| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
From the Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, 1020 Locust Street, Philadelphia, Pennsylvania.
PURPOSE. To analyze the dynamics of N- and B-cadherin cell adhesion molecule expression and cytoskeletal interaction during embryonic chick lens development.
METHODS. Localization of N- and B-cadherin, F-actin, and connexin 56 were determined by immunohistochemistry of developing lenses or immunocytochemistry of differentiating primary lens cultures. Biochemical analysis of cytoskeletal linkage of N- or B-cadherin was assessed by differential detergent extraction, electrophoresis, and immunoblotting.
RESULTS. The results indicate that although both cadherins are expressed throughout lens development, N-cadherin expression detected was similar in both lens epithelial and fiber cells, whereas B-cadherin was preferentially localized to the lens fiber cells. During differentiation, both cadherins become increasingly associated with the lens cytoskeleton, as indicated biochemically by a transition from largely Triton X-100–soluble to Triton X-100–insoluble pools and immunocytologically by cadherin localization to cell–cell borders and colocalization with the actin cytoskeleton. Although a significant fraction of N-cadherin remains Triton X-100–soluble as the lens cells differentiate, B-cadherin becomes resistant to extraction by both Triton X-100 as well as RIPA buffers. As detected immunocytochemically in lens cell cultures, the temporal localization of N-cadherin to cell–cell interfaces precedes that of B-cadherin. Furthermore, temporal localization of B-cadherin, as opposed to N-cadherin, to cell–cell borders more closely parallels that of connexin 56 in vitro as well as in vivo.
CONCLUSIONS. These results suggest that while both N- and B-cadherin are expressed during lens cell differentiation, both their patterns of expression as well as their cytoskeletal association differ between epithelial and fiber cells.
This article has been cited by other articles:
|
|
 |
|
  J.-h. Xi, F. Bai, J. Gross, R. R. Townsend, A. S. Menko, and U. P. Andley Mechanism of Small Heat Shock Protein Function in Vivo: A KNOCK-IN MOUSE MODEL DEMONSTRATES THAT THE R49C MUTATION IN {alpha}A-CRYSTALLIN ENHANCES PROTEIN INSOLUBILITY AND CELL DEATH J. Biol. Chem., February 29, 2008; 283(9): 5801 - 5814. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Liwosz, T. Lei, and M. A. Kukuruzinska N-Glycosylation Affects the Molecular Organization and Stability of E-cadherin Junctions J. Biol. Chem., August 11, 2006; 281(32): 23138 - 23149. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Y. Gao, M. A. Stepp, R. Fariss, and P. Zelenka Cdk5 regulates activation and localization of Src during corneal epithelial wound closure J. Cell Sci., August 15, 2004; 117(18): 4089 - 4098. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. N. Ripley, M. S. Chang, and D. M. Bader Bves Is Expressed in the Epithelial Components of the Retina, Lens, and Cornea Invest. Ophthalmol. Vis. Sci., August 1, 2004; 45(8): 2475 - 2483. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. D. Jacobs, C. Soeller, A. M. G. Sisley, M. B. Cannell, and P. J. Donaldson Gap Junction Processing and Redistribution Revealed by Quantitative Optical Measurements of Connexin46 Epitopes in the Lens Invest. Ophthalmol. Vis. Sci., January 1, 2004; 45(1): 191 - 199. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. K. Straub, J. Boda, C. Kuhn, M. Schnoelzer, U. Korf, T. Kempf, H. Spring, M. Hatzfeld, and W. W. Franke A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells J. Cell Sci., December 15, 2003; 116(24): 4985 - 4995. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
