• Journal of Korean Ophthalmic Optics Society
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• v.15 no.3
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• pp.227-234
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• 2010

Purpose: The cleaning effect of protein deposit and the change of contact lens parameters by ultrasonic cleaner for eye glasses on the soft contact lenses were investigated. Methods: Etafilcon A contact lenses contaminated with protein, was ultrasonicated by ultrasonic cleaner for eye glasses and for the control group, spoiled contact lenses were cleaned by multi-purpose solution. The remaining protein deposits on the contact lenses were determined after extraction and the changes of overall diameter, base curve, center thickness power, and water contents on contact lenses were measured and surfaces of contact lenses were observed by scanning electron microscope. Results: The cleaning efficacies of multi-purpose solution on protein deposited etafilcon A contact lenses were 6.08%, and 23.73~33.92% in the group of ultrasonic cleaner for eye glasses with multi-purpose solution and 0~12.99% in the group of ultrasonic clear for contact lens with multipurpose solution depending on the treatment time. The changes of parameters and surface on contact lenses by ultrasonication were not observed. Conclusions: Ultrasonic cleaner for eye glasses can be used to eliminate protein deposits for the diagnostic soft contact lens in the office since it was effective to eliminate protein deposits and not caused change of parameters on soft contact lenses.

• BMB Reports
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• v.38 no.3
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• pp.275-280
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• 2005

For most of proteins to be active, they need well-defined three-dimensional structures alone or in complex. Folding is a process through which newly synthesized proteins get to the native state. Protein folding inside cells is assisted by various chaperones and folding factors, and misfolded proteins are eliminated by the ubiquitin-proteasome degradation system to ensure high fidelity of protein expression. Under certain circumstances, misfolded proteins escape the degradation process, yielding to deposit of protein aggregates such as loop-sheet polymer and amyloid fibril. Diseases characterized by insoluble deposits of proteins have been recognized for long time and are grouped as conformational diseases. Study of protein folding mechanism is required for better understanding of the molecular pathway of such conformational diseases.

• Bulletin of the Korean Chemical Society
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• v.34 no.5
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• pp.1503-1507
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• 2013

The two major symptoms characterizing Alzheimer's disease are the formation of amyloid-${\beta}$ extracellular deposits in the form of senile plaques and intracellular neurofibrillary tangles (NFTs) that consist of pathological hyperphosphorylated tau protein aggregated into insoluble paired helical filaments (PHFs). Neurons of the central nervous system have appreciable amounts of tau protein, a microtubule-associated protein. To maintain an optimal operation of nerves, the microtubules are stabilized, which is necessary to support cell structure and cellular processes. When the modified tau protein becomes dysfunctional, the cells containing misfolded tau cannot maintain cell structure. One of the pathological hallmarks of Alzheimer's disease is hyperphosphorylated tau protein. This paper shows that the small heat shock protein from humans (Hsp27) reduces hyperphosphorylated tau and prevents hyperphosphorylated tau-induced cell death of the human neuroblastoma cell line SH-SY5Y.

• Journal of Korean Ophthalmic Optics Society
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• v.10 no.2
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• pp.119-126
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• 2005

The purpose of this study was analyzed to compare on the physical characters of two companies of color contact lenses. Artificial tear solution was used for measuring the rate of protein deposits and wettability. The surface roughness of lenses was measured by SEM(scanning electron microscope, Japan) and AFM(atomic force microscope, MultimodeTM, USA). As a results, The color contact lenses was not different from general soft contact lenses in a respect of other properties. However, the colored contact lenses showed a severe crack on the surface under SEM observation. There was no irregularity on the surface of the colored contact lenses in AFM photograph. The dyes were deposited in inside of lenses by microscope observation.

• Clinical and Experimental Reproductive Medicine
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• v.2 no.2
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• pp.41-46
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• 1975

Careful scruting of the data indicate that malnutrition actually limits fertility. Spermatogenesis may likewise be impaired by inadequate diet, particularly one that is very poor in protein. For those who are underweight, increased caloric intake stressing high protein content is recommended. Included are supplementary vitamins, particularly B complex, which stimulate the appetite. Injudicious dieting by the woman to conform to current standards of beauty may also result in malnutrition. This contributes to faulty oogenesis and, in extreme dieting, may produce a long-standing amenorrhea. Obsity may also reduce fertility. Since most cases of obesity are due to over-eating, the full cooperation of the patient must be enlisted. And no device is effective for breaking up fatty deposits. Instead, a program of exercise is recommended. The treatment of both malnutrition and obesity is directed toward general dietary habits either weight gain or weight reduction, with a well balanced high protein diet.

