scholarly journals Connexin 50 and AQP0 are Essential in Maintaining Organization and Integrity of Lens Fibers

2019 ◽  
Vol 60 (12) ◽  
pp. 4021 ◽  
Author(s):  
Sumin Gu ◽  
Sondip Biswas ◽  
Luis Rodriguez ◽  
Zhen Li ◽  
Yuting Li ◽  
...  
Keyword(s):  
Lens Fibers ◽  
Connexin 50

Volume change of the ocular lens during accommodation

2007 ◽  
Vol 293 (2) ◽  
pp. C797-C804 ◽  
Author(s):  
R. Gerometta ◽  
A. C. Zamudio ◽  
D. P. Escobar ◽  
O. A. Candia
Keyword(s):  
Structural Parameters ◽  
Center Of Mass ◽  
Physiological Solution ◽  
Volume Determination ◽  
Cross Sectional ◽  
Lens Fibers ◽  
Human Lenses ◽  
Lens Surface ◽  
Shape Changes ◽  
Anterior Posterior

During accommodation, mammalian lenses change shape from a rounder configuration (near focusing) to a flatter one (distance focusing). Thus the lens must have the capacity to change its volume, capsular surface area, or both. Because lens topology is similar to a torus, we developed an approach that allows volume determination from the lens cross-sectional area (CSA). The CSA was obtained from photographs taken perpendicularly to the lenticular anterior-posterior (A-P) axis and computed with software. We calculated the volume of isolated bovine lenses in conditions simulating accommodation by forcing shape changes with a custom-built stretching device in which the ciliary body-zonulae-lens complex (CB-Z-L) was placed. Two measurements were taken (CSA and center of mass) to calculate volume. Mechanically stretching the CB-Z-L increased the equatorial length and decreased the A-P length, CSA, and lens volume. The control parameters were restored when the lenses were stretched and relaxed in an aqueous physiological solution, but not when submerged in oil, a condition with which fluid leaves the lens and does not reenter. This suggests that changes in lens CSA previously observed in humans could have resulted from fluid movement out of the lens. Thus accommodation may involve changes not only in capsular surface but also in volume. Furthermore, we calculated theoretical volume changes during accommodation in models of human lenses using published structural parameters. In conclusion, we suggest that impediments to fluid flow between the aquaporin-rich lens fibers and the lens surface could contribute to the aging-related loss of accommodative power.

Connexin 50 mutation in a family with congenital "zonular nuclear" pulverulent cataract of Pakistani origin

1999 ◽  
Vol 105 (1-2) ◽  
pp. 168-170 ◽  
Author(s):  
V. Berry ◽  
D. Mackay ◽  
S. Khaliq ◽  
P.J. Francis ◽  
A. Hameed ◽  
...  
Keyword(s):  
Pakistani Origin ◽  
Connexin 50

scholarly journals Lens fibers have a fully functional ubiquitin-proteasome pathway

2003 ◽  
Vol 76 (5) ◽  
pp. 623-631 ◽  
Author(s):  
Paulo Pereira ◽  
Fu Shang ◽  
Marisa Hobbs ◽  
Henrique Girão ◽  
Allen Taylor
Keyword(s):  
Ubiquitin Proteasome Pathway ◽  
Lens Fibers ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

scholarly journals Connexin 50 Functions as an Adhesive Molecule and Promotes Lens Cell Differentiation

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Zhengping Hu ◽  
Wen Shi ◽  
Manuel A. Riquelme ◽  
Qian Shi ◽  
Sondip Biswas ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Adhesive Molecule ◽  
Lens Cell ◽  
Connexin 50

scholarly journals Molecular heterogeneity of adherens junctions.

1985 ◽  
Vol 101 (4) ◽  
pp. 1523-1531 ◽  
Author(s):  
B Geiger ◽  
T Volk ◽  
T Volberg
Keyword(s):  
Adherens Junctions ◽  
Intercellular Junctions ◽  
The Other ◽  
Molecular Heterogeneity ◽  
Immunofluorescent Localization ◽  
Lens Fibers ◽  
Tissue Extracts ◽  
Focal Contacts ◽  
Cell Substrate ◽  
Membrane Bound

We describe here the subcellular distributions of three junctional proteins in different adherens-type contacts. The proteins examined include vinculin, talin, and a recently described 135-kD protein (Volk, T., and B. Geiger, 1984, EMBO (Eur. Mol. Biol. Organ.) J., 10:2249-2260). Immunofluorescent localization of the three proteins indicated that while vinculin was ubiquitously present in all adherens junctions, the other two showed selective and mutually exclusive association with either cell-substrate or cell-cell adhesions. Talin was abundant in focal contacts and in dense plaques of smooth muscle, but was essentially absent from intercellular junctions such as intercalated disks or adherens junctions of lens fibers. The 135-kD protein, on the other hand, was present in the latter two loci and was apparently absent from membrane-bound plaques of gizzard or from focal contacts. Radioimmunoassay of tissue extracts and immunolabeling of cultured chick lens cells indicated that the selective presence of talin and of the 135-kD protein in different cell contacts is spatially regulated within individual cells. On the basis of these findings it was concluded that adherens junctions are molecularly heterogeneous and consist of at least two major subgroups. Contacts with noncellular substrates contain talin and vinculin but not the 135-kD protein, whereas their intercellular counterparts contain the latter two proteins and are devoid of talin. The significance of these results and their possible relationships to contact-induced regulation of cell behavior are discussed.

Mutation in the connexin 50 gene (GJA8) in a Russian family with zonular pulverulent cataract

2001 ◽  
Vol 60 (6) ◽  
pp. 476-478 ◽  
Author(s):  
AV Polyakov ◽  
IA Shagina ◽  
OV Khlebnikova ◽  
OV Evgrafov
Keyword(s):  
Connexin 50

scholarly journals Age-related compaction of lens fibers affects the structure and optical properties of rabbit lenses

2007 ◽  
Vol 7 (1) ◽  
Author(s):  
Samer Al-khudari ◽  
Sean T Donohue ◽  
Walid M Al-Ghoul ◽  
Kristin J Al-Ghoul
Keyword(s):  
Optical Properties ◽  
Lens Fibers ◽  
Age Related

Calcium-mediated disintegrative globulization of isolated ocular lens fibers mimics cataractogenesis

1995 ◽  
Vol 61 (3) ◽  
pp. 303-310 ◽  
Author(s):  
Aruni Bhatnagar ◽  
Naseem H. Ansari ◽  
Lifei Wang ◽  
Peeyush Khanna ◽  
Changsen Wang ◽  
...  
Keyword(s):  
Ocular Lens ◽  
Lens Fibers
Sign in / Sign up

Export Citation Format

Share Document