Lysosomal storage of sulfated glycosaminoglycans in cultured fibroblasts exposed to immunostimulatory acridine derivatives

Handrock, K.; Laschke, A.; Lüllmann-Rauch, R; Vogt, R.D.; Ziegenhagen, Manfred W.

doi:10.1016/0041-008x(92)90070-9

Cited by 10 publications

(1 citation statement)

References 22 publications

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“…On electroretinography, the chloroquine and tilorone retinopathies are characterised by decreasing b-wave and awave amplitudes [4,7,13]. Two other cationic amphiphilic agents, the antiviral and immunomodulatory acridine derivatives, compounds CL-90.100 (3,6-bis[2-(diethylamino) ethoxyl]acridine) and CL-246.738, have been reported to interfere with the lysosmal degradation of sulphated glycosaminoglycans (GAGs), thus inducing mucopolysaccharidosis in visceral organs of rats [2,8,9,11].…”

Section: Introductionmentioning

confidence: 99%

Morphological and functional changes due to drug-induced lysosomal storage of sulphated glycosaminoglycans in the rat retina

Bredehorn

Clausen

Duncker

et al. 2001

Graefe's Arch Clin Exp Ophthalmol

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the glycosaminoglycan storage in pigment epithelium is reminiscent of that seen in some inherited mucopolysaccharidoses of humans. When a given cell type shows lysosomal accumulation of glycosaminoglycans as a consequence of impaired degradation, it can be assumed to be engaged in the turnover of glycosaminoglycans under normal conditions. Thus the present results suggest that not only the retinal pigment epithelium but also Müller cells, photoreceptor cells, and, to variable degree, retinal neurons are normally involved in the catabolism of sulphated glycosaminoglycans. We believe that the lysosomal storage of glycosaminoglycans caused secondary cellular disturbance responsible for the functional changes shown by electroretinography.

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Section: Introductionmentioning

confidence: 99%

Morphological and functional changes due to drug-induced lysosomal storage of sulphated glycosaminoglycans in the rat retina

Bredehorn

Clausen

Duncker

et al. 2001

Graefe's Arch Clin Exp Ophthalmol

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Chemically Induced Accumulation of GAGs Delays PrPSc Clearance but Prolongs Prion Disease Incubation Time

et al. 2008

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Prion diseases are a group of fatal neurodegenerative diseases affecting humans and animals. The only identified component of the infectious prion is PrP(Sc), an aberrantly folded isoform of PrP(C). Glycosaminoglycans, which constitute the main receptor for prions on cells, play a complex role in the pathogenesis of prion diseases. For example, while agents inducing aberrant lysosomal accumulation of GAGs such as Tilorone and Quinacrine significantly reduced PrP(Sc) content in scrapie-infected cells, administration of Quinacrine to prion-infected subjects did not improve their clinical status. In this study, we investigated the association of PrP(Sc )with cells cultured with Tilorone. We found that while the initial incorporation of PrP(Sc) was similar in the treated and untreated cells, clearance of PrP(Sc) from the Tilorone-treated cells was significantly impaired. Interestingly, prolonged administration of Tilorone to mice prior to prion infection resulted in a significant delay in disease onset, concomitantly with in vivo accumulation of lysosomal GAGs. We hypothesize that GAGs may complex with newly incorporated PrP(Sc) in lysosomes and further stabilize the prion protein conformation. Over-stabilized PrP(Sc) molecules have been shown to comprise reduced converting activity.

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Tilorone-induced lysosomal storage of sulphated glycosaminoglycans can be separated from tilorone-induced enhancement of lysosomal enzyme secretion

Lüllmann‐Rauch

Pods

Witzendorff

1995

Biochemical Pharmacology

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Lysosomal storage of sulfated glycosaminoglycans in cultured fibroblasts exposed to immunostimulatory acridine derivatives

Cited by 10 publications

References 22 publications

Morphological and functional changes due to drug-induced lysosomal storage of sulphated glycosaminoglycans in the rat retina

Morphological and functional changes due to drug-induced lysosomal storage of sulphated glycosaminoglycans in the rat retina

Chemically Induced Accumulation of GAGs Delays PrPSc Clearance but Prolongs Prion Disease Incubation Time

Tilorone-induced lysosomal storage of sulphated glycosaminoglycans can be separated from tilorone-induced enhancement of lysosomal enzyme secretion

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