, alternating with patches formed by the EPPD complexes. The latter, a new type of junctional plaque ensemble of proteins hitherto known only from certain other cell types, must be added to the list of major lens cortex proteins. We here discuss its possible functional importance for the maintenance of lens structure and functions, notably clear and sharp vision.
Publisher
The Company of Biologists
Reference107 articles.
1. Achtstätter, T., Hatzfeld, M., Quinlan, R. A., Parmelee, D. C. and Franke, W. W. (1986). Separation of cytokeratin polypeptides by gel electrophoretic and chromatographic techniques and their identification by immunoblotting. Methods Enzymol.134, 355-371. 2. Aho, S., McLean, W. H. I., Li, K. and Uitto, J. (1998). cDNA cloning, mRNA expression, and chromosomal mapping of human and mouse periplakin genes. Genomics48, 242-247. 3. Ahrens, T., Lambert, M., Pertz, O., Sasaki, T., Schulthess, T., Mège, R.-M., Timpl, R. and Engel, J. (2003). Homoassociation of VE-cadherin follows a mechanism common to `classical' cadherins. J. Mol. Biol.325, 733-742. 4. Alcala, J., Lieska, N. and Maisel, H. (1975). Protein composition of bovine lens cortical fiber cell membranes. Exp. Eye Res.21, 581-595. 5. Allen, D. P., Low, P. S., Dola, A. and Maisel, H. (1987). Band 3 and ankyrin homologues are present in eye lens: evidence for all major erythrocyte membrane components in same non-erythroid cell. Biochem. Biophys. Res. Commun.149, 266-275.
Cited by
108 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|