• Journal of Korean Ophthalmic Optics Society
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• v.17 no.2
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• pp.233-239
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• 2012

Purpose: In the study, the change of protein and lipid deposits on soft contact lens by drinking was investigated. Methods: Fifty male subjects wearing soft contact lens were surveyed whether they felt any discomfort induced by drinking or not. Further, 32 male subjects who has no ocular disease drank 190 mL alcohol. The protein and lipid deposits on soft contact lens (etafilcon A material) of subjects were measured after 4 hours later and compared with those of non-drinking subject. Results: When subjects drink alcohol with soft contact lens on, 58% of subjects answered they experienced the change of lens awareness such as stiffness, blurry sight, dryness and so on. The protein deposit on soft contact lens increased an average of $59.3{\mu}g/lens$ by drinking and the case of more than double in protein deposit was reached in 9 eyes. However, the protein deposited on soft contact lens was lysozyme which was unchanged by drinking. The amounts of cholesterol and methyl oleate after drinking were 85.5% (p=0.25) and 52.6% (p=0.002) of non-drinking's indicating some change of lipid deposit on soft contact lens by drinking. Conclusions: The results showed the composition of protein and lipid deposited on soft contact lens was changed due to drinking. Thus, it is suggested that wearing soft contact lens when drinking might be one of the reasons to feel discomfort.

• Journal of Nutrition and Health
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• v.29 no.10
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• pp.1059-1071
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• 1996

This study was performed to investigate the effect of dietary protein level on renal senescence. Male rats of 337.8$\pm$5.7g body weight were underlateral nephrectomy or shamoperation. The rats were divided into high protein(40% casein), normal protein(15% casein) and low protein(8% casein)diets and fed experimental diets ad libitum for 24 weeks. The results are summarized as follows. There was a hypertophy of the remnant kidney of uninephrectomized rats of 40% or 15% protein group, coming up to the comparable weights of both kidneys of sham-operated rats. However, the hypertrophic effect was not seen in uninephrectomized rats of 8% protein group. Serum albumin was lower in uninephrectomized rats. With increasing dietary protein level blood urea nitrogen was increased, whereas, urinary urea nitrogen excretion was decreased. Urinary solute excretion was higher in uninephrectomized group than in sham-operated group. However, effect of dietary protein level on urinary solute excretion varied dpending on th solutes tested. GFR and urinary protein excretion, throughout experiment, increased with feeding period and with dietary protein level. Proteinuria was most severe in uninephrectomized rats fed 40% casein diet. Maximum urine concentration ability measured after dehydration was not different among the experimental groups. Light microscopic examination showed focal segmental glomerulosclerosis and mild increas of glomerular mesangial matrix in uninephrectomized rats fed 40% and 15% protein diet, however, which was not observed in uninephrectomized rats fed 8% protein diet and in sham-operated rats fed 40% diet. Immunofluorescence studies revealed segmental deposits of albumin in the mesangium and capillary loops in high protein and uninephrectomized groups. Minimal granular deposition of IgG was noted in the mesangium of all experimental groups. In conclusion, high protein intake accelerated deterioration of renal function and it was correlated with morphological change. Low protein intake was effective in preventing these changes.

• Applied Microscopy
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• v.29 no.4
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• pp.499-509
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• 1999

Accumulations of the storage proteins in protein storage vacuole and the differentiation of protein bodies from protein-filled ER in developing pea cotyledons have been investigated using conventional and immunoelectron microscopy. To improve the fixation quality, single cells separated enzymatically from sliced cotyledons were used. At early stages of seed development osmiophilic protein accumulates in rER lumen were observed quite often. This protein-filled ER cisternae were differentiated into cytoplasmic protein bodies at late stage by the process called terminal dilations which have been considered a principal route of the formation of cytoplasmic protein bodies somewhat later in seed maturation. Immunocytochemical labellings of the vicilin and legumin show that presence of vicilin on both of the cytoplasmic PB and PD, but limited presence of legumin only on the cytoplasmic PB at intermediate stage of seed development. Immunogold labellings of Bip, ER retention protein, were observed on the inner periphery of protein deposits in protein storage vacuole. This result was regarded that Bip can recognize and retrieve misfolded protein during active accumulation of storage protein to the PD in PSV.

• Applied Microscopy
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• v.31 no.4
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• pp.347-354
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• 2001

Immunoelectron microscopy of storage protein at early stage of seed development showed legumin was firstly accumulated protein in between endoplasmic reticulum (ER) cisternae, and these accumulates were differentiated into protein body (PB) by transformation at later stage. Thin sections of pea cotyledons during the later stages of seed maturation showed three morphologically different types of protein bodies. One of these, presented as rough-surfaced cisternae with terminal dilations, which contained protein deposits and were often found interdigitated between stacks of rough endoplasmic reticulum. Conventional electron microscopy at earlier stages of cotyledon development showed this protein body type initially developed from the rough ER. This transformation of endoplasmic reticulum into a protein body is believed to represent a new pathway of protein body development.

• Applied Microscopy
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• v.31 no.2
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• pp.199-206
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• 2001

In 1980s, the fragmentation or subdivision of protein deposits at the periphery of protein storage vacuole was suggested as the only route of PB development in pea cotyledon cells. Since then, other independant processes such as terminal dilation , transformation and de novo development have been discussed as alternative routes for PB development, and today, these multiple mechanisms of PB development are accepted as a result of active investigations. For analysis of the protein accumulations in the ER cisternae during seed development, immunocytochemical gold labellings were applyed on the single cells separated by enzymatic digestion from cotyledon tissue. Anti-legumin labellings at the early stage, and anti-vicilin labellings at the intermediate stage were observed on the protein-filled ER. The $\alpha-Tip$, which is the ER retention protein, was labelled somewhat at late stage, and PPase, a sort of tonoplast membrane protein, was labelled at early stage.