The Fine Structure of the Lens Epithelium

Wanko, Theodor

doi:10.1001/archopht.1958.00940080888007

Cited by 44 publications

(6 citation statements)

References 22 publications

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“…This behavior is consistent with a lens structure of concentric layers of closely apposed fiber cells that forms a complex protein gel with an overall protein content that is about one-third of the lens mass. Light and electron microscopy studies of the lens structure [35] reveal numerous interdigitations between lens fibers that presumably stabilize the lens mass, resist deformation during accommodation and help account for the low shear modulus that would be consistent with our study. Our approach yields a description of the local constitutive compressional properties of the lens fibers.…”

Section: Discussionsupporting

confidence: 87%

Light-Scattering Study of the Normal Human Eye Lens: Elastic Properties and Age Dependence

Bailey

Twa

Gump

et al. 2010

IEEE Trans. Biomed. Eng.

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The human ocular lens is a tissue capable of changing its shape to dynamically adjust the optical power of the eye, a function known as accommodation, which gradually declines with age. This capability is the response of the lens tissue to external forces which, in turn, is modulated by the biomechanical characteristics of lens tissues. In order to investigate the contributions of lens sclerosis to loss of accommodation, we report on in vitro confocal Brillouin light scattering studies of human ocular lenses spanning over a 30-70 year age range. Using this non-destructive measurement method, we determined that the longitudinal bulk modulus (average ± SD) of the lens nucleus (2.79±0.14 GPa) was consistently greater than the bulk modulus of the lens cortex (2.36±0.09 GPa). Moreover, our results showed that these differences were not age dependent over the 40 year age range that we evaluated using healthy lens tissues. Our results are consistent with the hypothesis that an age-dependent change in the bulk modulus of lens tissues does not fully account for the natural decline of accommodation.

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Section: Discussionsupporting

confidence: 87%

Light-Scattering Study of the Normal Human Eye Lens: Elastic Properties and Age Dependence

Bailey

Twa

Gump

et al. 2010

IEEE Trans. Biomed. Eng.

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“…2, a schematic drawing illustrates this variance in cytoplasmic contents. It also depicts the findings obtained from central, intermediate, and equatorial portions of the lens epithelium in the adult animal (14). These differentiations in cellular organization, from one part of the lens to the other, may be the morphological expression of biologically different functions in the individual lens regions.…”

Section: Commentsmentioning

confidence: 84%

Electron Microscope Study of Lens Fibers

Wanko

Gavin

1959

The Journal of Cell Biology

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PLATES 58 TO 62(Received for publication, January 16, 1959) ABSTRACT Comparative electron microscope investigations on sections of the lens cortex of the normal, mature rat, rabbit, monkey, and the normal calf reveal similar patterns of intracellular organization.The superficial lens fiber contains a nucleus, mitochondria, endoplasmic reticulum, dense granules, Golgi complex, and a quantity of small structures of low opacity which appear as filamentous and spherical configurations.Variations in number, distribution, and spatial arrangement of cytoplasmic elements in lens fibers are described. These changes in the pattern of cytoplasmic organization are concomitant with development of fibers and their displacement towards the center of the lens. Structural details of the various zones of the lens epithelium and the lens fibers are compared.

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“…Although Golgi and vesicular structures in the ocular lens have been reported as early as 195835–38 and more recently by other investigators,39–41 their relationship to crystallin distribution in the context of fiber cell differentiation has not been explored. The polarity of Golgi and, therefore, α B-crystallin in the lens epithelium (Figs.…”

Section: Discussionmentioning

confidence: 99%

αB-crystallin: A Golgi-Associated Membrane Protein in the Developing Ocular Lens

Gangalum¹,

Bhat²

2009

Invest. Ophthalmol. Vis. Sci.

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Purpose All crystallins have non-crystallin catalytic functions. Because catalytic functions do not require large concentrations of protein, as are seen in the lens, there is a perception of dichotomy in the catalytic/physiological function of crystallins within and outside the lens. The status of αB-crystallin, a ubiquitously expressed small heat shock protein (and a crystallin) in the ocular lens, was investigated. Methods Discontinuous sucrose density gradients were used for fractionation of Golgi membranes and vesicles. Light microscopy and confocal microscopy were used for immunolo-calization in cultured cells and the native lens. Results αB-crystallin is highly organized, as indicated by its polar presence in the apical Golgi in lens epithelium and in the perinuclear Golgi streaks in differentiating lens fiber cells. Assessment of the distribution of αB-crystallin in Golgi-enriched and vesicular fractions (characterized by the presence of Golgi membrane protein GM130 and vesicle coat protein γCOP) in the developing lens reveal a gradual transition from Golgi to vesicular fraction, concomitant with the appearance of αB-crystallin as a “soluble” protein. Conclusions These data demonstrate that αB-crystallin, known to be a soluble protein, starts life as a Golgi-associated membrane protein in the fetal and early postnatal lens and that the developmentally controlled physical state of the Golgi determines the status of this protein in the lens. These findings also show the similarity in the localization/ physiological function of αB-crystallin within and outside the ocular lens and suggest that non-crystallin/catalytic function is an innate component of the expression of a crystallin in the lens.

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The Fine Structure of the Lens Epithelium

Cited by 44 publications

References 22 publications

Light-Scattering Study of the Normal Human Eye Lens: Elastic Properties and Age Dependence

Light-Scattering Study of the Normal Human Eye Lens: Elastic Properties and Age Dependence

Electron Microscope Study of Lens Fibers

αB-crystallin: A Golgi-Associated Membrane Protein in the Developing Ocular Lens

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