Differential Effects of Fibronectin-DerivedOligopeptides on the Attachment of Rabbit Lens Epithelial Cells in vitro

1996 ◽  
Vol 28 (4) ◽  
pp. 201-208 ◽  
Author(s):  
Tetsuo Sasabe ◽  
Yuzo Suwa ◽  
Akira Kiritoshi ◽  
Masamitsu Doi ◽  
Takenosuke Yuasa ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Lens Epithelial Cells ◽  
Differential Effects ◽  
Rabbit Lens

scholarly journals Biosynthesis of sulphated macromolecules by rabbit lens epithelium. I. Identification of the major macromolecules synthesized by lens epithelial cells in vitro.

1984 ◽  
Vol 99 (3) ◽  
pp. 852-860 ◽  
Author(s):  
J G Heathcote ◽  
R W Orkin
Keyword(s):  
Molecular Weight ◽  
Epithelial Cells ◽  
Basement Membrane ◽  
Culture Medium ◽  
Cell Layer ◽  
Heparan Sulphate ◽  
Lens Epithelial Cells ◽  
Heparan Sulphate Proteoglycan ◽  
Rabbit Lens

Rabbit lens epithelial cells synthesize and secrete a variety of [35S]sulphate-labeled glycoconjugates in vitro. Associated with the cell layer, and with the medium, was a high molecular weight glycoconjugate(s) that contained heparan sulphate which was apparently covalently linked to sulphated glycoprotein. This component(s) was eluted in the void volume of a Sepharose CL-2B column and could not be fractionated by detergent treatment or extraction with lipid solvents. The cell layer also contained glycosaminoglycans (72% heparan sulphate, 28% chondroitin sulphate), as well as a small proportion of a low molecular weight sulphated glycoprotein. The major 35S-labeled species secreted into the medium were sulphated glycoproteins with approximate molecular weights of 120,000 and 35,000 together with a heparan sulphate proteoglycan. This proteoglycan could be precipitated from the culture medium with 30% saturated (NH4)2SO4 and eluted from Sepharose CL-4B columns at approximately the same position (Kav = 0.15) as heparan sulphate proteoglycans described in the basement membrane of the EHS "sarcoma" (Hassell, J. R., P. G. Robey, H. J. Barrach, J. Wilczek, S. I. Rennard, and G. R. Martin, 1980, Proc. Natl. Acad. Sci. USA, 77:4494-4498) and of the mouse mammary epithelium (David, G., and M. Bernfield, 1981, J. Cell Biol., 91:281-286). Its presence in the culture medium was unanticipated but may be explained by the inability of these cultures to deposit a basement membrane when grown on a plastic surface. The relationship of this heparan sulphate proteoglycan to the lens epithelial basement membrane is the subject of the following paper.

Donor age influences the growth of rabbit lens epithelial cells in vitro

1981 ◽  
Vol 21 (1) ◽  
pp. 11-23 ◽  
Author(s):  
John R. Reddan ◽  
Thomas B. Friedman ◽  
M. Kazem Mostafapour ◽  
Robert L. Bondy ◽  
Steven H. Sutherland ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Lens Epithelial Cells ◽  
Donor Age ◽  
Rabbit Lens

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

scholarly journals P 229 Growth of human lens epithelial cells on the anterior lens capsule in vitro

1995 ◽  
Vol 35 ◽  
pp. S199
Author(s):  
J.H. Meyer ◽  
J. Schmidt ◽  
F. Eppinger ◽  
B. Flügel ◽  
K.U. Löffler ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Lens Capsule ◽  
Human Lens ◽  
Lens Epithelial Cells ◽  
Human Lens Epithelial Cells ◽  
Anterior Lens Capsule

scholarly journals On the Anticataractogenic Effects of L-Carnosine: Is It Best Described as an Antioxidant, Metal-Chelating Agent or Glycation Inhibitor?

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Hamdy Abdelkader ◽  
Michael Longman ◽  
Raid G. Alany ◽  
Barbara Pierscionek
Keyword(s):  
Epithelial Cells ◽  
Antioxidant Activities ◽  
Ex Vivo ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Human Lens ◽  
Lens Epithelial Cells ◽  
Metal Chelating ◽  
Human Lens Epithelial Cells

Purpose.L-Carnosine is a naturally occurring dipeptide which recently gained popularity as an anticataractogenic agent due to its purported antioxidant activities. There is a paucity of research and conclusive evidence to support such claims. This work offers compelling data that help clarify the mechanism(s) behind the anticataract properties of L-carnosine.Methods.Direct in vitro antioxidant free radical scavenging properties were assayed using three different antioxidant (TEAC, CUPRAC, and DPPH) assays. Indirect in vitro and ex vivo antioxidant assays were studied by measuring glutathione bleaching capacity and total sulfhydryl (SH) capacity of bovine lens homogenates as well as hydrogen-peroxide-stress assay using human lens epithelial cells. Whole porcine lenses were incubated in high galactose media to study the anticataract effects of L-carnosine. MTT cytotoxicity assays were conducted on human lens epithelial cells.Results.The results showed that L-carnosine is a highly potent antiglycating agent but with weak metal chelating and antioxidant properties. There were no significant decreases in lens epithelial cell viability compared to negative controls. Whole porcine lenses incubated in high galactose media and treated with 20 mM L-carnosine showed a dramatic inhibition of advanced glycation end product formation as evidenced by NBT and boronate affinity chromatography assays.Conclusion.L-Carnosine offers prospects for investigating new methods of treatment for diabetic cataract and any diseases that are caused by glycation.

scholarly journals p-Coumaric Acid Protects Human Lens Epithelial Cells against Oxidative Stress-Induced Apoptosis by MAPK Signaling

2018 ◽  
Vol 2018 ◽  
pp. 1-7 ◽  
Author(s):  
Jiao Peng ◽  
Ting-ting Zheng ◽  
Yue Liang ◽  
Li-fang Duan ◽  
Yao-dong Zhang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Epithelial Cells ◽  
Mapk Signaling ◽  
Human Lens ◽  
Lens Epithelial Cells ◽  
Dependent Manner ◽  
Coumaric Acid ◽  
Underlying Mechanisms ◽  
Induced Apoptosis

To protect against oxidative stress-induced apoptosis in lens epithelial cells is a potential strategy in preventing cataract formation. The present study aimed at studying the protective effect and underlying mechanisms of p-coumaric acid (p-CA) on hydrogen peroxide- (H2O2-) induced apoptosis in human lens epithelial (HLE) cells (SRA 01–04). Cells were pretreated with p-CA at a concentration of 3, 10, and 30 μM before the treatment of H2O2 (275 μM). Results showed that pretreatment with p-CA significantly protected against H2O2-induced cell death in a dose-dependent manner, as well as downregulating the expressions of both cleaved caspase-3 and cleaved caspase-9 in HLE cells. Moreover, p-CA also greatly suppressed H2O2-induced intracellular ROS production and mitochondrial membrane potential loss and elevated the activities of T-SOD, CAT, and GSH-Px of H2O2-treated cells. As well, in vitro study showed that p-CA also suppressed H2O2-induced phosphorylation of p-38, ERK, and JNK in HLE cells. These findings demonstrate that p-CA suppresses H2O2-induced HLE cell apoptosis through modulating MAPK signaling pathways and suggest that p-CA has a potential therapeutic role in the prevention of cataract.

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